A Protein Kinase C Pseudosubstrate Peptide Blocks G—Protein and Mitogenic Lectin Induced Phosphorylation of the CD3 Antigen in Human T—Lymphocytes View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

1990

AUTHORS

Denis R. Alexander , Jonathan D. Graves , Susan C. Lucas , J. Mark Hexham , Doreen A. Cantrell , Michael J. Crumpton

ABSTRACT

Protein kinase C (PKC) activation occurs upon binding of mitogenic monoclonal antibodies (mAbs) to the antigen receptor complex (Ti-CD3) or CD2 antigen of human T-lymphocytes (Isakov et al., 1987; Truneh et al., 1985; Weiss and Imboden, 1987; Friedrich and Gullberg, 1988; Nel et al., 1987; Alexander and Cantrell, 1989). Activation of T-cell PKC is associated with changes in cell-surface expression of antigens such as CD2 (Cantrell et al., 1988), CD3 (Cantrell et al., 1985) and CD4 (Acres et al., 1986), with the phosphorylation of cytosolic 19kDa and 80kDa proteins (Friedrich and Gullberg, 1988; Friedrich et al., 1988), and with the induction of specific genes, such as the IL-2 recepcor gene, which are required for a proliferative response (Isakov et al., 1987; Crabtree, 1989; Irving et al., 1989). Such data imply, though do not prove, that PKC plays a role in linking signals from Ti-CD3 and CD2 to nuclear events. In contrast, PKC is apparently not required for mediating mitogenic signals via the IL-2 receptor (Mills et al., 1988). More... »

PAGES

253-262

References to SciGraph publications

Book

TITLE

Biology of Cellular Transducing Signals

ISBN

978-1-4612-7866-5
978-1-4613-0559-0

Author Affiliations

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-1-4613-0559-0_26

DOI

http://dx.doi.org/10.1007/978-1-4613-0559-0_26

DIMENSIONS

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