Abstract
Phorbol esters, tetradecanoylphorbolacetate, sapintoxin-A, 12-deoxyphorbol-phenylacetate, 12-deoxyphorbol-phenylacetate-20-acetate, thymeleatoxin and resiniferatoxin were investigated for their abilities to activate the PKC-isotypes alpha, beta 1, gamma, delta and epsilon. PKC-isotypes were grouped into two classes on the basis of Ca2+ requirements for activation by phorbol esters; alpha, beta 1, and gamma being Ca(2+)-dependent forms and delta and epsilon being Ca(2+)-independent. PKC-isotype selective activation by phorbol esters was observed in that SAPA failed to activate PKC-delta up to a concentration of 1000 ng.ml-1 and DOPPA only activated PKC-beta 1 over the same range of concentrations.
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