Polymyxin B causes coordinate inhibition of phorbol ester-induced C-kinase activity and proliferation of B lymphocytes

Andre E. Nel, Marie W. Wooten, Pascal J. Goldschmidt-Clermont, Paul J. Miller, Henry C. Stevenson, Robert M. Galbraith

Research output: Contribution to journalArticle

32 Scopus citations

Abstract

Lymphocytes were found to be rich in phospholipid Ca2+-dependent (C-kinase) activity. Addition of polymyxin B (PMB) to in vitro assays of endogenous and exogenous phosphorylation resulted in profound inhibition of C-kinase activity. The phorbol ester 12-o-tetradecanoyl phorbol-13-acetate (TPA) directly activated C-kinase, leading to increased phosphorylation of the same substrates. TPA also stimulated proliferation of B cells as assessed by 3H-thymidine uptake, and PMB strongly inhibited this effect. This coordinate inhibition of TPA-induced phosphorylation and mitogenesis indicates that PMB is a potentially useful inhibitor of C-kinase activity, and that this enzyme may play an important role in mediating B cell responses.

Original languageEnglish (US)
Pages (from-to)1364-1372
Number of pages9
JournalBiochemical and biophysical research communications
Volume128
Issue number3
DOIs
StatePublished - May 16 1985

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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