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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 appearance of changes in phosphorylation previously described. These results suggest that p56lck may play an important role in the CD2 activation pathway.

Original publication

DOI

10.1002/eji.1830210828

Type

Journal article

Journal

Eur J Immunol

Publication Date

08/1991

Volume

21

Pages

1967 - 1970

Keywords

Antigens, CD, Antigens, CD2, Antigens, Differentiation, T-Lymphocyte, Humans, Lymphocyte Activation, Lymphocyte Specific Protein Tyrosine Kinase p56(lck), Phosphorylation, Protein-Tyrosine Kinases, Proto-Oncogene Proteins, Receptors, Immunologic, T-Lymphocytes