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© 1995 Oxford University Press

research-article

Lack of an effect of novel inhibitors with high specificity for protein kinase C on the action of the phorbol ester 12-O-tetradecanoylphorbol-13-acetate on mouse skin in vivo

M. Gschwendt, G. Fürstenberger, H. Leibersperger, W. Kittstein, D. Lindner, C. Rudolph 1, H. Barth 1, J. Kleinschroth 1, D. Marmé 1, C. Schächtele 1 and F. Marks

German Cancer Research Center 69120 Heidelberg 79108 Freiburg, Germany
1Gödecke AG 79108 Freiburg, Germany

The inhibitory effects of three novel staurosporine-derived compounds were tested with five different types of protein kinases, including protein kinase C (PKC). IC50 values of two of these compounds were found to be 300 to {succeeds}5000 times lower for PKC{alpha}ß{gamma} (a mixture of the PKC isoeiviymes {alpha}, ß and {gamma}) than for any of the other protein kinases. The inhibitory action of the most selective inhibitor was tested also with the Ca2+-unresponsive PKC isoenzyme {delta} and was found to suppress PKC{alpha}ß{gamma} and PKC differentially. The highly specific PKC inhibitors are active both in cell culture and in vivo. They inhibit the PKC-catalyzed phosphoryla tion of the specific PKC substrate MARCKS in Swiss-3T3 fibroblasts and the okadaic acid-induced edema of the mouse ear. However, the more complex biological processes triggered by the phorbol ester 12-O-tetradecanoylphorbol-13-acetate in mouse skin, such as Inflammation, stimulation of cellular hyperproliferation and tumor promotion, remain largely unaffected upon topical application of these com pounds.


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