Heterogeneity of the regulation of phospholipase C by phorbol esters in T lymphocytes

S. G. Ward (Lead / Corresponding author), D. A. Cantrell

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19 Citations (Scopus)


In many cells, protein kinase C (PKC) activation inhibits cellular phospholipase C thereby preventing receptor-mediated phosphatidylinositol (PI) metabolism. In T lymphocytes, the T cell antigen receptor (Ti)/CD3 complex regulates PI hydrolysis and we have exmained the consequences of PKC activation on Ti/CD3-mediated PI metabolism in human peripheral blood-derived T lymphocytes (T lymphoblasts) and the leukemic T cell line Jurkat. In Jurkat cells, PI metabolism after Ti/CD3 stimulation, is inhibited by PKC activation. PKC activation also inhibits calcium-induced PI metabolism in permeabilized Jurkat cells. In marked contrast, PI metabolism after Ti/CD3 stimulation in T lymphoblasts, is not inhibited by PKC activation. Moreover, in permeabilized T lymphoblasts PI metabolism can be induced by calcium in synergy with guanine 5'-O-(3-thiotrisphosphate) via a PKC-insensitive mechanism. The different effect of PKC stimulation on PI metabolism in Jurkat cells and T lymphoblasts reveals heterogeneity of PLC regulation in T lymphocytes. The data also indicate that the role of PKC as a regulatory of Ti/CD3 signal transduction can differ depending on cell type.

Original languageEnglish
Pages (from-to)3523-3528
Number of pages6
JournalJournal of Immunology
Issue number9
Publication statusPublished - 1 May 1990

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology


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