| Interacting proteins: P51888 and P98160 |
Pubmed |
SVM Score :0.0 |
| The intimal proteoglycan composition in these preatherosclerotic lesions was found to be more complex than previously appreciated with up to eight distinct core proteins present , including the large extracellular proteoglycans versican and aggrecan , the basement membrane proteoglycan perlecan , the class 1 small leucine rich proteoglycans biglycan and decorin , and the class 2 small leucine rich proteoglycans lumican , fibromodulin , and prolargin / PRELP ( proline arginine rich end leucine rich repeat protein ) . ^^^ |
|
| Interacting proteins: P51888 and P98160 |
Pubmed |
SVM Score :0.0 |
| The leucine rich repeat protein PRELP binds perlecan and collagens and may function as a basement membrane anchor . ^^^ In search of natural ligands and biological functions of this molecule , we found that PRELP binds the basement membrane heparan sulfate proteoglycan perlecan . ^^^ Also , recombinant perlecan domains 1 and 5 carrying heparan sulfate bound PRELP , whereas other domains without glycosaminoglycan substitution did not . ^^^ Glycosaminoglycan free recombinant perlecan domain 5 and mutated domain 1 did not bind PRELP . ^^^ The dissociation constants of the PRELP perlecan interactions were in the range of 3 18 nm as determined by surface plasmon resonance . ^^^ |
|