| Interacting proteins: Q15124 and P11532 |
Pubmed |
SVM Score :0.60590828 |
| A 60 kDa protein localised in adherens type cellular junctions , and previously called aciculin , has been found to interact with the cytoskeletal proteins dystrophin and utrophin [ Belkin , A . 0.60590828^^^ |
|
| Interacting proteins: Q15124 and P11532 |
Pubmed |
SVM Score :0.0 |
| Association of aciculin with dystrophin and utrophin . ^^^ The association between aciculin and dystrophin in C2C12 cells was shown to resist Triton 10 100 extraction and the majority of the complex could be extracted only in the presence of ionic detergents . ^^^ In the reverse immunoprecipitation experiments , aciculin was detected in the precipitates with different anti dystrophin antibodies . ^^^ Immunodepletion experiments with lysates of metabolically labeled C2C12 myotubes showed that aciculin is a major dystrophin associated protein in cultured skeletal muscle cells . ^^^ Double immunostaining of differentiating and mature C2C12 myotubes with antibodies against aciculin and dystrophin revealed precise colocalization of these two cytoskeletal proteins throughout the process of myodifferentiation in culture . ^^^ |
|
| Interacting proteins: Q15124 and P11532 |
Pubmed |
SVM Score :0.0 |
| Dystrophin , vinculin , and aciculin in skeletal muscle subject to chronic use and disuse . ^^^ We hypothesized 1 ) that chronic muscle use and disuse would alter the expression of dystrophin as a compensatory mechanism designed to prevent muscle damage , and 2 ) that other subsarcolemmal cytoskeletal proteins ( vinculin , M vinculin , aciculin 60 / 63 kDa ) that colocalize with dystrophin in muscle adherens junctions would be changed in parallel . ^^^ Denervation also induced 3 . 3 fold increases in vinculin and aciculin 60 kDa , in parallel with dystrophin . ^^^ However , in contrast to its effects on dystrophin , chronic stimulation increased the levels of vinculin and aciculin 60 kDa by 3 . 4 and 6 . 4 fold , respectively . ^^^ |
|
| Interacting proteins: Q15124 and P11532 |
Pubmed |
SVM Score :0.0 |
| We attempted to determine ( 1 ) the immunostainability of anti aciculin antibody for the 6 histochemically normal human muscles and seven muscles from boys with Duchenne muscular dystrophy ( DMD ) and 11 disease control muscles , ( 2 ) the ultrastructural localization of aciculin in normal skeletal myofibers , ( 3 ) aciculin ' s spacial relationship with dystrophin and beta spectrin , and ( 4 ) if the aciculin is ultrastructurally colocalized with dystrophin , the distance from the aciculin epitope to the epitope of the dystrophin N or C terminal domain . ^^^ Immunohistochemical staining showed that the immunostainability of DMD muscles for anti aciculin antibody was markedly decreased as compared with normal and disease control muscles . ^^^ Aciculin and its relation to dystrophin : immunocytochemical studies in human normal and Duchenne dystrophy quadriceps muscles . ^^^ Aciculin is a novel adherens junction antigen extracted from human uterine smooth muscle that is reported to associate biochemically with dystrophin . ^^^ Single and double immunogold labeling electron microscopy of 6 histochemically normal human quadriceps femoris muscles revealed that aciculin was present along the inner surface of muscle plasma membrane and that aciculin formed doublets more frequently with dystrophin ( 23 . 5 + / 1 . 8 % ; group mean + / SE ) than with beta spectrin ( 12 . 8 + / 1 . 1 % ; P < 0 . 01 two tailed t test ) . ^^^ |
|