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J. Biol. Chem., Vol. 266, Issue 19, 12135-12139, 07, 1991
JP Secrist, L Karnitz and RT Abraham
Ligand-mediated perturbation of the T-cell antigen receptor (TCR) triggers
a rapid increase in phosphoinositide-specific phospholipase C (PLC)
activity in resting T-cells. Although the mechanism by which TCR ligation
regulates PLC activity is unknown, recent studies suggest that coupling of
this receptor complex to PLC activity is dependent on an intermediate
protein tyrosine phosphorylation event(s). In the present study, we
demonstrate that antibody-mediated TCR cross-linkage results in the
tyrosine phosphorylation of PLC-gamma 1. Stimulation of the TCR for 30 s
induced a 4-5-fold increase in the level of PLC activity recovered in
anti-phosphotyrosine (Tyr(P)) antibody immunoprecipitates from stimulated
Jurkat cells. The appearance of PLC activity in the immunoprecipitates
preceded the onset of phosphoinositide hydrolysis in vivo, which began
30-60 s after TCR ligation. Furthermore, the TCR- mediated increase in
anti-Tyr(P) antibody-bound PLC activity was inhibited by staurosporine at
drug concentrations identical with those required for in vivo inhibition of
TCR-dependent phosphoinositide breakdown. Immunoblot analyses demonstrated
that TCR ligation dramatically increased the level of
tyrosine-phosphorylated PLC-gamma 1 present in anti-Tyr(P) antibody
immunoprecipitates from stimulated Jurkat cells. These results strongly
suggest that the TCR complex expressed by Jurkat cells is functionally
coupled to the phosphoinositide-dependent signaling pathway through the
tyrosine phosphorylation of PLC-gamma 1.
T-cell antigen receptor ligation induces tyrosine phosphorylation of phospholipase C-gamma 1
Department of Pharmacology, Mayo Foundation, Rochester, Minnesota 55905.
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