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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Holers, V. M. Anderson, D. C. Brown, E. J. Graham, I. L. |
| Description | Author Affiliation: Graham IL ( Department of Pediatrics, Washington University School of Medicine, St. Louis, Missouri 63110.) |
| Abstract | Expression of the leukocyte (beta 2) integrins is required for many functions of activated neutrophils (PMN), even when there is no recognized ligand for any beta 2 integrin. To investigate the hypothesis that beta 2 integrins may be involved in a signal transduction pathway related to cytoskeletal reorganization, we examined whether beta 2 integrins have a role in tyrosine phosphorylation of the cytoskeletal protein paxillin. Treatment of PMN in suspension with phorbol esters, f-Met-Leu-Phe, and TNF-alpha resulted in paxillin tyrosine phosphorylation. However, treatment of beta 2-deficient (LAD) PMN failed to induce paxillin tyrosine phosphorylation. Normal PMN phosphorylated paxillin in response to adhesion to immune complexes, while the LAD PMN did not. Adhesion of phorbol ester activated-LAD PMN to the extracellular matrix proteins fibronectin, laminin, and vitronectin failed to induce paxillin tyrosine phosphorylation. Treatment of activated normal PMN with mAb directed against the beta 2 integrin alpha chains demonstrated that CR3 (alpha M beta 2) was required for paxillin phosphorylation. Transfection of the cell line K562 with CR3 confirmed that CR3 ligation resulted in paxillin tyrosine phosphorylation. As a control, K562 transfected with CR2 (CD21) which bound equally avidly to the same complement C3-derived ligand (C3bi) as the CR3 transfectants, showed no enhanced tyrosine phosphorylation of paxillin upon receptor ligation. While both CR2 and CR3 transfectants showed efficient adhesion to a C3bi-coated surface, only the CR3 transfectants spread during adhesion and phosphorylated paxillin. Together these data demonstrate that CR3 is required for paxillin phosphorylation during activation of both adherent and nonadherent PMN. Even PMN activated in suspension or by adhesion to immune complexes, when no CR3 ligand is apparent, still require CR3 for a signal transduction pathway leading to paxillin tyrosine phosphorylation. This pathway is likely to be important for PMN function in inflammation and host defense. |
| ISSN | 00219525 |
| e-ISSN | 15408140 |
| Journal | The Journal of Cell Biology |
| Issue Number | 4 |
| Volume Number | 127 |
| Language | English |
| Publisher | Rockefeller University Press (United States) |
| Publisher Date | 1994-11-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Cell Adhesion Cytoskeletal Proteins Metabolism Integrins Physiology Neutrophils Phosphoproteins Receptors, Complement Tyrosine Analogs & Derivatives Adolescent Antigens, CD18 Cell Line Isolation & Purification Extracellular Matrix Proteins In Vitro Techniques Biosynthesis N-Formylmethionine Leucyl-Phenylalanine Pharmacology Drug Effects Paxillin Phorbol 12,13-Dibutyrate Phosphorylation Phosphotyrosine Signal Transduction Transfection Tumor Cells, Cultured Tumor Necrosis Factor-alpha Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Cell Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Medicine |
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