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Title: Selective inhibition of collagen synthesis by okadaic acid in cultured human fibroblasts. Author: Kim IS, Park RW, Sohn KY, Jo JS. Journal: Biochem Biophys Res Commun; 1994 Feb 28; 199(1):177-82. PubMed ID: 8123009. Abstract: 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.[Abstract] [Full Text] [Related] [New Search]