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

Authors
  • Cruciani, V
  • Husøy, T
  • Mikalsen, S O
Type
Published Article
Journal
Experimental cell research
Publication Date
Aug 15, 2001
Volume
268
Issue
2
Pages
150–161
Identifiers
PMID: 11478841
Source
Medline
License
Unknown

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 C alpha, delta, and epsilon may be involved to different extents in different fibroblastic systems in the response to phorbol esters.

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