Premium
Bisindolylmaleimide inhibits the PMA‐induced down‐regulation of collagen synthesis in fibroblasts
Author(s) -
Park RangWoon,
Kim InSan,
Jo JoonSeung
Publication year - 1996
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549600201582
Subject(s) - protein kinase c , bisindolylmaleimide , phorbol , chemistry , fibroblast , signal transduction , microbiology and biotechnology , biochemistry , biology , in vitro
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.