Bisindolylmaleimide inhibits the PMA-induced down-regulation of collagen synthesis in fibroblasts

Rang Woon Park, In-San Kim, Joon Seung Jo

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

We assessed the role of protein kinase C (PKC) in the regulation of collagen synthesis. Two PKC activators, Phorbol 12-myristate 13-acetate (PMA) and 1-oleyl 2-acetyl-sn-glycerol (OAG), decreased the relative rate of collagen synthesis in a dose- and time-dependent manner in fibroblasts, whereas an inactive phorbol ester, 4α-phorbol didecanoate failed to affect the collagen synthesis. In PKC-depleted cells both PMA and OAG were unable to inhibit collagen synthesis. Bisindolylmaleimide, a specific inhibitor of PKC, completely abrogated PMA-induced inhibition of collagen synthesis in a dose-dependent fashion while two other PKC inhibitors with low specificity, H7 and staurosporin failed to block PMA effect on collagen synthesis. The results provide evidence that collagen synthesis is regulated through the signal pathway involving PKC activation.

Original languageEnglish
Pages (from-to)101-109
Number of pages9
JournalBiochemistry and Molecular Biology International
Volume40
Issue number1
Publication statusPublished - 1996 Oct 17
Externally publishedYes

Fingerprint

Fibroblasts
Acetates
Protein Kinase C
Collagen
Down-Regulation
Glycerol
Protein C Inhibitor
Phorbol Esters
Protein Kinase Inhibitors
bisindolylmaleimide
phorbol-12-myristate
Signal Transduction
Chemical activation

Keywords

  • Bisindolylmaleimide
  • Collagen
  • Protein kinase C

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Genetics

Cite this

Bisindolylmaleimide inhibits the PMA-induced down-regulation of collagen synthesis in fibroblasts. / Park, Rang Woon; Kim, In-San; Jo, Joon Seung.

In: Biochemistry and Molecular Biology International, Vol. 40, No. 1, 17.10.1996, p. 101-109.

Research output: Contribution to journalArticle

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