T-Lymphocyte Interleukin 2-Dependent Tyrosine Protein Kinase Signal Transduction Involves the Activation of p56lck

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 88; no. 5; pp. 1996 - 2000
• Main Authors: Horak, Ivan D., Gress, Ronald E., Lucas, Phillip J., Horak, Eva M., Waldmann, Thomas A., Bolen, Joseph B.
• Format: Journal Article
• Language: English
• Published: Washington, DC National Academy of Sciences of the United States of America 01-03-1991; National Acad Sciences
• Subjects: Analysis of the immune response. Humoral and cellular immunity; Antibodies; Automatic picture transmission; Biological and medical sciences; CD4 Antigens - analysis; Cell Line; Cell lines; Clone Cells; Enzyme Activation; Fundamental and applied biological sciences. Psychology; Fundamental immunology; Gels; Humans; Immunobiology; Immunology; Interleukin-2 - pharmacology; Interleukins; Kinetics; Lymphocyte Specific Protein Tyrosine Kinase p56(lck); Lymphokines, interleukins ( function, expression); Phosphorylation; Protein-Tyrosine Kinases - metabolism; Receptors; Regulatory factors and their cellular receptors; Signal Transduction; T lymphocytes; T-Lymphocytes - drug effects; T-Lymphocytes - enzymology; T-Lymphocytes - immunology; Human; Signal transduction; Phosphorylation; Interleukin 2; Cytokine; T-Lymphocyte; Molecular interaction; Activation; Mechanism of action; Protein-tyrosine kinase; Biological receptor
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.88.5.1996

Addition of interleukin 2 (IL-2) to IL-2-dependent T cells results in tyrosine protein kinase signal transduction events even though the IL-2 receptor α and β chains lack intrinsic enzymatic activity. Here we report that addition of IL-2 to IL-2-dependent human T cells transiently stimulates the specific activity of p56lck, a member of the src family of nonreceptor tyrosine protein kinases expressed at high levels in T lymphocytes. The ability of IL-2 to induce p56lckactivation was found to be independent of the capacity of p56lckto associate with either CD4 or CD8. Following IL-2 treatment, p56lckwas found to undergo serine/threonine phosphorylation modifications that resulted in altered mobility of the lck gene product on polyacrylamide gels. These observations raise the possibility that p56lckparticipates in IL-2-mediated signal transduction events in T cells.