The activation of protein kinase C is not necessary for the monoclonalantibody‐induced modulation of CD3 and CD4 antigens
- 1 May 1990
- journal article
- research article
- Published by Wiley in European Journal of Immunology
- Vol. 20 (5) , 1197-1200
- https://doi.org/10.1002/eji.1830200539
Abstract
We studied the effect of staurosporine, a potent inhibitor of protein kinase C (PKC) activity, on the phorbol ester‐ or monoclonal antibody (mAb)‐induced modulation of CD3 and CD4 surface antigens. Staurosporine (10−5 M) completely inhibited phorbol ester‐induced modulation but had no effect on that induced by mAb. These results indicate that the down‐regulation of CD3 and CD4 observed after activation of the cells by the corresponding mAb is independent from PKC‐mediated phosphorylations, and thus that the activation of PKC is sufficient but not necessary to induce the modulation of CD3 and CD4 antigens.This publication has 16 references indexed in Scilit:
- Evidence that protein kinase C differentially regulates the human T lymphocyte CD2 and CD3 surface antigensEuropean Journal of Immunology, 1988
- Stimulation and proliferation of CD4+ peripheral blood T lymphocytes induced by an anti‐CD4 monoclonal antibodyEuropean Journal of Immunology, 1988
- Staurosporine, a potent protein kinase C inhibitor, fails to inhibit 12-O-tetradecanoylphorbol-13-acetate-caused ornithine decarboxylase induction in isolated mouse epidermal cellsBiochemical and Biophysical Research Communications, 1987
- Internalization and cycling of the T cell antigen receptor. Role of protein kinase C.Journal of Biological Chemistry, 1987
- Endocytosis and recycling of the T3-T cell receptor complex. The role of T3 phosphorylation.The Journal of Experimental Medicine, 1987
- Association of phosphorylation of the T3 antigen with immune activation of T lymphocytesNature, 1987
- Internalization of human T lymphocyte receptorsEuropean Journal of Immunology, 1987
- Translocation of protein kinase C during membrane immunoglobulin-mediated transmembrane signaling in B lymphocytes.The Journal of Immunology, 1986
- Activators of protein kinase C down-regulate and phosphorylate the T3/T-cell antigen receptor complex of human T lymphocytes.Proceedings of the National Academy of Sciences, 1985
- Transmembrane signalling by the T cell antigen receptor. Perturbation of the T3-antigen receptor complex generates inositol phosphates and releases calcium ions from intracellular stores.The Journal of Experimental Medicine, 1985