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The Journal of Immunology, Vol 154, Issue 3 1167-1176, Copyright © 1995 by American Association of Immunologists

ARTICLES

MHC class I signaling in T cells leads to tyrosine kinase activity and PLC-gamma 1 phosphorylation

S Skov, N Odum and MH Claesson
Department of Medical Anatomy, Panum Institute, University of Copenhagen, Denmark.

We have studied the biochemical signal pathway leading to a rise in intracellular free calcium concentration ([Ca2+]i) following cross- linking of MHC class I (MHC-I) molecules on human T leukemic Jurkat cells. Evidence is presented that MHC-I signaling is dependent on tyrosine kinase activity before the observed increase in [Ca2+]i. Thus, tyrosine phosphorylation was detected within 5 s after MHC-I cross- linking, whereas an increase in [Ca2+]i was observed after a lag period of 30 s. Moreover, an inhibitor of tyrosine kinases, herbimycin A, almost completely blocked MHC-I-induced tyrosine phosphorylation and the subsequent calcium response. The early tyrosine kinase activity was found to be dependent on expression of the TCR/CD3 complex and the CD45 molecule on the surface of the T cells. Furthermore, MHC-I cross- linking was shown to tyrosine phosphorylate PLC-gamma 1 (phospholipase C-gamma 1). Collectively, these results indicate that the MHC-I signaling pathway is linked to activation of tyrosine kinase(s) in Jurkat cells.


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