DEVELOPMENT OF A NEW METHOD TO MEASURE PROTEIN KINASE C-MEDIATED SUPEROXIDE PRODUCTION IN CRYOSECTIONS OF FROZEN RAT MESENTERIC ARTERY

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Superoxide has been suggested to play a pivotal role to develop vascular dysfunction seen in patients with cardiovascular disease. It is found that protein kinase C (PKC) induces superoxide production through an activation of NAD(P)H oxidase in vascular cells, although it remains to be clarified which PKC subtypes contribute to such response. Superoxide production was estimated using ethidium fluorescence in cryosections from frozen rat mesenteric artery. The potent PKC activator phorbol 12, 13-dibutylate (PDBu) did not modify superoxide preduction in a solution containing phosphate buffered saline while it enhanced superoxide production in a mimicked intracellular ionic solution (including Mg-ATP, referred to intracellular solution). In the intracellular solution, the NAD(P)H oxidase substrates NADPH and NADH enhanced superoxide prodution and Ca^<2+> (0.3μM) increased the superoxide production in the presence of NADH plus NADPH. PDBu enhanced the supreoxide prodution in the absence and presence of Ca^<2+> but its effect was storonger in the presence of Ca^<2+> than in the absence of Ca^<2+>. The PDBu-induced increase in superoxide producitons was abolished by the NAD(P)H oxidase inhibitor apocynin diphenyleneiodonium chloride. In conclusion, we developed a new method to study the action of PKC subtypes in superoxide production in cryosections of frozen rat mesenteric artery. Using this methods, we found thatPDBu induces superoxide prodution through an activation of NAD(P)H oxidase. It is also suggested that both cPKCs and nPKCs subtypes contribute to the PDBu-induced vascularsuperoxide production .
名古屋市立大学の論文
2008-03-31

DEVELOPMENT OF A NEW METHOD TO MEASURE PROTEIN KINASE C-MEDIATED SUPEROXIDE PRODUCTION IN CRYOSECTIONS OF FROZEN RAT MESENTERIC ARTERY

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