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| Content Provider | PubMed Central |
|---|---|
| Author | Takada, Y. Strominger, J. L. Hemler, M. E. |
| Abstract | The very late antigen (VLA) protein family contains at least five related heterodimers, including a fibronectin receptor structure, and probably other cell substrate adhesion receptors. These cell-surface VLA proteins were immunopurified from human placenta (VLA-1, VLA-3, and VLA-5), platelets (VLA-2), and Molt-4 cells (VLA-4) using a series of monoclonal antibody-Sepharose immunoaffinity columns. After further purification by gel electrophoresis, the N-terminal amino acid sequence for each of the five VLA alpha subunits was determined. In the first 14 positions, the five VLA alpha subunits showed an average of 42% homology to each other, rising to 59% including conservative amino acid substitutions. In addition, the alpha subunits from the LFA-1, Mac-1 (CR-3), and p150,95 family of heterodimers, the vitronectin receptor-platelet GPIIb/IIIa family, and a position-specific (PS) antigen important in Drosophila embryogenesis each showed average homologies of 31-40% to individual VLA alpha sequences and 46-52% homology to VLA alpha subunits including conservative substitutions. Taken together, these results suggest that the VLA proteins, the LFA-1, Mac-1, and p150,95 family, the GPIIb/IIIa, vitronectin receptor family, and the Drosophila PS antigens have evolved as four subgroups in a highly conserved supergene family of receptors involved in fundamentally important functions, such as cell adhesion, migration, and embryogenesis. |
| Starting Page | 3239 |
| File Format | |
| ISSN | 10916490 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 10 |
| Volume Number | 84 |
| Language | English |
| Publisher Date | 1987-05-01 |
| Access Restriction | Open |
| Subject Keyword | Research in Higher Education |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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