Differential dependence on protein kinase C of arachidonic acid metabolism stimulated by hydrogen peroxide and by zymosan in the alveolar macrophage

Peter H S Sporn*, Teresa M. Marshall, Marc Peters-Golden

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

16 Scopus citations

Abstract

The dependence on protein kinase C (PKC) of arachidonic acid (AA) metabolism stimulated by the biologically important oxidant H2O2 as compared to zymosan particles, was investigated in the rat alveolar macrophage. The PKC inhibitor staurosporine markedly reduced AA release and eicosanoid synthesis stimulated by zymosan, but only slightly inhibited AA release and metabolism induced by H2O2. Furthermore, in macrophages depleted of PKC by extended exposure to phorbol 12-myristate 13-acetate, AA release in response to zymosan was greatly inhibited, whereas that stimulated by H2O2 was attenuated to a significantly lesser degree. Thus, zymosan-stimulated AA metabolism requires active PKC, whereas H2O2-induced metabolism is largely PKC-independent. This provides direct evidence for the existence of two pathways of agonist-stimulated AA metabolism, which differ in their dependence on PKC, in the alveolar macrophage.

Original languageEnglish (US)
Pages (from-to)187-191
Number of pages5
JournalBiochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism
Volume1047
Issue number2
DOIs
StatePublished - Nov 12 1990

Keywords

  • Alveolar macrophage
  • Arachidonic acid
  • Hydrogen peroxide
  • Phorbol myristate acetate
  • Protein kinase C
  • Staurosporine

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Endocrinology

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