Antibody and B7/BB1-mediated ligation of the CD28 receptor induces tyrosine phosphorylation in human T cells
| العنوان: | Antibody and B7/BB1-mediated ligation of the CD28 receptor induces tyrosine phosphorylation in human T cells |
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| المؤلفون: | Craig B. Thompson, Peter Vandenberghe, Gordon J. Freeman, Lee M. Nadler, Laurence A. Turka, Mary C. Fletcher, Jeffrey A. Ledbetter, Carl H. June, Malek Kamoun |
| المصدر: | The Journal of Experimental Medicine |
| بيانات النشر: | Rockefeller University Press, 1992. |
| سنة النشر: | 1992 |
| مصطلحات موضوعية: | Antigens, Differentiation, T-Lymphocyte, Time Factors, Lactams, Macrocyclic, T-Lymphocytes, Immunology, Receptors, Cell Surface, chemical and pharmacologic phenomena, Protein tyrosine phosphatase, In Vitro Techniques, SH2 domain, Receptor tyrosine kinase, chemistry.chemical_compound, CD28 Antigens, Antigens, CD, Histocompatibility Antigens, Benzoquinones, Tumor Cells, Cultured, Humans, Immunology and Allergy, Phosphorylation, Phosphotyrosine, biology, Receptor Aggregation, Quinones, Antibodies, Monoclonal, hemic and immune systems, Tyrosine phosphorylation, Articles, Phosphoproteins, Molecular biology, Molecular Weight, Rifabutin, chemistry, ROR1, biology.protein, Interleukin-2, Leukocyte Common Antigens, Tetradecanoylphorbol Acetate, Tyrosine, Tyrosine kinase, Platelet-derived growth factor receptor, Signal Transduction |
| الوصف: | CD28 is an adhesion receptor expressed as a 44-kD dimer on the surface of a major subset of human T cells. The CD28 receptor regulates the production of multiple lymphokines, including interleukin 2 (IL-2), by activation of a signal transduction pathway that is poorly understood. Here we show that ligation of CD28 by a monoclonal antibody (mAb) or by a natural ligand, B7/BB1, induces protein tyrosine phosphorylation that is distinct from T cell receptor (TCR)-induced tyrosine phosphorylation. CD28-induced protein tyrosine phosphorylation was greatly enhanced in cells that had been preactivated by ligation of the TCR, or by pretreatment with phorbol esters. Rapid and prolonged tyrosine phosphorylation of a single substrate, pp100, was induced in T cells after interaction with B7/BB1 presented on transfected Chinese hamster ovary (CHO) cells. Anti-B7 mAb inhibited B7/BB1 receptor-induced tyrosine phosphorylation, indicating that B7-CD28 interaction was required. CD28-induced tyrosine phosphorylation was independent of the TCR because it occurred in a variant of the Jurkat T cell line that does not express the TCR. Herbimycin A, a protein tyrosine kinase inhibitor, could prevent CD28-induced tyrosine phosphorylation and CD28-induced IL-2 production in normal T cells. The simultaneous crosslinking of CD28 and CD45, a tyrosine phosphatase, could prevent tyrosine phosphorylation of pp100. These results suggest that specific tyrosine phosphorylation, particularly of pp100, occurs directly as a result of CD28 ligand binding and is involved in transducing the signal delivered through CD28 by accessory cells that express the B7/BB1 receptor. Thus, this particular form of signal transduction may be relevant to lymphokine production and, potentially may provide a means to study the induction of self-tolerance, given the putative role of the costimulatory signal in the induction of T cell activation or anergy. |
| تدمد: | 1540-9538 0022-1007 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cd23c730f6ac473f3e60e0133282bccc https://doi.org/10.1084/jem.175.4.951 |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....cd23c730f6ac473f3e60e0133282bccc |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 15409538 00221007 |
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