Transmembrane signaling via both CD3 and CD2 human T cell surface molecules involves protein kinase-C translocation.

The activation of T lymphocytes by appropriate pairs of anti-CD2 monoclonal antibodies has been shown to involve phospholipase-C and phosphoinositide hydrolysis. In this paper we show that the stimulation of the human cloned leukemic T cell line Jurkat by anti-CD2 as well as anti-CD3 monoclonal antibodies induces translocation from cytosol to cell membrane of protein kinase-C (PKC), which is dependent on the formation of 1,2-diacylglycerol from inositol 4,5-diphosphate. PKC translocation is rapid and transient: the kinetics of enzyme redistribution are similar for CD2 and CD3. These results further stress that CD2 and CD3 T cell activation pathways use similar signal transducing mechanisms.