Pharmacological evidence for system-dependent involvement of protein kinase C isoenzymes in phorbol ester-suppressed gap junctional communication

Véronique Cruciani, Trine Husøy, Svein-Ole Mikalsen

Research output: Contribution to journalArticlepeer-review

Abstract

Several phorbol esters are potent activators of protein kinase C. They down-regulate gap junctional intercellular communication and induce phosphorylation of connexin43, but the sensitivity and extent of responses vary much between systems. We asked whether the total protein kinase C enzyme activity or the protein kinase C isoenzyme constitution was of importance for such variations. Some fibroblastic culture systems were compared. It was concluded that the total protein kinase C enzyme activity did not determine the sensitivity to phorbol esters. Furthermore, the use of isotype-specific inhibitors of protein kinase C indicated that protein kinase Cα, δ, and ε may be involved to different extents in different fibroblastic systems in the response to phorbol esters.
Original languageEnglish
Pages (from-to)150-161
Number of pages11
JournalExperimental Cell Research
Volume268
DOIs
Publication statusPublished - Aug 2001
Externally publishedYes

Keywords

  • protein kinase C
  • gap junctional intercellular communication
  • connexin43

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