The activity of a beta subtype of protein kinase C purified from nuclei of human neutrophils is enhanced by treatment with phorbol 12-myristate 13-acetate.

Two protein kinase C isoenzymes were partially purified from the nuclei of human neutrophils, and identified as beta and alpha subtypes. Treatment of neutrophils with phorbol 12-myristate 13-acetate (PMA) caused a 3.8-fold increase of nuclear beta PKC activity, while a minor increase of alpha PKC was observed. This selective activation of beta PKC could help to understand the molecular events involved in phorbol ester-induced cellular modifications.