| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.58528317 |
| The latter is similar in size to plasma HDL3a , LpA 1 particles , suggesting that extracellularly assembled apoA 1 lipid complexes can directly give rise to a major plasma LpA 1 subpopulation upon interaction with LCAT . 0.58528317^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.52236788 |
| The ability of LCAT to interact with lipid poor apoA 1 suggests that LCAT does not need to bind to the lipid interface on an HDL particle but that LCAT may directly interact with apoA 1 . 0.52236788^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Various combinations of incorporation and addition of apolipoprotein A 1 ( apo A 1 ) and apolipoprotein A 2 ( apo A 2 ) individually or together to a defined lecithin cholesterol ( 250 / 12 . 5 molar ratio ) liposome prepared by the cholate dialysis procedure were used to study the effect of apo A 2 on lecithin : cholesterol acyltransferase ( LCAT , EC 2 . 3 . 1 . 43 ) activity of both purified enzyme preparations and plasma . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Statistically significant increases in lecithin cholesterol acyltransferase ( EC 2 . 3 . 1 . 43 ; LCAT ) , HDL cholesterol and apolipoprotein AI were also observed after Mg supplementation . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| A specific cofactor protein for lecithin cholesterol acyltransferase , apoA 1 , also enhanced both activities . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Altered epitope expression of human interstitial fluid apolipoprotein A 1 reduces its ability to activate lecithin cholesterol acyl transferase . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Interaction of rat lecithin cholesterol acyltransferase with rat apolipoprotein A 1 and with lecithin cholesterol vesicles . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Apo AI activates the lecithin cholesterol acyltransferase within the HDL particle and functions as ligand for a putative HDL receptor two properties , which render this apolipoprotein a key mediator in reversed cholesterol transport . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Non cholesterol sterols , absorption and synthesis of cholesterol and apolipoprotein A 1 kinetics in a Finnish lecithin cholesterol acyltransferase deficient family . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| The apoA 1 form isolated from the culture medium of C 127 cells was analyzed for its ability to activate lecithin cholesterol acyltransferase ( LCAT ) and to bind to phospholipid vesicles and high density lipoprotein ( HDL ) . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Localization of an apolipoprotein A 1 epitope critical for activation of lecithin cholesterol acyltransferase . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Apolipoprotein AI ( apo AI ) of human serum high density lipoprotein functions as an activator of lecithin cholesterol acyltransferase ( LCAT ) and therefore plays an important role in reversed cholesterol transport . ^^^ Apolipoprotein AI ( apo AI ) of human serum high density lipoprotein functions as an activator of lecithin cholesterol acyltransferase ( LCAT ) and therefore plays an important role in reversed cholesterol transport . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| This mutant apolipoprotein A 1 has much the same potential as to activate lecithin cholesterol acyltransferase . . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| To elucidate further the conformation of human apolipoprotein A 1 ( apoA 1 ) in lipid bound states and its effect on the reaction with lecithin cholesterol acyltransferase ( LCAT ) , we prepared reconstituted HDL ( rHDL ) particles from a reaction mixture containing dipalmitoylphosphatidylcholine / cholesterol / apoA 1 in the molar ratios of 150 : 7 . 5 : 1 . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| We prepared a spherical reconstituted high density lipoprotein ( rHDL ) particle in pure form and compared it with its homogeneous discoidal rHDL precursors , in terms of the structure and stability of the apolipoprotein A 1 ( apoA 1 ) component , the dynamics of the surface lipids , and the relative reactivity with lecithin cholesterol acyltransferase . ^^^ The reactivity with lecithin cholesterol acyltransferase was highest for the 96 A rHDL disc , and 16 and 34 fold lower for the 78 A rHDL disc and the 93 A rHDL sphere , respectively , possibly as a result of differences in apoA 1 structure and product inhibition in these particles . . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| The concentration of apolipoprotein A 1 increased slightly during pindolol therapy . beta Blockers with the exception of pindolol decrease the concentration of serum free fatty acids . beta blocker therapy has little influence on the adipose tissue lipoprotein lipase activity , but lecithin cholesterol acyltransferase activity may increase during pindolol therapy . . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Fasting blood samples were obtained from subjects at the beginning , and following one year of treatment , for plasma lipids , apolipoproteins AI ( apo AI ) and B ( apo B ) , and lecithin cholesterol acyltransferase ( LCAT ) activity . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| At 6 , 12 , 24 , and 48 h the cells were harvested , and the culture medium collected at each time point was assayed for lecithin cholesterol acyltransferase mass and activity , cholesterol esterification rate , and apolipoprotein A 1 mass . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Anion effects on the reaction of lecithin cholesterol acyltransferase with discoidal complexes of phosphatidylcholines . apolipoprotein A 1 . cholesterol . ^^^ Discoidal complexes of phosphatidylcholine ( PC ) . apolipoprotein A 1 . cholesterol were prepared with egg PC , palmitoyloleoylPC , dipalmitoylPC , or dimyristoylPC , and were used as substrates of purified lecithin cholesterol acyltransferase to investigate the effects of neutral salts on the enzymatic reaction . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Reaction of discoidal complexes of apolipoprotein A 1 and various phosphatidylcholines with lecithin cholesterol acyltransferase . ^^^ Complexes of phospholipids apolipoprotein A 1 cholesterol , containing various bulk phosphatidylcholines or a matrix of the ether analog of 1 palmitoyl 2 oleoyl phosphatidylcholine including test phosphatidylcholines were used as substrates for human lecithin cholesterol acyltransferase . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Transformation of large discoidal complexes of apolipoprotein A 1 and phosphatidylcholine by lecithin cholesterol acyltransferase . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| This could reflect the role of apo AI in the transformation of nascent HDL C particles into mature ones via its cofactor activity to lecithin cholesterol acyltransferase . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Low levels of apolipoprotein A 1 are not contributors to the low lecithin cholesterol acyl transferase activity in premature newborn infants . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| In comparison with healthy controls , patients with end stage liver disease had significantly decreased concentrations of lecithin cholesterol acyltransferase mass , apolipoprotein A 1 , total phospholipids , and both total and esterified cholesterol . ^^^ By the third month after hepatic replacement , the plasma concentrations of total cholesterol , phospholipids , lecithin cholesterol acyltransferase , and apolipoprotein A 1 were comparable to those of the healthy subjects . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Apolipoprotein AI activates the lecithin cholesterol acyltransferase , apolipoprotein CII and CIII regulate the lipoprotein lipase , and apolipoprotein B 100 , B 48 , and E control the cholesterol uptake into hepatic and extrahepatic cells . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| All purified lecithin cholesterol acyltransferase species were activated by human apolipoprotein A 1 and were similarly inhibited by p hydroxymercuribenzoate and phenylmethylsulfonyl fluoride . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Discoidal substrates for purified human lecithin cholesterol acyltransferase were prepared with human apolipoprotein A 1 , cholesterol , and egg phosphatidylcholine ( PC ) or dipalmitoyl PC , including dihexadecyl PC in various proportions as an enzymatically inert dilutor of the interfacial PC substrate . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Interspecies activation of lecithin cholesterol acyltransferase by apolipoprotein A 1 isolated from the plasma of humans , horses , sheep , goats and rabbits . ^^^ The abilities of apolipoprotein A 1 species isolated from humans , horses , sheep , goats and rabbits to activate purified human lecithin cholesterol acyltransferase and the enzyme from homologous plasmas and plasma of other mammalian species were compared . ^^^ All apolipoprotein A 1 species tested had the ability , but with different effectiveness , to activate plasma lecithin cholesterol acyltransferase from their own and other animal species and from purified human lecithin cholesterol acyltransferase . ^^^ Horse apolipoprotein A 1 was nearly as effective as human apolipoprotein A 1 , whereas apolipoproteins A 1 from goats , sheep or rabbits were , in descending order , slightly less effective than either horse or human apolipoprotein A 1 in activating human plasma lecithin cholesterol acyltransferase . ^^^ A similar trend in ability to activate purified human lecithin cholesterol acyltransferase by these apolipoprotein A 1 species was seen , but apolipoprotein A 1 from sheep , goats and rabbits was only about 55 65 % as effective as human apolipoprotein A 1 . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Apolipoprotein A 1 , the major protein in mammalian high density lipoprotein , acts as a cofactor for lecithin cholesterol acyltransferase during the formation of cholesterol ester and as such , is thought to promote cholesterol efflux from peripheral cells to the liver . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Reaction of human lecithin cholesterol acyltransferase with synthetic micellar complexes of apolipoprotein A 1 , phosphatidylcholine , and cholesterol . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| The in vitro conversion of biotin pre beta 1 LpA 1 was investigated in the presence of plasmas of healthy probands and patients with Tangier disease , with apoA 1 deficiency , and with lecithin cholesterol acyltransferase ( LCAT ) deficiency . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| The isolated apoAI ( 1 192 ) rHDLs retained a high ability to activate lecithin cholesterol acyltransferase , comparable with the most effective apoAI rHDL . ^^^ The results suggest that the C terminal domain of apoAI is crucial for self association and initial lipid binding but is not involved in specific lecithin cholesterol acyltransferase activation . . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| In the present study , lecithin cholesterol acyltransferase ( LCAT ) catalyzed esterification of oxysterols was investigated by using discoidal bilayer particles ( DBP ) containing various oxysterols , phosphatidylcholines , and apolipoprotein A 1 . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| The synthetic lipid associating peptide , LAP 20 ( VSSLLSSLKEYWSSLKESFS ) , activates lecithin cholesterol acyltransferase ( LCAT ) despite its lack of sequence homology to apolipoprotein A 1 , the primary in vivo activator of LCAT . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Cholesterol efflux , lecithin cholesterol acyltransferase activity , and pre beta particle formation by serum from human apolipoprotein A 1 and apolipoprotein A I / apolipoprotein A 2 transgenic mice consistent with the latter being less effective for reverse cholesterol transport . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| To assess the effect of this structural modification on a major function of the apolipoprotein , its activation of lecithin cholesterol acyltransferase ( LCAT ) , we prepared well defined complexes of A IM / A IM and apoA 1 with phospholipids and cholesterol and compared their reactivities with LCAT . ^^^ Activation of lecithin cholesterol acyltransferase by a disulfide linked apolipoprotein A 1 dimer . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Acylation of 3beta ( 2 hydroxyethoxy ) cholest 5 ene in the presence of lecithin : cholesterol acyltransferase from blood plasma ] . 3 beta ( 2 Hydroxyethoxy ) cholest 5 ene in the composition of the micellar complexes with apolipoprotein A 1 and palmitoyloleoylphosphatidylcholine was acylated in the presence of lecithin cholesterol acyltransferase from human plasma . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| First , the reverse cholesterol transport pathway including the roles of nascent ( pre beta ) HDL , apolipoprotein A 1 , lecithin cholesterol acyltransferase ( LCAT ) , cholesteryl ester transport protein , and hepatic uptake of cholesteryl ester from HDL by liver is better understood . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Plasma apolipoprotein AI ( apoAI ) and lecithin cholesterol acyltransferase ( LCAT ) play important roles in reverse cholesterol transport , promoting the removal of excess cholesterol from peripheral cells and reducing formation of atherosclerotic lesions . ^^^ Efficient coexpression and secretion of anti atherogenic human apolipoprotein AI and lecithin cholesterol acyltransferase by cultured muscle cells using adeno associated virus plasmid vectors . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| A series of mutant apolipoprotein ( apoA 1 ) constructs were designed and then expressed in cell culture to identify structural domains within the mature native apoA 1 protein that participate in the activation of the plasma enzyme , lecithin cholesterol acyltransferase ( LCAT ) . ^^^ Apolipoprotein A 1 domains involved in lecithin cholesterol acyltransferase activation . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Four isoforms of human apolipoprotein A 1 ( apo A 1 ) : the normal allele product and the corresponding Lys 107 deletion mutant , and apo A 1 with sulfoxidized Met 112 and Met 148 residues and the corresponding reduced form , were investigated in their lipid binding properties , structures , and abilities to activate lecithin cholesterol acyltransferase . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Since apolipoprotein A 1 is the presumed primary physiological activator of lecithin cholesterol acyltransferase , the distribution of the enzyme among A 1 containing lipoprotein particles and A 1 free plasma in normolipidemic and dyslipidemic subjects was examined . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| In sharp contrast , prolonged degradation of HDL ( 3 ) by chymase failed to reduce the ability of HDL ( 3 ) to activate LCAT , even though it led to modification of three epitopes in the central region of apoA 1 that are involved in lecithin cholesterol acyltransferase ( LCAT ) activation . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Furthermore , the rHDL particles containing the V156E mutant did not rearrange to smaller particles in the presence of low density lipoproteins , and had minimal reactivity with lecithin cholesterol acyltransferase ( LCAT ) , compared with rHDL particles made with control apoA 1 . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Structural differences exist between human and mouse A apoproteins because : 1 ) human cholesterol ester transfer protein , lecithin cholesterol acyl transferase and phospholipid transfer protein interact better with human apoA 1 ; 2 ) human apoA 1 and A 2 , alone or in combination , form polydisperse instead of monodisperse HDL particles . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| The function of apoA 1 and its interaction with other components of HDL , including lecithin cholesterol acyltransferase , seems to be closely linked to its structural plasticity . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Human apoA 1 self associates more and activates human lecithin cholesterol acyltransferase better than mouse apoA 1 . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Expression of lecithin cholesterol acyltransferase and / or apoA 1 mediated by recombinant adeno associated virus in myogenic cells ] . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| In contrast , apolipoprotein A 1 ( apoA 1 ) represents the primary protein content of the high density lipoprotein ( HDL ) particles , which interacts with the putative HDL receptor , and stimulates the enzymatic reaction of lecithin cholesterol acyltransferase ( LCAT ) resulting in esterified cholesterol , which is the essential step in the process of reverse cholesterol transport . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Construction and characterization of polycistronic retrovirus vectors for sustained and high level co expression of apolipoprotein A 1 and lecithin cholesterol acyltransferase . ^^^ Apolipoprotein A 1 ( apo A 1 ) and lecithin cholesterol acyltransferase ( LCAT ) are constituents of circulating high density lipoprotein ( HDL ) particles and play an important role in ' reverse cholesterol transport ' , the process by which cholesterol in peripheral tissues is transferred to the liver for excretion . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Additional implicated loci include lipoprotein lipase , apolipoprotein CII , cholesteryl ester transfer protein , apolipoprotein AI , and lecithin cholesterol acyl transferase . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| However , the fraction of ionized magnesium was significantly correlated with HDL cholesterol ( n = 46 , r = 0 . 31 , p = 0 . 0345 ) , apolipoprotein A 1 ( n = 41 , r = 0 . 39 , p = 0 . 0124 ) , and lecithin cholesterol acyltransferase ( LCAT ) ( n = 20 , r = 52 , p = 0 . 0184 ) . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Distinct central amphipathic alpha helices in apolipoprotein A 1 contribute to the in vivo maturation of high density lipoprotein by either activating lecithin cholesterol acyltransferase or binding lipids . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Compared with LA apoA I+ / + mice , serum from LA apoA 1 / mice had a significantly reduced capacity to function as an acceptor of ABCA 1 and SR BI mediated cellular cholesterol efflux , and also had markedly reduced lecithin cholesterol acyltransferase activity . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| The data analyzed include LCAT ( lecithin cholesterol acyl transferase ) concentrations in solution to egg white apoA 1 rHDL immobilized on a biosensor chip surface ( 1 ) , native , mildly oxidized , and strongly oxidized LDL in solution to a heparin modified Au surface of a surface plasmon resonance ( SPR ) biosensor ( 2 ) , and TRITC labeled HDL in solution to a bare optical fiber surface ( 3 ) . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Despite progress in molecular characterization , specific diagnoses of disorders belonging to a group of inherited hypoalphalipoproteinemias , i . e . , apolipoprotein AI deficiency , lecithin cholesterol acyltransferase deficiency , Tangier disease ( TD ) , and familial high density lipoprotein ( HDL ) deficiency , remain difficult on a purely clinical basis . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| The effects of common variants of cholesteryl ester transfer protein ( CETP ) ( TaqIB ) , hepatic lipase ( HL ) ( 514C > T ) , lipoprotein lipase ( LPL ) ( S447X ) and lecithin cholesterol acyl transferase ( LCAT ) ( S208T ) on the determination of high density lipoprotein cholesterol ( HDL C ) and apolipoprotein AI ( apoAI ) levels were examined in 2773 healthy middle aged men participating in the second Northwick Park Heart Study . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Enhancement of scavenger receptor class B type 1 mediated selective cholesteryl ester uptake from apoA 1 ( / ) high density lipoprotein ( HDL ) by apolipoprotein A 1 requires HDL reorganization by lecithin cholesterol acyltransferase . ^^^ Lecithin cholesterol acyltransferase treatment alone or addition of apoA 1 to apoA 1 ( / ) HDL alone also had little effect . ^^^ However , addition of apoA 1 to apoA 1 ( / ) HDL in the presence of lecithin cholesterol acyltransferase reorganized the large heterogeneous apoA 1 ( / ) HDL to a more discrete particle with enhanced CE selective uptake activity . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| The ABCA 1 transporter regulates intracellular cholesterol levels in the liver and in peripheral cells by effluxing excess cholesterol to lipid poor apoA 1 to form nascent HDL , which is converted to mature alpha HDL by esterification of cholesterol to cholesteryl esters ( CE ) by lecithin cholesterol acyltransferase . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| These observations prompted an investigation to determine if charged residues in helix 6 maintain a structural conformation for protein protein interaction with lecithin cholesterol acyltransferase ( LCAT ) the enzyme for which apoA 1 acts as a cofactor . ^^^ Apolipoprotein A 1 helix 6 negatively charged residues attenuate lecithin cholesterol acyltransferase ( LCAT ) reactivity . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Apolipoprotein A 1 [ ApoA 1 ] activates the enzyme Lecithin Cholesterol Acyl Transferase to esterify cell cholesterol for transport to liver . ^^^ Apolipoprotein A 1 [ ApoA 1 ] activates the enzyme Lecithin Cholesterol Acyl Transferase to esterify cell cholesterol for transport to liver . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| These isopeptides were isolated from subjects homozygous for one of the isoforms , incorporated into phospholipid / cholesterol / [ 14C ] cholesterol complexes by the cholate dialysis procedure and used to measure capacity to activate phosphatidylcholine sterol acyltransferase in comparison to apolipoprotein A 1 lipid substrate particles prepared by the same procedure . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Two of the four peptides obtained by cyanogen bromide cleavage of apoA 1 retained some ability to activate LCAT . ^^^ ApoC and apoA 2 were both found to inhibit the activation of LCAT by apoA 1 . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Lecithin : cholesterol acyltransferase ( LCAT ) was more highly activated by apolipoprotein A 1 ( apoA 1 ) with dimyristoyl phosphatidylcholine ( DMPC ) than with dilinoleoyl phosphatidylcholine ( DLPC ) when lipid dispersion of cholesterol and each phosphatidylcholine was used as a substrate . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| A role of ApoA 1 in LCAT reaction . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| The recombinant particles ( PC : cholesterol : apoA 1 molar ratio = 42 : 1 . 9 : 1 ) exhibited the following order of reactivity towards purified human LCAT in vitro : POPC greater than PLPC greater than PEPC = PAPC greater than PDPC . ^^^ There was a linear decrease in CE formation when the percentage of PEPC or PDPC was increased from 0 to 100 % relative to POPC in recombinant particles with a constant PC : cholesterol : apoA 1 molar ratio , suggesting that the PEPC and PDPC were competitive inhibitors of the LCAT reaction . ( ABSTRACT TRUNCATED AT 250 WORDS ) . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| This shift in apoA 1 mass to alpha electrophoretic mobility was blocked by the addition of either 1 . 4 mM DTNB or 10 mM menthol to the plasma prior to incubation , suggesting that lecithin : cholesterol acyltransferase ( LCAT ) activity was involved . ^^^ Based on these findings , we propose a cyclical model in which 1 ) apoA 1 mass moves from pre beta HDL to alpha HDL in connection with the action of LCAT and the generation of cholesteryl esters within the HDL , and 2 ) apoA 1 moves from alpha HDL to pre beta HDL in connection with the action of CETP and the movement of cholesteryl esters out of the HDL . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Finally , comparison of sequence homology between bovine apoA 1 and the lecithin : cholesterol acyl transferase ( LCAT ) activating region of human apoC 1 suggests that several LCAT activating domains may be present in calf apoA I . . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Plasma LCAT activity , concentrations of HDL 3 apoAI and apoAII in plasma and lipoprotein fractions were normal in both the diabetic groups . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| The observation of an abnormal immunoblot banding pattern of apolipoprotein A 1 ( apo A 1 ) and of reduced lecithin : cholesterol acyltransferase ( LCAT ) activity in plasma led to sequence analysis of the genes for apo A 1 and LCAT in this patient and his family . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| We hypothesize that the HDL subpopulations rich in apoA 1 promote cholesterol removal predominantly via the interaction with HDL receptors , while apoA 4 rich HDL particles receive their driving force for cholesterol efflux from the concomitant action of LCAT via a predominantly nonspecific interaction of the particles with the cell surface . ( ABSTRACT TRUNCATED AT 400 WORDS ) . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| There are five major classes of apo Lp known : Apo AI , the main component of HDL not only mediates the action of LCAT , a key enzyme in cholesterol metabolism , but also through specific cell receptors is responsible for the reverse cholesterol transport , which is discussed as the main atherogenic process . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| The baseline data and the one year change data showed consistent positive correlations between LCAT concentrations and total cholesterol , low density lipoprotein cholesterol , very low density lipoprotein cholesterol , and apolipoprotein B concentrations , and consistently weak correlations between LCAT concentrations and high density lipoprotein ( HDL ) cholesterol , HDL 2 , and apolipoprotein A 1 concentrations . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| It is likely that 4 fat improves the nutritional status of premature infants , thereby stimulating increased liver synthesis of important proteins , including apoAI and LCAT , associated with HDL metabolism . . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| The apparent secretion rates of apoA 1 , A 2 , E , D , A 4 , and lecithin : cholesterol acyltransferase ( LCAT ) were 4013 + / 1368 , 851 + / 217 , 414 + / 64 , 171 + / 51 , 32 + / 14 , and 2 . 9 + / 0 . 7 ng / mg cell protein per 24 h , respectively ( n = 3 5 ) . ^^^ The majority of HepG 2 apoA 4 ( 78 + / 4 % ) ( n = 3 ) and LCAT ( 85 + / 6 % ) ( n = 3 ) was not associated with either apoA 1 or A 2 . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Apolipoprotein A 1 was required to transform artificial lecithin cholesterol liposomes into substrates for the purified LCAT . . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| The apoA 1 samples were reconstituted with palmitoyloleoyl phosphatidylcholine ( POPC ) or dipalmitoyl phosphatidylcholine ( DPPC ) , and small amounts of cholesterol , into discoidal high density lipoprotein ( HDL ) complexes in order to examine their lipid binding and structural properties as well as their ability to activate lecithin : cholesterol acyltransferase ( LCAT ) . ^^^ The kinetic experiments with LCAT indicated that the apoA 1 variants , Lys 107 0 and Pro 165 Arg , in rHDL particles had statistically different ( 30 to 90 % ) kinetic constants from the corresponding normal allele products ; however , the variability in the kinetic constants among the normal apoA 1 products was even greater ( 40 to 430 % ) . ^^^ Therefore , we conclude that the effects of these six mutations in apoA 1 on the activation of LCAT are minor , and that the structural effects on rHDL , and possibly native HDL , are insignificant with the exception of the Lys 107 0 mutation . . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| We conclude that the galactosamine treatment induces a complex mixture of HDL that bears strong similarities to the small , apoA 1 rich and large , apoE rich particles seen in LCAT deficiency or secreted by hepatic cells in culture . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| In addition , lecithin : cholesterol acyltransferase ( LCAT ) activity was measured and correlated with plasma apolipoprotein A 1 concentration and particle size distribution . ^^^ LCAT activity was diminished in all subjects to 8 54 % of normal , and was strongly positively correlated ( r = 0 . 91 P less than 0 . 05 ) with plasma apolipoprotein A 1 levels . . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| It was demonstrated previously that LDL can serve as substrate for LCAT , probably because they contain sufficient amounts of apoA 1 and other non apoB proteins , known as LCAT activators . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| The HDL particles isolated from monkey liver perfusate stored at 4 degrees C and not exposed to added LCAT contained apoA 1 and apoE , were deficient in neutral lipids , and were observed by electron microscopy as discoidal particles . ^^^ However , HDL subfractions derived from incubations at 37 degrees C with active LCAT contained apoA 1 as the major apoprotein , appeared round by electron microscopy , and possessed chemical compositions similar to plasma HDL . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| When serum was used as an enzyme source , addition of purified apolipoprotein A 1 , which is known to be an endogenous activator of LCAT , to the assay mixture resulted in a slight decrease in enzyme activity . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| The activity of LCAT in the perfusate was dependent on the presence of the major protein of the high density lipoprotein class , apoA 1 . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Apolipoproteins of LCAT modified LDL exhibited a 10 fold increase of apo AI , a 4 5 fold increase of apo E , and a 2 fold increase of apo C . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Using apoA 1 and small liposomes as a substrate , the addition of apoC 2 up to 4 micrograms / ml had no effect on the LCAT reaction , but above this concentration LCAT was inhibited . ^^^ Small liposomes with phosphatidylcholine / cholesterol molar ratios of 3 : 1 up to 8 . 4 : 1 did not show any significant differences in the LCAT reaction , when used as substrates in the presence of various amounts of apoA 1 and albumin . ^^^ Pig and human LCAT were activated to the same extent by either human or pig apolipoprotein A 1 ( apo A 1 ) using small liposomes as substrate . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| The apolipoprotein A 1 ( apo A 1 ) from the patients with familial lecithin : cholesterol acyltransferase ( LCAT ) deficiency has been characterized . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| The lecithin : cholesterol acyltransferase ( LCAT ) induced transformation of two discrete species of model complexes that differ in number of apolipoprotein A 1 ( apoA 1 ) molecules per particle was investigated . ^^^ Transformation of 3A 1 ( UC ) complexes by partially purified LCAT yielded a product ( 24 hr , 37 degrees C ) with a cholesteryl ester ( CE ) core , 3 apoA 1 , and a mean diameter of 9 . 2 nm . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Apolipoprotein A 1 was the most potent LCAT activator in our system followed by apolipoproteins C 1 and D . ^^^ Neither apolipoprotein A 1 nor C 1 containing proteoliposomes gave linear reaction kinetics with LCAT . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Ultracentrifugally isolated HDL subclasses ; concentrations of apoA 1 , apoA 2 , LpA 1 and LpA 1 : A 2 particles ; post heparin plasma lipoprotein lipase ( LPL ) , hepatic lipase ( HL ) and plasma cholesteryl ester transfer protein ( CETP ) activities ; phospholipid transfer protein ( PLTP ) and lecithine cholesteryl acyltransferase ( LCAT ) activities were measured in plasma from six patients from both groups . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| The in vivo substrate specificity of Hu LCAT was assessed by creating animals expressing Hu apo AI + Hu LCAT ( HuAI / LCAT ) , Hu apo AI + Hu apo AII + Hu LCAT ( HuAI / AII / LCAT ) , and Hu apo AII + Hu LCAT ( HuAII / LCAT ) . ^^^ The increase in LCAT activity in the HuAI / LCAT and HuAI / AII / LCAT mice was associated with 62 and 27 % reductions respectively , in the proportion of Hu apo AI in the pre beta HDL fraction , when compared with HuAI and HuAI / AII transgenic mice . ^^^ These data demonstrate that moderate increases in LCAT activity are associated with significant changes in lipoprotein cholesterol levels and that Hu LCAT has a significant preference for HDL containing Hu apo AI . . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| The ability of isolated variant apoA 1 to serve as a cofactor for LCAT in vitro did not differ from that of normal apoA 1 . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| The reaction of highly purified lecithin : cholesterol acyltransferase ( LCAT ) with defined reconstituted discoidal apoA 1 containing lipoproteins ( LpA 1 ) with 2 , 3 , or 4 apoA 1 molecules / particle ( Lp 2 , 3 , or 4A 1 ) has been studied in the presence of a number of specific anti apoA 1 antibodies . ^^^ Among nine anti apoA 1 monoclonal antibodies ( mAbs ) reacting with epitopes distributed over 80 % of the sequence , three significantly inhibit the LCAT reaction with all particles . ^^^ The intercalation of epitopes for mAbs that inhibit or enhance LCAT reaction with small LpA 1 is compatible not with steric hindrance but with conformational modifications of apoA 1 and indirectly of the lipids in small particles . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| In nephrotic VLDL , apo AI was distinctly increased at the expense of a decrease in apo CII , and increased LCAT was explained by the relative rise of apo AI in nephrotic VLDL . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| The two subjects with LCAT deficiency had no detectable LCAT mass ( below 0 . 1 microgram / ml ) or LCAT activity ( below 0 . 76 nmol / h / ml ) , apolipoprotein A 1 and D levels approximately 50 % of normal , and apolipoproteins B and A 2 levels only 30 35 % of normal . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| The LCAT preparation was pure according to alkaline polyacrylamide and SDS polyacrylamide gel electrophoresis and did not react against antisera to apo AI , AII , and D . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| However , all forms of LpA 1 are absent in apoA 1 deficient plasma , pre beta 3 LpA 1 and alpha LpA 1 from the plasma of patients with Tangier disease ( TD ) , and pre beta 3 LpA 1 and large alpha LpA 1 from the plasma of patients with lecithin : cholesterol acyltransferase ( LCAT ) deficiency and fish eye disease ( FED ) . ^^^ After a 1 minute pulse with labeled fibroblasts , efflux of [ 3H ] UC into HDL deficient plasmas decreased , compared with normal plasma , by 49 % ( apoA 1 deficiency ) , 36 % ( TD ) , 21 % ( LCAT deficiency ) , and 28 % ( FED ) . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| We studied the effect of plasma apoA 1 concentration on LCAT activation , using normal , heterozygous or homozygous apoA 1 deficient mice made by gene targeting . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| It could , however , be explained by glycation of lysine residues in apolipoprotein A 1 , which is the most potent activator of LCAT . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Cholesterol esterifying activity was identified in feline plasma and was typical of LCAT , in that it was dependent on apolipoprotein A 1 as a cofactor . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Cholesterol was esterified by LCAT in such particles generated with human apoA 1 , but not in those with apoA 2 . ^^^ The reactivity of the apoA 1 pre beta HDL particles with LCAT was in the same order as that in human plasma HDL and in phosphatidylcholine / cholesterol unilamellar vesicles activated by apoA 1 when compared on the rate of percent cholesterol esterification . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| The effects of treatment on lecithin : cholesterol acyltransferase ( LCAT ) catalytic activity and mRNA level as well as on the apolipoprotein A 1 ( apo A 1 ) mRNA level were determined . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| It has been suggested that a normal gastrointestinal function might be necessary to induce a postnatal increase of LCAT activity because apoproteins A 1 and A 4 ( apoA 1 and apoA 4 ) synthesized in considerable amounts in the intestine are known activators of LCAT . ^^^ The plasma LCAT activity , plasma levels of apoA 1 and apoA 4 , plasma cholesteryl esters , and plasma fatty acid composition of cholesteryl esters and phospholipids were then determined . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Lecithin : cholesterol acyltransferase ( LCAT ) is a serine protease type enzyme that esterifies cholesterol in human plasma and is activated by apolipoprotein A 1 in high density lipoproteins . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| To elucidate the molecular events involved , the relationship between LCAT activation and apolipoprotein ( apo ) A 1 charge and structure in high density lipoproteins ( HDL ) has been studied in both native HDL and homogeneous recombinant HDL ( Lp2A 1 ) particles containing apoA 1 , palmitoyloleoyl phosphatidylcholine and cholesterol . ^^^ Increasing the cholesterol content of the different HDL particles progressively increases the particle net negative charge , and these changes in apoA 1 charge are strongly correlated with both the Vmax and apparent Km values for LCAT . ^^^ This suggests that the conformation and charge of apoA 1 play a central role in LCAT activation and that these parameters are influenced by the amount of cholesterol in the surface of HDL particles . . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| For these analyses we cloned partial rabbit cDNAs for apolipoprotein A 1 ( apoA 1 ) , apolipoprotein B ( apoB ) , apolipoprotein E ( apoE ) , cholesteryl ester transfer protein ( CETP ) , hepatic lipase ( HL ) , lipoprotein lipase ( LPL ) , HMG CoA reductase , LDL receptor , 7 alpha hydroxylase , albumin , bile salt dependent cholesteryl ester hydrolase ( CEH ) , lecithin : cholesterol acyl transferase ( LCAT ) , and plasminogen activator inhibitor protein 1 ( PAI 1 ) . ^^^ Messenger RNA levels in isolated liver cell populations normalized to total RNA revealed a cell segregation pattern for hepatic gene expression : parenchymal cells showed higher levels of apoA 1 , apoB , apoE , albumin , LCAT , HL , and 7 alpha hydroxylase mRNAs compared to nonparenchymal cells while nonparenchymal cells showed higher levels of CETP , LDL receptor , HMG CoA reductase , and PAI 1 mRNAs compared to parenchymal cells . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| We investigated the metabolism of the HDL apolipoproteins ( apo ) apoA 1 and apoA 2 in a total of five patients with LCAT deficiency , one with classic LCAT deficiency and four with Fish eye disease . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| The rLCAT was activated by apolipoprotein A 1 and had an average specific activity that was similar to purified plasma LCAT . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Thus , apoB may activate LCAT in a very different manner from apoA 1 . ^^^ Unlike the apolipoprotein A 1 activated reaction , cholesterol was esterified only slightly by the LCAT reaction on low density lipoprotein and , consequently , did not compete against lysophosphatidylcholine for generation of phosphatidylcholine . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Furthermore , at a concentration of nonparenchymal cell conditioned media that inhibited apoA 1 mRNA levels by > 80 % compared to control , there were only slight changes in apoB , apoE , LDL receptor , LCAT , 7 alpha hydroxylase , hepatic lipase , HMG CoA reductase , and albumin mRNA levels . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| We characterized the two species of lipoproteins containing apolipoprotein A 1 ( apoA 1 ) , one containing only apoA 1 ( LpA 1 ) and the other containing apoA 1 and apoA 2 ( LpA I / A 2 ) , in four homozygotes for familial lecithin : cholesterol acyltransferase ( LCAT ) deficiency . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| LCAT activity increased significantly ( P < 0 . 05 ) with improved metabolic control in the diabetic patients , and showed positive within person correlation with HDL 2 cholesterol ester ( r = 0 . 67 ; P < 0 . 01 ) , HDL 2 free cholesterol ( r = 0 . 67 ; P < 0 . 01 ) , phosphatidylcholine ( r = 0 . 49 ; P < 0 . 05 ) , total phospholipids ( r = 0 . 50 ; P < 0 . 01 ) and apolipoprotein A 1 ( apo A 1 : r = 0 . 72 ; P < 0 . 01 ) . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| High density lipoproteins ( fraction 1 to 6 ) are separated into three major subpopulations , the fast migrating high density lipoprotein ( HDL ) subpopulation , containing mainly apo AI and phosphatidylcholine , the subpopulation with intermediate mobility , consisting of particles rich in apo AII , apo E , and C apolipoproteins , and the slowly migrating HDL subfraction , containing mainly particles rich in apo AI , apo AIV , and lecithin : cholesterol acyltransferase ( LCAT ) activity . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| ApoA 1 , apoA 2 , apoA 4 , apoB , apoC 3 , apoD , apoE , apoH , lecithin : cholesterol acyltransferase ( LCAT ) , cholesteryl ester transfer ( CET ) protein , proline rich protein , and a protein of Mr 59 , 000 were detected in the A IVLp . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| In HepG 2 conditioned medium ( CM ) , 60 70 % of apoA 1 is in the d > 1 . 235 g / ml fraction ( lipid poor apoA 1 ) ; hence we investigated whether inclusion of d > 1 . 235 g / ml fraction in LCAT incubations altered HDL subpopulations . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Apolipoprotein A 1 dependent lecithin : cholesterol acyl transferase ( LCAT ) activity was identified in equine lipoprotein deficient plasma ( LPDP ) . 2 . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| We investigated the effects of a polymorphic PvuII site in the gene for lecithin : cholesterol acyltransferase ( LCAT ) on serum high density lipoprotein cholesterol ( HDL C ) and apolipoprotein A 1 ( apo A 1 ) concentrations in a population of 750 pedigreed baboons . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| To investigate whether a direct protein protein interaction between apoA 1 and lecithin : cholesterol acyltransferase ( LCAT ) is necessary for the activation of the enzyme , apoA 1 was labelled with N methylisatoic anhydride at lysine residues . ^^^ The intermolecular resonance energy transfer from tryptophan residues of LCAT ( donor ) to N methyl anthraniloyl ( NMA ) labelled apoA 1 ( NMA apoA 1 ) ( acceptor ) was used as a sensitive fluorescence method for studying molecular interactions . 2 . ^^^ Fluorescence energy transfer occurred from LCAT to NMA apoA 1 in the presence of liposomes with phospholipid / cholesterol ratios ranging from 5 : 1 to 18 : 1 and regardless whether only 1 or up to 5 NMA apoA 1 molecules resided at the liposome surface . 4 . ^^^ This indicates a preferred binding of the enzyme directly to or in spatial proximity to the activator protein NMA apoA 1 even if enough space at the liposome surface is available to allow LCAT binding at a distance , where no energy transfer is measurable . . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| But , cholesterol esters content in hepatocytes was higher in daunomycin induced nephrotic rats than control rats . 3 ) LCAT activity in serum was increased in daunomycin induced nephrotic rats . 4 ) Apolipoproteins composition of HDL in daunomycin induced nephrotic rats showed the increased apoA 1 and the decreased apo E . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| The disorder is characterized by elevated plasma total cholesterol ( TC ) , triglycerides ( TG ) , LDL cholesterol ( LDL C ) , apolipoproteins ( apo ) B , C 3 , and E , and by decreased levels of HDL cholesterol ( HDL C ) , apoA 1 , and lecithin : cholesterol acyltransferase ( LCAT ) activity . ^^^ The measured serum parameters included the levels of TC , VLDL C , LDL C , HDL C , TG , lathosterol , apoA 1 , B , C 3 , and E , as well as LCAT activity . ^^^ Simvastatin at 200 mg / d significantly decreased the levels of TC ( 25 % ) , LDL C ( 27 % ) , lathosterol ( 40 % ) , apoB ( 22 % ) , apoC 3 ( 37 % ) , and apoE ( 24 % ) and modestly decreased the levels of HDL C ( 12 % ) and apoA 1 ( 11 % ) ( percent relative to the average pretreatment and posttreatment baseline values ) but did not affect the levels of TG , VLDL C , the lathosterol / TC ratio , or LCAT activity . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Unlike serum it seems that in the tear fluid apoD exists mainly as a disulphide linked homodimer which is not associated with lecithin / cholesterol acyltransferase ( LCAT ) or apolipoprotein A 1 ( apo A 1 ) . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| It was associated with the high density lipoprotein fraction that contains apolipoprotein A 1 , an activator of LCAT . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Second , human and guinea pig LCAT were purified and used in phosphatidylcholine reconstituted vesicles containing human apoAI to show their ability to esterify tritiated cholesterol , PREG , and DHEA in the absence of unlabeled steroid . ^^^ The PREG and DHEA esterifying activities of LCAT were cofactor dependent , as shown by the absence of acylation without apoAI . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| We hypothesize that LCAT induced changes in HDL composition and size ultimately reduce apoA 1 catabolism by altering apoA 1 conformation and / or HDL particle regeneration . . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| When the discoidal rHDL of POPC / SPM / UC / apoA 1 molar ratio 99 . 6 / 0 . 0 / 10 . 2 / 1 . 0 were incubated with low density lipoproteins ( LDL ) and LCAT , SPM transferred spontaneously from the LDL to the rHDL ( t1 / 2 = 0 . 8 h ) and spherical particles with a POPC / SPM / UC / CE / apoA 1 molar ratio of 24 . 6 / 4 . 9 / 3 . 6 / 24 . 9 / 1 . 0 were formed . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| The biochemical changes in the 11 . 1 line , which is markedly deficient in plasma apoA 1 , an activator for LCAT , are reminiscent of those in patients with partial LCAT deficiency . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| The objective of this study was to evaluate the role of LCAT and apolipoprotein A 1 ( apoA 1 ) in Lp 10 metabolism in vitro and to elucidate the regulation of cholesterol esterification in this unique lipoprotein . ^^^ However , addition of human apoA 1 in the presence of albumin resulted in significant cholesterol esterification in Lp 10 ( Vmax 0 . 25 + / 0 . 04 nmol / h per microgram LCAT protein ) . ^^^ A reduction in Lp 10 size was observed when both apoA 1 and LCAT were included in the reaction mixture ( from 47 nm to 42 nm ) . ^^^ Our results suggest that while LCAT binds to isolated Lp 10 , apoA 1 is needed for the LCAT reaction to proceed . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| In order to clarify the role of sphingomyelin in the regulation of the LCAT reaction and its effects on the structure of apolipoprotein A 1 , we prepared reconstituted HDL ( rHDL ) containing egg phosphatidylcholine , cholesterol , apolipoprotein A 1 , and up to 22 mol % sphingomyelin . ^^^ Because the interfacial properties of substrate particles can dramatically affect LCAT binding and kinetics , we also prepared and analyzed proteoliposome substrates having the same components as the rHDL , except for a 4 fold higher ratio of phospholipid to apolipoprotein A 1 . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Increased prebeta HDL levels , cholesterol efflux , and LCAT mediated esterification in mice expressing the human cholesteryl ester transfer protein ( CETP ) and human apolipoprotein A 1 ( apoA 1 ) transgenes . ^^^ Furthermore , the LCAT mediated esterification of cell derived cholesterol is increased 1 . 7 fold in mice expressing the human apoA 1 and CETP transgenes compared to HuAITg mouse plasma . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Human apolipoprotein A 1 ( apoA 1 ) is the major protein component of high density lipoproteins ( HDL ) where it defines the particle structure and stability and functions as the main activator of the enzyme lecithin : cholesterol acyltransferase ( LCAT ) . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Discoidal reconstituted high density lipoproteins ( rHDL ) with a diameter of 7 . 9 nm , a molar ratio of egg phosphatidylcholine ( PC ) : unesterified cholesterol ( UC ) : cholesteryl esters ( CE ) : apolipoprotein ( apo ) A 1 of 33 : 7 : 0 : 1 and containing two molecules of apoA 1 per particle were incubated with lecithin : cholesterol acyltransferase ( LCAT ) in the presence of low density lipoproteins as a source of additional UC and PC for the LCAT reaction . ^^^ Thus , when lipid free apoA 1 is available , the LCAT mediated increase in number of apoA 1 molecules per rHDL particle is achieved by a direct incorporation of lipid free apolipoprotein without any need for particle fusion and therefore without a reduction in the number of rHDL particles . . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| To address this issue , we exposed the HDL containing d > 1 . 063 g / ml fraction of human plasma to copperoxidized LDL and assessed lecithin : cholesterol acyltransferase ( LCAT ) activity and apolipoproteinA 1 ( apoA 1 ) structure . ^^^ To determine whether LCAT was directly affected by oxidized LDL , independent of crosslinking of apoA 1 , we used an exogenous , [ 14C ] cholesterol labeled proteoliposome substrate to measure plasma LCAT activity . ^^^ Taken together , these data suggest that products of LDL oxidation may adversely affect HDL cholesterol metabolism by two separate mechanisms : 1 ) a direct inhibitory effect on LCAT activity and 2 ) through crosslinking of apoA 1 . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| To facilitate the investigation of apoA 1 structure : function relationships as they relate to LCAT activation and lipid binding , we have developed an apoA 1 baculoviral expression and purification system that yields milligram quantities of wild type or mutant proapoA 1 . ^^^ In addition , recombinant discoidal apoA 1 : phospholipid complexes prepared from wild type or plasma apoA 1 showed similar particle size and LCAT activation properties . ^^^ In summary , we show that baculovirus derived wild type proapoA 1 shows properties similar to plasma apoA 1 relative to recombinant HDL formation , LCAT reactivity , and alpha helical content . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| LCAT deficiency resulted in significant reductions in the plasma concentrations of total cholesterol , HDL cholesterol , and apoA 1 in both LCAT / mice ( 25 , 7 , and 12 % ; p < 0 . 001 of normal ) and LCAT + / mice ( 65 and 59 % ; p < 0 . 001 and 81 % ; not significant , p = 0 . 17 of normal ) . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| The concentrations in the serum of apolipoprotein A 1 , an activator of LCAT , was also reduced in cows with fatty livers . ^^^ These results suggest that the decreased LCAT activity , which may be attributable to impaired hepatic secretion or to the suppression of the activity in the plasma by reduced concentrations of phosphatidylcholine and apolipoprotein A 1 , resulted in the lower concentrations of cholesteryl esters . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| The lecithin : cholesterol acyltransferase ( LCAT ) kinetics and activation energy and the stability of apolipoprotein A 1 ( apoA 1 ) were investigated using recombinant HDL ( rHDL ) containing phosphatidylcholine ( PC ) , [ 3H ] cholesterol , and apo A 1 . ^^^ The concentration of guanidine HCl ( D1 / 2 ) required to denature one half of the apoA 1 on rHDL containing long chain PUFA was reduced ( 1 . 2 16 M ) compared to those containing 100 % POPC or 10 % PC / 90 % OPPC ( 2 . 2 2 . 4 M ) and there was a strong correlation ( r = 0 . 71 ) between LCAT activation energy and the stability of apoA 1 ( i . e . , D1 / 2 ) . ^^^ We conclude that long chain PUFA in the sn 2 position of PC decreases the catalytic efficiency of LCAT , the activation energy of the LCAT reaction and the stability of apoA 1 on the rHDL particles . ^^^ The strong association between rHDL apoA 1 stability and LCAT activation energy suggests that the temperature dependent step of the LCAT reaction may be sensitive to the strength of the interaction of apoA 1 with rHDL PC . . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Eight murine monoclonal antibodies ( Mab ) to apolipoprotein A 1 were characterized for their epitopes and for their ability to interfere with lecithin : cholesterol acyltransferase ( LCAT ) activation mediated by apo apoA 1 using a synthetic substrate . ^^^ When antibodies were tested for their ability to inhibit LCAT activation , an inhibitory effect was observed with those whose epitopes covered the area of apoA 1 encompassing amino acids 96 174 . ^^^ From these data we conclude that several areas of apoA 1 spanning the middle region of the apolipoprotein act in concert to stimulate LCAT activity , possibly by cooperative interaction with the enzyme . . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Our previous studies demonstrated that deletion of repeat 6 ( 143 164 ) or repeat 7 ( 165 186 ) resulted in a 98 99 % reduction of LCAT activation as compared with wild type apoA 1 . ^^^ Therefore , we speculate that the 5 6 fold lower LCAT reactivity in 10F6 compared with wild type apoA 1 recombinant particles results from increased stabilization within the 121 165 amino acid domain due to more stable apoprotein helix phospholipid interactions as well as from conformational alterations among adjacent amphipathic helix repeats . . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Compared to control mice there was more triglyceride and free cholesterol and less cholesteryl ester ( CE ) , suggesting that apoA 1 deficient HDL is a poor substrate for hepatic lipase and lecithin : cholesterol acyltransferase ( LCAT ) . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| These studies demonstrate that LCAT deficiency , similar to apoA 1 deficiency , is associated with a marked decrease in adrenal cholesterol delivery and supports the hypothesis that adrenal SR BI expression is regulated by the adrenal cholesterol . . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Binding of radiolabeled LCAT to rHDL of apoA 1 and apoA 1 ( Delta ( Arg 123 Tyr166 ) , nablaA 2 ( Ser 12 Ala75 ) ) was very similar . ^^^ In conclusion , although substitution of the Arg 123 Tyr166 central or Ala 190 Gln243 carboxyl terminal pair of helices of apoA 1 with the pair of helices of apoA 2 yields chimeras with structure similar to that of native apoA 1 , exchange of the central domain ( but not the carboxyl terminal domain ) of apoA 1 reduces the rate of LCAT activity that is independent of binding to rHDL . . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| We performed a series of mutations in the human apolipoprotein A 1 ( apoA 1 ) gene designed to alter specific amino acid residues and domains implicated in lecithin : cholesterol acyltransferase ( LCAT ) activation or lipid binding . ^^^ Mutant ( Glu 191 > Ala , His 193 > Ala , Lys 195 > Ala ) enhanced LCAT activation ( 131 % ) , and mutant ( Ala 152 > Leu , Leu 159 > Trp ) exhibited normal LCAT activation as compared with the wild type proapoA 1 and plasma apoA 1 forms [ corrected ] . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Interfacial binding affinities and capacities of lecithin : cholesterol acyltransferase ( LCAT ) and apolipoprotein A 1 ( apoA 1 ) for surfaces of different phosphatidylcholine ( PC ) composition , cholesterol content , and apolipoprotein content were measured with a vesicle model system . ^^^ ApoA 1 was isolated from human plasma and radiolabeled with iodine , whereas radiolabeled LCAT was purified from the media of Chinese hamster ovary cells that were transfected with human LCAT cDNA and incubated in the presence of [ 35S ] cysteine and methionine . ^^^ Bound and free radiolabeled LCAT and apoA 1 were quantified by phosphorimage analysis . ^^^ We conclude that vesicle surface PC fatty acyl composition and cholesterol content significantly influence LCAT and apoA 1 interfacial binding and therefore may alter LCAT enzymatic activity . . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Very low concentrations of alpha HDL in plasmas of apoA 1 ( L141R ) Pisa hemizygotes combined with reduced LCAT activity cause a decrease of the slow , unspecific , and LCAT dependent components of cholesterol efflux into plasma . . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| However , compared to control animals , the reductions in the plasma concentrations of HDL cholesterol and apoA 1 were less in LCAT tg mice ( HDL cholesterol : 62 + / 15 % vs . 78 + / 15 % , P = 0 . 18 ; apoA 1 : 36 + / 7 % vs . 76 + / 8 % , P < 0 . 0005 ) . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| As the beneficial effects of wild type apoA 1 are linked to its role in HDL cholesterol transport , we examined the capacity of apoA IMilano to recruit cell cholesterol and activate lecithin : cholesterol acyltransferase ( LCAT ) ( two key events in the antiatherogenic reverse cholesterol transport pathway ) . ^^^ We conclude that , even though apoA IMilano is a normal activator of LCAT , it is less efficient that wild type apoA 1 in recruiting cell cholesterol , suggesting that the putative antiatherogenic properties attributed to apoA IMilano may be unrelated to the initial stages of reverse cholesterol transport . . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Both apoA 1 ( Milano ) transgenics possessed normal levels of plasma LCAT activity , but endogenous cholesterol esterification rates were reduced by 50 % compared to controls . ^^^ Thus , HDL particle size restriction was not the result of impaired LCAT activation ; rather , dimerization of apoA 1 ( Milano ) limited the esterification of cholesterol on endogenous HDL . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Next , we used the stable apoA II / apoA 1 rHDL complex at the apoA II / apoA 1 ratio of 1 : 2 to examine its physical properties , apoA 1 structure , and reactivity with lecithin : cholesterol acyltransferase ( LCAT ) . ^^^ Finally , we showed that the reaction of the hybrid HDL with LCAT was inhibited 2 5 fold , relative to apoA 1 rHDL , due to a corresponding increase in the apparent Km value . ^^^ This suggests that LCAT binding to the hybrid particles is sterically hindered by the excess protein ( portions of apoA 1 and apoA 2 not bound to lipid ) . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| In the present study we investigated the effect of the apoA IFin mutation on lipoprotein profile , apoA 1 kinetics , lecithin : cholesterol acyltransferase ( LCAT ) activation , and cholesterol efflux in vitro . ^^^ Experiments with reconstituted proteoliposomes showed that the capacity of apoA IFin protein to activate LCAT was reduced to 40 % of that of the wild type apoA 1 . ^^^ In conclusion , although the apoA IFin mutation does not alter the properties of apoA 1 involved in promotion of cholesterol efflux , its ability to activate LCAT in vitro is defective . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Strong correlations were noted between LCAT activity and both apoA 1 ( r= 0 . 868 , P < 0 . 01 ) and LDL ( r = 0 . 670 , P = 0 . 06 ) FCR , indicating that LCAT activity played a major role in the mediation of lipoprotein metabolism . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Plasma levels of LCAT , cholesterol , low density lipoprotein cholesterol ( LDL C ) , high density lipoprotein cholesterol ( HDL C ) , triglycerides , apoB , and apoAI were evaluated before and after 1 and 3 months of therapy . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Increase in the maximum rate of CE production ( Vmax ) by LCAT is directly related to an increased negative charge on the different Lp2A 1 particles and to a reduced amount and stability of amphipathic alpha helices in apoA 1 . ^^^ In contrast , increasing the Lp2A 1 complex negative charge directly by addition of a charged lipid , phosphatidylinositol ( PI ) , has minimal effect on apoA 1 conformation and LCAT activation . ^^^ These results show that LCAT is stimulated by an apoA 1 conformation dependent increase in negative charge but is less sensitive to electrostatic changes in the lipid interface of discoidal Lp2A 1 . ^^^ The activation of LCAT appears to be dependent on the exposure of both central ( residues 98 132 ) and N terminal ( residues 2 8 ) domains in apoA 1 . ^^^ A strong relationship between the immunoreactivity of two specific mAbs , 4H1 and A 11 , and LCAT reactivity suggests that the N terminus of apoA 1 may interact with a central domain in a manner that may regulate the accessibility of LCAT to the edge of the disc . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Our data suggest that the Val156Glu substitution is associated with apoA 1 and HDL deficiency , partial LCAT deficiency , and corneal opacities and that Val 156 of apoA 1 may play an important role in apoA 1 function . . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| The data suggest that apoA 1 residues 146 160 and / or 220 242 partake in normal LCAT activation and that cooperative interactions between helices may be important for maximal cholesterol esterification . . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Apolipoprotein A 1 ( apoA 1 ) activates the plasma enzyme lecithin : cholesterol acyltransferase ( LCAT ) , catalyzing the rapid conversion of lipoprotein cholesterol to cholesterol ester . ^^^ Structural mutants of apoA 1 have been used to study the details of apoA 1 LCAT catalyzed cholesterol ester formation . ^^^ Apolipoprotein A 1 ( apoA 1 ) activates the plasma enzyme lecithin : cholesterol acyltransferase ( LCAT ) , catalyzing the rapid conversion of lipoprotein cholesterol to cholesterol ester . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Hepatic CETP , LCAT and apoA 1 mRNA levels were determined using reverse transcription polymerase chain reaction ( RT PCR ) . ^^^ Hepatic CETP mRNA levels , compared to GAPDH mRNA levels as a control , were increased in the HC group ( 2 . 226 + / 0 . 115 ) compared with the LC group ( 1 . 649 + / 0 . 170 ) ( p < 0 . 05 ) , while hepatic LCAT and apoA 1 mRNA levels were unchanged . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| To identify the effects of HDL oxidation on LCAT activity , a purified enzyme and cofactor in a vesicle solution ( an artificial substrate ) were used . 1 ) LCAT activity was inhibited by the oxidation of substrate vesicles , this inhibition being related to the degree of oxidation . 2 ) This inhibition was observed even if apolipoprotein A 1 was not oxidized . 3 ) Oxidized phosphatidylcholine , but not oxidized cholesterol , in the vesicles affected LCAT activity . 4 ) The addition of 0 40 % of oxidized vesicles to normal substrate vesicles resulted in the activity of LCAT being inhibited in a dose dependent manner . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| This study was designed to examine the effect of FA on the hepatic secretion of LCAT , triglyceride and apolipoprotein A 1 ( apoA 1 ) . ^^^ All FA ( except DHA ) significantly enhanced triglyceride secretion ; however , only the 18 carbon FA significantly stimulated the synthesis and secretion of apoA 1 and secretion of LCAT . ^^^ The secretion of LCAT correlated with apoA 1 secretion ( r = 0 . 88 , P = 0 . 004 ) but not with triglyceride secretion ( r = 0 . 55 , P = 0 . 12 ) . ^^^ These data indicate that FA that promote the apparent synthesis and secretion of apoA 1 also stimulate the secretion of LCAT in vitro , suggesting a coordinate regulatory mechanism for apoA 1 and LCAT expression . . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| A significant positive correlation of LCAT activity with total HDL ( r=0 . 42 ) , HDL 3 cholesterol ( r=0 . 46 ) and apolipoprotein A 1 ( r=0 . 47 ) was observed in affected subjects but not in controls . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Significant correlations ( P < 0 . 02 ) were observed between plasma LCAT activity and HDL C ( r = 0 . 857 ) , apoA 1 FCR ( r = 0 . 774 ) , and apoA 1 PR ( r = 0 . 771 ) , while HDL C correlated with both apoA 1 FCR ( 0 . 812 ) and PR ( 0 . 751 ) . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| In contrast to two other monogenic HDL deficiencies in which defects in the plasma proteins apoA 1 and LCAT interfere primarily with the formation of HDL ( refs 7 10 ) , TD shows a defect in cell signalling and the mobilization of cellular lipids . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| The compound heterozygous proband had negligible HDL and severely reduced apolipoprotein A 1 , LCAT mass , LCAT activity , and cholesterol esterification rate ( CER ) . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| We have studied the role of amphipathic alpha helices in the ability of apoA 1 to promote cholesterol efflux from human skin fibroblasts and activate lecithin : cholesterol acyltransferase ( LCAT ) . ^^^ In conclusion , our results show that no specific sequence in the central domain of apoA 1 is required for efficient diffusional cholesterol efflux from normal fibroblasts ; however , residues 144 186 appear critical for optimum LCAT activation and cholesteryl ester accumulation . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| To study LCAT activation by the trimeric apo AI ( 145 183 ) construct , complexes were prepared with dipalmitoylphosphatidylcholine ( DPPC ) , cholesterol ( C ) and either the trimeric construct or apoAI . ^^^ LCAT activation by the trimeric construct was much lower than by apo AI , possibly because the conformation of the trimeric 145 183 peptide in DPPC / C / peptide complexes does not mimic that of apoAI in the corresponding complexes . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| To date , transgenes for human apo ( a ) , apoA 1 , apoB , apoE 2 , apoE 3 , HL , and lecithin : cholesterol acyltransferase ( LCAT ) , as well as for rabbit apolipoprotein B mRNA editing enzyme catalytic poly peptide 1 ( APOBEC 1 ) , have been expressed in NZW rabbits , whereas only those for human apoA 1 and LCAT have been introduced into the WHHL background . ^^^ In both NZW and WHHL rabbits , human apoA 1 expression was associated with a significant reduction in the extent of aortic atherosclerosis , which was similarly the case for LCAT in rabbits having at least one functional LDL receptor allele . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Compared to normal apoA 1 , the LCAT cofactor activity of apoA 1 ( P165R ) and apoA 1 ( R160L ) Oslo as defined by the ratio of Vmax to appKm was reduced significantly by 62 % and 29 % , respectively ( here and throughout the text , the apparent Km is given as Michaelis Menten kinetics do not take particle binding into account and therefore would result in errors with an interfacial enzyme such as LCAT ; Vmax estimates are not affected by this error ) . ^^^ We conclude that amino acid residues arginine 160 and proline 165 of apoA 1 contribute to the formation of a domain that is very important for initial lipid binding and contributes to LCAT activation and promotion of initial cholesterol efflux but not to the stabilization of preformed rLpA I . . ^^^ |
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| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| We carried out HDL CE turnover studies in mice expressing human CETP and / or human lecithin : cholesterol acyltransferase ( LCAT ) transgenes on a background of human apoA 1 expression . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Compared to Lcat ( + / + ) mice , HDL cholesterol is reduced 94 % and apoA 1 , 90 % , in Lcat ( / ) mice ; this reduction in HDL is paralleled by a 71 % decrease in PAF AH activity and in a 58 % decrease in PON activity . ^^^ Fast protein liquid chromatography ( FPLC ) revealed that in Lcat ( + / + ) mice both PON and PAF AH activity is associated with large , apoA 1 containing HDL particles ( 9 . 7 nm by non denaturing gradient gel electrophoresis ) while in Lcat ( / ) mice both enzymes are associated with small 8 . 2 nm particles . ^^^ We conclude that the concomitant reduction in HDL and apoA 1 concentrations and PON and PAF AH activities is best explained by rapid clearance of the small HDL particles found in LCAT deficiency . . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Substrate saturation studies , using rHDL composed of 1 palmitoyl 2 oleoyl sn glycero 3 phosphocholine ( POPC ) , cholesterol , and apolipoprotein A 1 ( 80 : 5 : 1 ) indicated that the appK ( m ) for CHO hLCATH 6 , CHO hLCAT , and purified plasma LCAT were nearly identical at approximately 2 microm substrate cholesterol . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| ApoA 1 ( R 151 ) Paris is a natural apolipoprotein ( apo ) A 1 variant that is associated with low levels of high density lipoprotein cholesterol ( HDL cholesterol ) and the partial deficiency of lecithin : cholesterol acyl transferase ( LCAT ) in the plasma of heterozygous carriers . ^^^ We compared the abilities of recombinant normal apoA 1 and recombinant apoA 1 ( R151C ) Paris to clear an emulsion of dimyristoylphosphatidylcholine ( DMPC ) , to form reconstituted lipoproteins with dipalmitoylphosphatidylcholine ( DPPC ) , to activate LCAT , and to promote efflux of biosynthetic cholesterol from porcine aortic smooth muscle cells ( SMCs ) or of exogenous cholesterol from lipid loaded mouse peritoneal macrophages . ^^^ Compared to normal apoA 1 , apoA 1 ( R151C ) Paris had a reduced LCAT cofactor activity with a 60 % lower Vmax / Km ratio due to a 50 % higher affinity constant , Km . ^^^ In conclusion , in addition to its ability to form homo and heterodimers , apoA 1 ( R151C ) Paris is characterized by defective LCAT cofactor activity but by normal lipid binding and cholesterol efflux promoting abilities . . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| We have used transgenic mice ( Tgm ) expressing either both human apolipoprotein AI ( apo AI ) and human LCAT genes or only the human apo AI gene ( HuAILCAT or HuAI Tgm , respectively ) to assess the consequences of LCAT overexpression on serum lipid and lipoprotein profiles and on the ability of each serum to promote bidirectional flux of cholesterol between serum and Fu5AH hepatoma cells . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Reconstituted high density lipoproteins ( rHDL ) containing apolipoprotein A 1 or A 2 , ( apoA 1 or apoA 2 ) , low density lipoproteins ( LDL ) , and small unilamellar phosphatidylcholine vesicles , with biotin tags , were immobilized on biosensor chips containing streptavidin , and the binding kinetics of pure recombinant LCAT were examined as a function of LCAT concentration . ^^^ For the wild type LCAT , binding to all lipid surfaces had the same association rate constant , k ( a ) , but different dissociation rate constants , k ( d ) , that depended on the presence of apoA 1 ( k ( d ) decreased ) and different lipids in LDL . ^^^ Furthermore , increased ionic strength of the buffer decreased k ( a ) for the binding of LCAT to apoA 1 rHDL . ^^^ In conclusion , the association of LCAT to lipoprotein surfaces is essentially independent of their composition but has a small electrostatic contribution , while dissociation of LCAT from lipoproteins is decreased due to the presence of apoA 1 , suggesting protein protein interactions . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| We examined the effect of lipid free apolipoprotein A 1 ( apoA 1 ) and apoA 2 on the structure of reconstituted high density lipoproteins ( rHDL ) and on their reactivity as substrates for lecithin : cholesterol acyltransferase ( LCAT ) . ^^^ Finally , the effect of lipid free apoA 1 and apoA 2 on rHDL as substrates for LCAT was determined . ^^^ The addition of apoA 1 to A 2 POPCrHDL increased its reactivity with LCAT 24 fold , reflected by a 4 fold increase in apparent 5 ( m ) ax and a 6 fold decrease in apparent K ( m ) , while the addition of apoA 2 to A 2 POPCrHDL had no effect on its minimal reactivity with LCAT . ^^^ Likewise , the addition of apoA 1 to A 1 POPCrHDL inhibited the reaction with LCAT to about two thirds that of A 1 POPCrHDL without added apoA 1 . ^^^ Both apoA 1 and apoA 2 affect the reactivity of rHDL with LCAT , when added to the reaction in lipid free form . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| High density lipoprotein ( HDL ) metabolism and lecithin : cholesterol acyltransferase ( LCAT ) induced HDL remodeling were investigated in transgenic mice expressing human apolipoprotein ( apo ) AI or an apoAI / apoAII chimera in which the Arg 123 Tyr166 domain of apoAI was substituted with the Ser 12 Ala75 domain of apoAII . ^^^ Human LCAT gene transfer into apoAI transgenic mice resulted in a 5 . 1 fold increase of endogenous LCAT activity . ^^^ Agarose gel electrophoresis revealed that human LCAT gene transfer into human apoAI transgenic mice resulted in an increase of pre beta HDL and of pre alpha HDL . ^^^ In contrast , human LCAT gene transfer did not affect cholesterol levels and HDL distribution profile in mice expressing the apoAI / apoAII chimera . ^^^ Mouse LCAT did not `` see ' ' a difference between wild type and mutant human apoAI , whereas human LCAT did , thus localizing the species specific interaction in the central domain of apoAI . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Their serum lipid , apoA 1 , apoB 100 , ketone body ratio ( KBR ) , fat clearance , LCAT and so on were investigted . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Formation of such selectively oxidized apoA 1 ( i . e . apoA 1 ( +32 ) ) may affect the antiatherogenic properties of HDL , because it has been suggested that Met ( 86 ) and Met ( 112 ) are important for cholesterol efflux and Met ( 148 ) is involved in the activation of lecithin : cholesterol acyl transferase ( LCAT ) . ^^^ We also assessed the capacity of discoidal reconstituted HDL containing apoA 1 ( +32 ) to act as substrate for LCAT , and the dissociation of apoA 1 and apoA 1 ( +32 ) from reconstituted HDL . ^^^ Selective oxidation did not alter the alpha helicity of lipid free and lipid associated apoA 1 as assessed by circular dichroism , and the affinity for LCAT was comparable for reconstituted HDL containing apoA 1 or apoA 1 ( +32 ) . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Hepatic levels of apoA 1 mRNA in coconut oil fed animals were elevated 150 % after 4 weeks compared to chow fed controls ; hepatic mRNA levels for ten other genes either decreased slightly ( apoB , LCAT , hepatic lipase , albumin , ACAT , and HMG CoA reductase ) or were unchanged ( CETP , apoE , LDL receptor , and acyl CoA oxidase ) . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| The efficiency of RCT depends on the specific ability of apoA 1 to promote cellular cholesterol efflux , bind lipids , activate lecithin : cholesterol acyltransferase ( LCAT ) , and form mature HDL that interact with specific receptors and lipid transfer proteins . ^^^ The lower lipid binding affinity of the region 144 186 may be important to the activation mechanism allowing displacement of these apoA 1 helices by LCAT and presentation of the lipid substrates . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| In contrast , the mRNA levels of the potential regulatory proteins of the HDL level such as apoA 1 , apoE , LCAT , PLTP , SRB 1 and ABC 1 did not change with probucol . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| In order to investigate the effect of Probucol therapy on reverse cholesterol transport , apo AI containing lipoprotein particles were isolated and characterized , and their cholesterol effluxing capacity and LCAT activity were assayed in four familial hypercholesterolemia patients before and after 12 weeks of Probucol therapy . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| In summary , these data show a domain corresponding to apoA 1 repeat 6 is responsible for providing an essential conformation for LCAT catalyzed generation of cholesterol esters . ^^^ Deletion of apoA 1 repeat 6 not only blocks normal levels of cholesterol esterification but also exerts a dominant inhibition on the ability of wild type apoA 1 to activate LCAT in vivo . . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| We aimed to distinguish between the effects of mutations in apoA 1 on the requirements for the secondary structure and a specific amino acid sequence for lecithin : cholesterol acyltransferase ( LCAT ) activation . ^^^ Combined , our results strongly suggest that although the correct conformation and orientation of apoA 1 in the complex with lipids are crucial for activation of LCAT , when these conditions are fulfilled , activation also strongly depends on the sequence that includes amino acids 140 150 . . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| These data suggest that residues T 123 and F 382 , located N terminal of helices alpha 3 4 and alpha His , contribute specifically to the interaction of LCAT with HDL and possibly with its co factor apoA 1 . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Accumulation of cholestatic lipoproteins in ANIT treated human apolipoprotein A 1 transgenic rats is diminished through dose dependent apolipoprotein A 1 activation of LCAT . ^^^ It was hypothesised that the clearance was mediated through the movement of the PL and FC into apolipoprotein A 1 ( apo A 1 ) containing lipoproteins followed by LCAT esterification to form CE . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| This review gives an overview of the genes regulating these mechanisms , such as those encoding apolipoprotein AI , lecithin : cholesterol acyltransferase ( LCAT ) , scavenger receptor B 1 ( SR BI ) , and the ATP binding cassette transporter 1 ( ABC 1 ) , and the potential to exploit them to develop gene based therapeutic approaches to increase the level or function of HDL . . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| OBJECTIVE : To find out the change of serum total cholesterol , HDL cholesterol , LCAT activity , and the expression of apoA 1 mRNA in liver and intestine in the very early stage of experimental hyperlipidemia of rabbits . ^^^ CONCLUSION : In the very early stage of experimental hyperlipidemia , serum TC , FC , LCAT activity increase remarkably and apoA 1 , mainly produced in the small intestine , plays an important role in activating LCAT . . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| LCAT kinetic parameters were measured in two fractions with the same amount of ApoA 1 ( 5 microg / ml ) but different amounts of Hpt ( 0 . 69 or 3 . 77 microg / ml ) : the 5 ( max ) did not change while the K ( m ) values were 24 . 1 or 78 . 6 microM in the presence of the low or high Hpt level , respectively . ^^^ The results suggest that Hpt inhibits the reverse transport of cholesterol by preventing ApoA 1 stimulation of the LCAT activity . . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| To date , transgenes for human apo ( a ) , apoA 1 , apoB , apoE 2 , apoE 3 , hepatic lipase , lecithin : cholesterol acyltransferase ( LCAT ) , lipoprotein lipase , 15 lipoxygenase , as well as for rabbit apolipoprotein B mRNA editing enzyme catalytic polypeptide 1 ( APOBEC 1 ) , have been expressed in rabbits . ^^^ In addition , human apoA 1 , LCAT and apo ( a ) have been introduced into WHHL rabbits which have deficient LDL receptor function . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| We suggest that the decrease of HDL during the acute phase is caused by reduced LCAT and increased PLTP activities both increasing the plasma levels of lipid poor apoA 1 particles . . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| In vitro , these deletions had little effect on cellular cholesterol efflux from macrophages but LCAT activation was reduced by 50 and 70 % for the Delta 1 43 and Delta 1 65 apoA 1 mutants , respectively , relative to wild type ( Wt ) apoA 1 . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| In the present study apoA 1 ( Lys 107del ) , a naturally occurring human apoA 1 variant with a deletion of Lys 107 , was expressed in E . coli to examine the effect of this mutation on lipid binding , cholesterol efflux and lecithin : cholesterol acyltranferase ( LCAT ) activation . ^^^ ProapoA 1 ( Lys107del ) also activated LCAT similar to wild type proapoA 1 and human plasma apoA 1 . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Thiol reactive fluorescent probes attached to cysteine containing apoA 1 mutants are currently being used to investigate the `` LCAT active ' ' conformation of lipid bound apoA 1 . ^^^ Discoidal rHDL were then prepared with donor and / or acceptor labeled apoA 1 and characterized with respect to their size , composition and ability to activate LCAT . . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| ApoA 1 ( MALLORCA ) impairs LCAT activation and induces dominant familial hypoalphalipoproteinemia . ^^^ ApoA 1 ( MALLORCA ) is associated with HDL cholesterol deficiency ( concentration ranging from 8 48 % of the value in non carriers ) , and a 2 to 3 fold decrease in plasma concentrations of apoA 1 and apoA 2 and endogenous LCAT activity , concomitant with a slight decrease in serum cholesterol efflux capability . ^^^ Impairment of LCAT activity in HDL particles containing only mutated forms of apoA 1 would not explain a pattern of dominant inheritance . ^^^ HDL particles containing wild type apoA 1 and at least one mutant apoA 1 may also present impaired LCAT activity and / or other alterations leading to defective HDL maturation , a situation that would increase HDL lipid catabolism . ^^^ We conclude that amino acids 165 175 of apoA 1 are critical for normal HDL metabolism , at least in part because of their role in LCAT activation . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Linkage analyses showed that this major gene was not located in chromosomal regions that contain six candidate genes whose protein products are important to HDL metabolism ( LCAT , CETP , APOA 1 , APOE , ABCA 1 , LIPC ) . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Only traces of apolipoprotein A 1 remained in the quantitatively desorbed LCAT preparation which , however , contained a residual fraction of apolipoprotein D and acidic plasma proteins . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| To identify a possible genetic contribution to his biochemical phenotype , we sequenced the LCAT and APOA 1 genes . ^^^ RESULTS : There were no sequence abnormalities in LCAT , but we found that he was a heterozygote for a novel APOA 1 mutation in codon 107 ( AAG > TGG ) , which predicted the replacement of lysine by tryptophan ( K107W ) . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| The crystal structure is a twisted circular four helix bundle , consisting of four molecules of apoA 1 ( 44 243 ) , where four copies of the lecithin : cholesterol acyltransferase ( LCAT ) activating domains are located outside the ring structure , while the aromatic rich strong lipid binding domains are inside . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Recombinant Cys mutants of apolipoprotein A 1 ( apoA 1 ) ( A124C and A232C ) have been prepared in disulfide linked forms in order to assess the effects of unnatural covalent constraints on the folding of apoA 1 in solution , its ability to bind lipids , form HDL like particles , activate LCAT , and undergo structural adaptations to changing lipid contents . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| The other main HDL apolipoprotein , apoA 2 is incorporated into apoA 1 containing particles in a process of particle fusion mediated by LCAT . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| In this study , we tried to determine ( a ) whether there is any permanent effect of oxLDL on the LCAT molecule and its activator lipoprotein apoA 1 , and ( b ) the fate of oxLDL after its exposure to LCAT and apoA 1 . ^^^ These results indicate modification of the LCAT and apoA 1 molecule . ^^^ But LCAT was found more affected compared to apoA 1 in terms of LCAT activity . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Five natural mutations of apolipoprotein A 1 ( apoA 1 ) , apoA 1 ( A95D ) , apoA 1 ( Y100H ) , apoA 1 ( E110K ) , apoA 1 ( V156E ) and apoA 1 ( H162Q ) , were studied for their ability to activate lecithin : cholesterol acyltransferase ( LCAT ) . ^^^ Mutants apoA 1 ( E110K ) , apoA 1 ( V156E ) and apoA 1 ( H162Q ) had an impaired ability to activate LCAT . ^^^ Combined with data on other apoA 1 mutants this finding is consistent with the idea that the central region between amino acids 110 and 160 is likely to be the `` active site ' ' of apoA 1 involved in the interaction with LCAT and that a specific sequence of apoA 1 is required for activation of the enzyme . . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| In the present study the effects of dietary fat with defined fatty acids on lecithin : cholesterol acyltransferase ( LCAT ) and apoA 1 , the two components of HDL that play a major role in reverse cholesterol transport ( RCT ) , were examined . ^^^ The data indicate that TO increases the secretion of HDL and its components ( apoA 1 and LCAT ) , and stimulates the production of hepatic SR B 1 receptor protein . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| The dramatic loss of enzyme activity suggests that the N terminal residues of LCAT may be involved in maintaining the conformation of the lid domain and influence activation by the alpha LCAT cofactor apoA 1 ( in Delta 1 ) and / or loss of enzyme activity ( in Delta 1 Delta 5 ) . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| ApoA 1 , LCAT enzyme , ABCA 1 and cholesterol ester transfer protein are involved in RCT . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Taken together , these observations suggest that ABCA 1 is necessary for the adequate lipidation of apoAI , which enables the interaction with LCAT and subsequent maturation . . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Serum HDL concentration was decreased pathologically ( 7 mg / dl ) , although the LCAT activity was combined with apo AI deficiency . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| We sequenced three candidate genes ( ABCA 1 , APOA 1 , and LCAT ) that cause Mendelian forms of low HDL C levels in individuals from a population based study . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| In vitro functional analyses showed that reconstituted HDL ( rHDL ) particles containing the mutant apoA 1 had 53 % of scavenger receptor class B type 1 ( SR BI ) mediated cholesterol efflux capacity and 37 % capacity to activate lecithin : cholesterol acyltransferase ( LCAT ) as compared to the WT control . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Haptoglobin ( Hpt ) was previously found to bind the high density lipoprotein ( HDL ) apolipoprotein A 1 ( ApoA 1 ) and able to inhibit the ApoA 1 dependent activity of the enzyme lecithin : cholesterol acyltransferase ( LCAT ) , which plays a major role in the reverse cholesterol transport . ^^^ Such a sequence contains an ApoA 1 domain required for binding cells , promoting cholesterol efflux , and stimulating LCAT . ^^^ The results suggest that Hpt might mask the ApoA 1 domain required for LCAT stimulation , thus impairing the HDL function . ^^^ Synthetic peptides , able to displace Hpt from ApoA 1 without altering its property of binding hemoglobin , might be used for treatment of diseases associated with defective LCAT function . . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Cholesterol esterification rate ( CER ) in apoA 1 ( ) ( / ) ( ) apoE ( ) ( / ) ( ) mouse plasma was < 7 % that of C57Bl / 6 ( B 6 ) mouse plasma , even though apoA 1 ( ) ( / ) ( ) apoE ( ) ( / ) ( ) plasma retained ( 1 ) / ( 3 ) the amount of B 6 LCAT activity . ^^^ This suggested that lack of LCAT enzyme did not explain the low CER in apoA 1 ( ) ( / ) ( ) apoE ( ) ( / ) ( ) mice and indicated that apoE and apoA 1 are the only major activators of LCAT in mouse plasma . ^^^ LDLs ( 1 microg FC ) from each genotype were incubated with purified recombinant mouse LCAT ; LDL particles from B 6 and apoA 1 ( ) ( / ) ( ) plasma were much better substrates for CE formation ( 5 . 7 % and 6 . 3 % CE formed / 30 min , respectively ) than those from apoE ( ) ( / ) ( ) and apoE ( ) ( / ) ( ) apoA 1 ( ) ( / ) ( ) plasma ( 1 . 2 % and 1 . 1 % CE formed / 30 min ) . ^^^ Adding apoE to incubations of apoA 1 ( ) ( / ) ( ) apoE ( ) ( / ) ( ) very low density lipoprotein ( VLDL ) resulted in a 3 fold increase in LCAT CER , whereas addition of apoA 1 resulted in a more modest 80 % increase . ^^^ We conclude that apoE is a more significant activator of LCAT than apoA 1 on mouse apoB lipoproteins . . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Fortuitously , we were able to directly compare carotid intima media thickness data of substantial numbers of individuals with mutations in either apolipoprotein A 1 ( apoA 1 ) , ATP binding cassette AI ( ABCA 1 ) , lecithin : cholesterol acyltransferase ( LCAT ) or cholesteryl ester transfer protein . ^^^ These data show that carriers of an apoA 1 mutation exhibit the most pronounced accelerated atherosclerosis compared with those carrying mutations in ABCA 1 and LCAT . ^^^ SUMMARY : Intima media thickness studies have provided evidence that hypoalphalipoproteinemia due to mutations in apoA 1 , ABCA 1 , and LCAT is associated with increased progression of atherosclerosis . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Although both particles had similar 5 ( max ) ( 8 . 4 vs . 8 . 2 nmol cholesteryl ester / h / microg LCAT , respectively ) , the K ( m ) value was increased 2 fold for alpha LpA 1 compared with r ( HDL ) ( 1 . 2 vs . 0 . 7 microM apoA 1 ) . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Plasma unesterified cholesterol , unesterified / total cholesterol ratio , triglycerides , very low density lipoprotein cholesterol , and pre beta high density lipoprotein ( LDL ) were elevated , and high density lipoprotein ( HDL ) cholesterol , apolipoprotein A 1 , apolipoprotein A 2 , apolipoprotein B , LpA 1 , LpA 1 : A 2 , cholesterol esterification rate , LCAT activity and concentration , and LDL and HDL 3 particle size were reduced in a gene dose dependent manner in carriers of mutant LCAT alleles . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| While no LCAT mutation was detected , a novel nonsense apoA 1 mutation ( E136X ) was found in 3 / 54 probands . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| ApoA 1 enters the plasma as a component of discoidal particles , which are remodeled into spherical ( A 1 ) HDL by LCAT . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| We have analyzed the effect of charged to neutral amino acid substitutions around the kinks flanking helices 4 and 6 of apoA 1 and of the deletion of helix 6 on the in vivo activity of LCAT and the biogenesis of HDL . ^^^ The LCAT activation capacity of apoA 1 in vitro was nearly abolished by the helix 6 point ( helix 6P apoA 1 [ R160V / H162A ] ) and deletion { helix 6Delta apoA 1 [ Delta ( 144 165 ) ] } mutants , but was reduced to 50 % in the helix 4 point mutant ( helix 4P apoA 1 [ D102A / D103A ] ) . ^^^ Coinfection of mice with adenoviruses expressing human LCAT and the helix 6P mutant dramatically increased plasma HDL and apoA 1 levels and converted the discoidal into spherical HDL , indicating that the LCAT activity was rate limiting for the biogenesis of HDL . ^^^ The LCAT treatment caused only a small increase in HDL cholesterol and apoA 1 levels and in alpha HDL particle numbers in the helix 6Delta mutant . ^^^ The findings indicate a critical contribution of residue 160 of apoA 1 to the in vivo activity of LCAT and the subsequent maturation of HDL and explain the low HDL levels in heterozygous subjects carrying this mutation . . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Major constituents of RCT include acceptors such as high density lipoprotein ( HDL ) and apolipoprotein A 1 ( apoA 1 ) , and enzymes such as lecithin : cholesterol acyltransferase ( LCAT ) , phospholipid transfer protein ( PLTP ) , hepatic lipase ( HL ) and cholesterol ester transfer protein ( CETP ) . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Monogenic high density lipoprotein ( HDL ) deficiency , because of defects in the genes of apolipoprotein A 1 ( apoA 1 ) , adenosine triphosphate binding cassette transporter A 1 ( ABCA 1 ) or lecithin : cholesterol acyltransferase ( LCAT ) , can be assumed in patients with HDL cholesterol levels below the fifth percentile within a given population . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| APOA 1 , LCAT , and SRB 1 exerted no measurable influence . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| When the ability of discoidal reconstituted high density lipoprotein ( rHDL ) containing apoE 2 [ ( E 2 ) rHDL ] , apoE 3 [ ( E 3 ) rHDL ] , or apoE 4 [ ( E 4 ) rHDL ] as the sole apolipoprotein to act as substrates for LCAT were compared with that of discoidal rHDL containing apoA 1 [ ( A 1 ) rHDL ] , the rate of cholesterol esterification was ( A 1 ) rHDL > > ( E 2 ) rHDL approximately ( E 3 ) rHDL > ( E 4 ) rHDL . ^^^ In conclusion , 1 ) apoE activates LCAT less efficiently than apoA 1 ; 2 ) apoE containing spherical rHDLs are structurally distinct from spherical ( A 1 ) rHDL ; and 3 ) the CETP mediated remodeling of apoE containing spherical rHDL differs from that of spherical ( A 1 ) rHDL . . ^^^ |
|
| Interacting proteins: P04180 and P02647 |
Pubmed |
SVM Score :0.0 |
| Role of apoA 1 , ABCA 1 , LCAT , and SR BI in the biogenesis of HDL . ^^^ Through a series of intermediate steps , lipidated apoA 1 proceeds to form discoidal HDL particles that can be converted to spherical particles by the action of lecithin : cholesterol acyltransferase ( LCAT ) . ^^^ In the same way , specific mutations in apoA 1 or LCAT prevent the conversion of discoidal to spherical HDL particles . ^^^ The phenotypes generated in experimental mouse models for apoA 1 , ABCA 1 , LCAT , SR BI , and other proteins of the HDL pathway may facilitate early diagnosis of similar phenotypes in the human population and provide guidance for proper treatment . . ^^^ |
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