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Biochem J. 1993 Sep 1;294 ( Pt 2):335-7.

Isoenzyme specificity of bisindolylmaleimides, selective inhibitors of protein kinase C.

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  • 1Research Centre, Roche Products Ltd., Welwyn Garden City, Herts, U.K.

Abstract

The protein kinase C (PKC) family of isoenzymes is believed to mediate a wide range of signal-transduction pathways in many different cell types. A series of bisindolylmaleimides have been evaluated as inhibitors of members of the conventional PKC family (PKCs-alpha, -beta, -gamma) and of a representative of the new, Ca(2+)-independent, PKC family, PKC-epsilon. In contrast with the indolocarbazole staurosporine, all the bisindolylmaleimides investigated showed slight selectivity for PKC-alpha over the other isoenzymes examined. In addition, bisindolylmaleimides bearing a conformationally restricted side-chain were less active as inhibitors of PKC-epsilon. Most noticeable of these was Ro 32-0432, which showed a 10-fold selectivity for PKC-alpha and a 4-fold selectivity for PKC-beta I over PKC-epsilon.

PMID:
8373348
PMCID:
PMC1134458
[PubMed - indexed for MEDLINE]
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