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• W2084059091 abstract "An alternative in vivo assay, based on growth inhibition of yeast expressing an individual mammalian protein kinase C (PKC) isoform (proportional to the degree of PKC activation), was used to characterize the activities of phorbol-12-myristate-13-acetate (PMA) and its analogues on classical (α and βI), novel (δ and η) and atypical (ζ) PKC isoforms. Effects of PMA, 4α-PMA, phorbol-12-myristate-13-acetate-4-O-methyl-ether (MPMA), phorbol-12-monomyristate (PMM), phorbol-12,13-diacetate (PDA), phorbol-13-monoacetate (PA), phorbol-12,13-dibutyrate (PDB), phorbol-12,13-didecanoate (PDD) and 12-deoxyphorbol-13-phenylacetate-20-acetate (dPPA), on growth of yeast expressing individual PKC isoforms was determined. PMA-induced growth inhibition on all isoforms tested (except on PKC-ζ). PDD and PDB presented an efficacy similar to PMA; the other PMA-analogues presented lower efficacies. MPMA and 4α-PMA stimulated growth of yeast expressing classical PKCs and reduced the PMA-induced growth inhibition, effects similar to those exhibited by the PKC inhibitors chelerythrine and R-2,6-diamino-N-[[1-(1-oxotridecyl)-2-piperidinyl]methyl]-hexanamide dihydrochloride (NPC 15437). This study reveals that phorbol esters differ on their potency to activate a given PKC isoform, and presents their isoform-selectivity. Furthermore, MPMA and 4α-PMA caused effects similar to those expected from PKC inhibition." @default.
• W2084059091 created "2016-06-24" @default.
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• W2084059091 date "2004-05-01" @default.
• W2084059091 modified "2023-10-17" @default.
• W2084059091 title "Characterization of phorbol esters activity on individual mammalian protein kinase C isoforms, using the yeast phenotypic assay" @default.
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• W2084059091 doi "https://doi.org/10.1016/j.ejphar.2004.03.035" @default.
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