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

Ric Clin Lab. 1989 Jul-Sep;19(3):221-9. doi: 10.1007/BF02871811.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antibodies, Monoclonal / pharmacology
  • Antigens, CD / physiology*
  • Antigens, Differentiation, T-Lymphocyte / physiology*
  • Biological Transport
  • CD2 Antigens
  • CD3 Complex
  • Calcium / metabolism
  • Cells, Cultured
  • Humans
  • Lymphocyte Activation
  • Protein Kinase C / metabolism*
  • Receptors, Antigen, T-Cell / physiology*
  • Receptors, Immunologic / physiology*
  • Signal Transduction / physiology*
  • T-Lymphocytes / physiology*

Substances

  • Antibodies, Monoclonal
  • Antigens, CD
  • Antigens, Differentiation, T-Lymphocyte
  • CD2 Antigens
  • CD3 Complex
  • Receptors, Antigen, T-Cell
  • Receptors, Immunologic
  • Protein Kinase C
  • Calcium