A protein kinase C translocation inhibitor as an isozyme-selective antagonist of cardiac function

John A. Johnson, Mary O. Gray, Che Hong Chen, Daria Mochly-Rosen

Research output: Contribution to journalArticle

336 Scopus citations


Protein kinase C (PKC) isozymes translocate to unique subcellular sites following activation. We previously suggested that translocation of activated isozymes is required for their function and that in addition to binding to lipids, translocation involves binding of the activated isozymes to specific anchoring proteins (receptors for activated protein kinase C. Using cultured cardiomyocytes we identified inhibitors, the V1 fragment of εPKC (εV1), and an 8-amino acid peptide derived from it that selectively inhibited the translocation of εPKC. Inhibition of εPKC translocation but not inhibition of δ or βPKC translocation specifically blocked phorbol ester- or norepinephrine-mediated regulation of contraction. These isozyme-selective translocation inhibitors provide novel tools to determine the function of individual PKC isozymes in intact cells.

Original languageEnglish (US)
Pages (from-to)24962-24966
Number of pages5
JournalJournal of Biological Chemistry
Issue number40
StatePublished - Oct 15 1996
Externally publishedYes


ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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