E. Bazan et al., EFFECTS OF PROTEIN-KINASE-C ACTIVATION ON NOREPINEPHRINE-INDUCED PHOSPHATIDYLINOSITIDE HYDROLYSIS IN INTACT RAT AORTA, European journal of pharmacology. Molecular pharmacology section, 245(2), 1993, pp. 173-177
The purpose of this study was to investigate the role of protein kinas
e C in the regulation of alpha1-adrenoceptor-mediated phosphatidylinos
itide hydrolysis in intact vascular smooth muscle. Phorbol myristate a
cetate (0.1 and 1 muM) and staurosporine inhibited and potentiated, re
spectively, norepinephrine-induced inositol phosphate formation in int
act rat aorta. In contrast, 30 muM prostaglandin F2alpha, which activa
ted protein kinase C to a similar magnitude as 1 muM phorbol myristate
acetate, was without effect on norepinephrine-induced inositol phosph
ate formation. These results suggest that protein kinase C activated i
n response to physiologic agonists, but not in response to phorbol est
ers, may be compartmentalized within the smooth muscle cell.