Resveratrol preferentially inhibits protein kinase C-catalyzed phosphorylation of a cofactor-independent, arginine-rich protein substrate by a novel mechanism

Research was conducted to investigate the effects of resveratrol on protein kinase C (PKC)-catalyzed phosphorylation of the cofactor-independent substrate protamine sulfate which is polybasic protein that activates PKC via a novel mechanism. Results indicate that the efficacy of resveratrol against cellular PKC may reflect antagonism of the phosphorylation of arginine-rich PKC substrates that bear resemblance to protamine sulfate in their interactions with PKC.