The CD4/CD8:p56lck complex in T lymphocytes: a potential mechanism to regulate T-cell growth

Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire
C E RuddS F Schlossman

Abstract

The CD4 and CD8 antigens on the surface of T cells appear to bind to major histocompatibility complex (MHC) class II and I antigens, respectively. These receptors have also been found to regulate T cell growth in a manner independent of MHC recognition. In this report, we describe recent work showing that the CD4 and CD8 receptors are coupled to a protein-tyrosine kinase, p56lck, from T lymphocytes. The p56lck protein is a member of the src family, which plays a crucial role in the activation and transformation of various mammalian cells. The CD4/CD8:p56lck complex is catalytically active as shown by its ability to phosphorylate at 55-60 kDa. Two-dimensional, nonequilibrium gel electrophoresis demonstrated the similarity of p56lck associated with the CD4 and CD8 antigens. Detergents were found to vary in their ability to solubilize the CD4:p56lck complex in a catalytically active form. We further demonstrated by in vitro phosphorylation that members of the CD3 complex including the gamma, delta, and epsilon chains, as well as a putative zeta subunit can be phosphorylated at tyrosyl residues by the CD4/CD8:p56lck complex. Thus, this interaction may play an important role in the activation of T cells, and may mediate the cooperat...Continue Reading

Citations

Apr 12, 1994·Proceedings of the National Academy of Sciences of the United States of America·T TanakaC Morimoto
Jun 1, 1991·The Journal of Experimental Medicine·K M AbrahamR M Perlmutter
Jun 28, 2003·Transplantation·Majed M Hamawy
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Oct 21, 2017·Immunogenetics·Fany BlancEmmanuelle Bourneuf
Dec 20, 2020·Veterinary Immunology and Immunopathology·Yuko Kato-MoriKatsuro Hagiwara
Oct 15, 2020·International Journal of Molecular Sciences·Nicholas J ChandlerMatthew E Call
Aug 23, 1993·Biochimica Et Biophysica Acta·C E RuddM Yamamoto

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