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© Andres Alcover
Scanning electron microscopy showing a conjugate formed between a T lymphocyte and an antigen presenting cell. It is worth noting the long shape of the T cell (Tc) polarized towards the antigen presenting cell (APC) and the membrane protrusions that adhere the T lymphocyte to the antigen presenting cell.
Publication : European journal of immunology

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

Team: Archived: Lymphocyte Cell Biology
Member: Andres Alcover
Scientific Fields
Diseases
Organisms
Applications
Technique

Published in European journal of immunology - 01 Aug 1991

Danielian S, Fagard R, Alcover A, Acuto O, Fischer S

Link to Pubmed [PMID] – 1678351

Eur. J. Immunol. 1991 Aug;21(8):1967-70

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.