Protein kinase C-β and -δ Isoenzymes promote arachidonic acid production and proliferation of MonoMac-6 cells

Zoltán Griger, Edit Páyer, Ildikó Kovács, Balázs I. Tóth, László Kovács, Sándor Sipka, Tamás Bíró

Research output: Article

12 Citations (Scopus)

Abstract

In this study, we investigated the putative roles of certain protein kinase C (PKC) isoenzymes in the regulation of proliferation and arachidonic acid (AA) release in the human monocytoid MonoMac-6 cell line. Experiments employing specific PKC inhibitors and molecular biological methods (RNA-interference, recombinant overexpression) revealed that the two dominantly expressed isozymes, i.e., the "conventional" cPKCβ and the "novel" nPKCδ, promote AA production and cellular proliferation. In addition, using different phospholipase A2 (PLA2) inhibitors, we were able to show that the calcium-independent iPLA2 as well as diacylglycerol lipase (but not the cytosolic PLA2) function as "downstream" targets of cPKCβ and nPKCδ. In addition, we have also found that, among the other existing PKC isoforms, cPKCα plays a minor inhibitory role, whereas nPKCε and aPKCζ apparently do not regulate these cellular processes. In conclusion, in this paper we provide the first evidence that certain PKC isoforms play pivotal, specific, and (at least partly) antagonistic roles in the regulation of AA production and cellular proliferation of human monocytoid MonoMac-6 cells.

Original languageEnglish
Pages (from-to)1031-1042
Number of pages12
JournalJournal of Molecular Medicine
Volume85
Issue number9
DOIs
Publication statusPublished - szept. 1 2007

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ASJC Scopus subject areas

  • Molecular Medicine
  • Drug Discovery
  • Genetics(clinical)

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