Selective inhibition of collagen synthesis by okadaic acid in cultured human fibroblasts.
To determine whether protein phosphatases can affect collagen synthesis, we examined the effect of okadaic acid, a potent specific inhibitor of protein phosphatases 1 and 2A, on collagen synthesis. Okadaic acid significantly decreased the [3H]proline incorporation into the collagenase-digestible protein and the percent collagen synthesis. These effects were synergistic with phorbol myristate acetate (PMA). The time course study showed that okadaic acid inhibited collagen synthesis after a 12 h treatment while PMA inhibited at 3 h. Down-regulation of protein kinase C by chronic treatment with PMA did not abrogate the okadaic acid-dependent inhibition. These results provide evidence for the involvement of protein phosphatases in the regulation of collagen synthesis.
Kim
I S
IS
Department of Biochemistry, School of Medicine, Kyungpook National University, Taegu, Korea.
Park
R W
RW
Sohn
K Y
KY
Jo
J S
JS
D002460:Cell Line; D002478:Cells, Cultured; D003094:Collagen / Q000096:biosynthesis*; D004988:Ethers, Cyclic / Q000494:pharmacology*; D005347:Fibroblasts / Q000378:metabolism*; D006801:Humans; D066298:In Vitro Techniques; D019319:Okadaic Acid; D016212:Transforming Growth Factor beta / Q000494:pharmacology
D004988:Ethers, Cyclic; D016212:Transforming Growth Factor beta; D019319:Okadaic Acid; D003094:Collagen