Integrin-associated protein: a 50-kD plasma membrane antigen physically and functionally associated with integrins
| Autor: | Eric J. Brown, H D Gresham, Lora V. Hooper, Thang Ho |
|---|---|
| Rok vydání: | 1990 |
| Předmět: |
Blood Platelets
Integrins Erythrocytes Neutrophils Immunoprecipitation Phagocytosis Molecular Sequence Data Integrin Biology Monocytes Antigen Signal-regulatory protein alpha Humans Amino Acid Sequence Lymphocytes Cell Membrane Antibodies Monoclonal Articles Cell Biology Molecular biology Molecular Weight Antigens Surface biology.protein Antibody Signal transduction Peptides Protein A |
| Zdroj: | The Journal of Cell Biology |
| ISSN: | 1540-8140 0021-9525 |
| DOI: | 10.1083/jcb.111.6.2785 |
| Popis: | Phagocytosis by monocytes or neutrophils can be enhanced by interaction with several proteins or synthetic peptides containing the Arg-Gly-Asp sequence. Recently we showed that an mAb, B6H12, specifically inhibited this enhancement of neutrophil phagocytosis by inhibiting Arg-Gly-Asp binding to the leukocyte response integrin (Gresham, H. D., J. L. Goodwin, P. M. Allen, D. C. Anderson, and E. J. Brown. 1989. J. Cell Biol. 108:1935-1943). Now, we have purified the antigen recognized by B6H12 to homogeneity. Surprisingly, it is a 50-kD molecule that is expressed on the plasma membranes of all hematopoietic cells, including erythrocytes, which express no known integrins. On platelets and placenta, but not on erythrocytes, this protein is associated with an integrin that can be recognized by an anti-beta 3 antibody. In addition, both the anti-beta 3 and several mAbs recognizing the 50-kD protein inhibit Arg-Gly-Asp stimulation of phagocytosis. These data demonstrate an association between integrins and the 50-kD protein on several cell types. For this reason, we call it Integrin-associated Protein (IAP). We hypothesize that IAP may play a role in signal transduction for enhanced phagocytosis by Arg-Gly-Asp ligands. |
| Databáze: | OpenAIRE |
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