Residues Y429 and Y463 of the human CD5 are targeted by protein tyrosine kinases
Autor: | Josep M. Vilà, Francisco Lozano, Olga Padilla, Idoia Gimferrer, Jordi Vives, Lourdes Places, Mònica Arman, Maria Simarro |
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Rok vydání: | 2001 |
Předmět: |
CD3 Complex
Recombinant Fusion Proteins T-Lymphocytes Immunology chemical and pharmacologic phenomena Protein tyrosine phosphatase Biology CD5 Antigens Lymphocyte Activation Proto-Oncogene Proteins c-fyn Transfection SH2 domain Receptor tyrosine kinase Jurkat Cells chemistry.chemical_compound Proto-Oncogene Proteins Humans Immunology and Allergy Phosphorylation Phosphotyrosine Tyrosine-protein kinase CSK Antibodies Monoclonal hemic and immune systems Tyrosine phosphorylation Protein-Tyrosine Kinases Cell biology Enzyme Activation Amino Acid Substitution Biochemistry chemistry Lymphocyte Specific Protein Tyrosine Kinase p56(lck) Mitogen-activated protein kinase Mutation biology.protein Tyrosine Protein Tyrosine Phosphatases Vanadates Tyrosine kinase Proto-oncogene tyrosine-protein kinase Src |
Zdroj: | European Journal of Immunology. 31:1191-1198 |
ISSN: | 1521-4141 0014-2980 |
DOI: | 10.1002/1521-4141(200104)31:4<1191::aid-immu1191>3.0.co;2-h |
Popis: | The human CD5 lymphocyte cell surface co-receptor modulates activation and differentiation responses mediated by the antigen-specific receptor of T and B cells. CD5 is phosphorylated following lymphocyte activation; however, the exact sites and kinases involved are yet to be determined. Jurkat T cell transfectants expressing tyrosine-mutated CD5 molecules have been used to show that residues Y429 and Y463 are targeted in vivo by protein tyrosine kinases following cell stimulation with anti-CD3 mAb or pervanadate. This is in agreement with data from direct in vitro kinase assays using purified recombinant Lck and Fyn protein tyrosine kinases. The analysis of Lck- and CD3-deficient Jurkat cells shows that tyrosine phosphorylation of CD5 requires Lck activity. We propose that T cell activation mediates CD5 tyrosine phosphorylation at residues Y429 and Y463 mainly through the activation of Lck. |
Databáze: | OpenAIRE |
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