The tyrosine kinase activity of p56lck is increased in human T cells activated via CD2.

Journal article

An early biochemical event associated with T cell activation is tyrosine phosphorylation. We have previously shown that p56lck, a lymphocyte-specific protein tyrosine kinase, is hyperphosphorylated on serine and tyrosine residues 15 minutes after activation via CD2 with a concomitant shift to a higher molecular mass. We now demonstrate that the tyrosine kinase activity of p56lck is increased within seconds following CD2 triggering. This activity decreases thereafter correlating with the appea...

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Authors: Danielian, S; Fagard, R; Alcover, A; Acuto, O; Fischer, S

• Publication status: Published
• Journal: European journal of immunology
• Volume: 21
• Issue: 8
• Pages: 1967-1970
• Publication date: 1991-08-01
• DOI: 10.1002/eji.1830210828
• EISSN: 1521-4141
• ISSN: 0014-2980
• Language: English
• Keywords: Lymphocyte Activation; Receptors, Immunologic; Proto-Oncogene Proteins; T-Lymphocytes; Lymphocyte Specific Protein Tyrosine Kinase p56(lck); Humans; Phosphorylation; Protein-Tyrosine Kinases; Antigens, CD2; Antigens, CD; Antigens, Differentiation, T-Lymphocyte