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Brain ischemia induces serine phosphorylation of neuronal nitric oxide synthase by Ca2+/calmodulin-dependent protein kinase II in rat hippocampus

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Acta Pharmacologica Sinica 2004年第5期25卷 75-80页

作者： Xue-bo YAN, Fan-jie MENG, Bo SONG, Guang-yi ZHANG2Research Center for Biochemistry and Molecular Biology, Xuzhou Medical College, Xuzhou 221002, China Research Center for Biochemistry and Molecular Biology Xuzhou Medical College Xuzhou 221002

AIM: To investigate whether brain ischemia induces serine phosphorylation of neuronal nitric oxide synthase(nNOS) by Ca2+/calmodulin-dependent protein kinase II (CaMKII) and the interaction between CaMKIIa and nNOSin rat hippocampus. METHODS: Brain ischemia was induced by bilateral carotid artery occlusion *** and the interaction of proteins were studied by immunoprecipitation and immunoblotting. Weinvestigated during brain ischemia serine phosphorylation and amount of nNOS in crude membranes fraction (P)and cytosolic fraction (S), interaction between CaMKIIa and nNOS, and the effects of 1-[N,O-bis-(5-isoquinolinesulfonyl)-N-methyl-L-tyrosyl]-4-phenylpiperazine (KN-62, a selective inhibitor of CaMKII) on phos-phorylation and the interaction of proteins in P. RESULTS: Serine phosphorylation of nNOS in P increased persis-tently during brain ischemia, and 15 min ischemia-induced serine phosphorylation of nNOS was attenuated signifi-cantly by KN-62. But there was no serine phosphorylation of nNOS in S. The distributions of nNOS were notaffected by ischemia and KN-62. However, the binding levels of both CaMKIIa with nNOS and Thr286autophosphorylated CaMKIIa with nNOS increased after ischemia, and were diminished by KN-62. CONCLUSION:CaMKII interacted with nNOS and regulated serine phosphorylation of nNOS during brain ischemia.

关键词： serine phosphorylation nitric oxide synthase calmodulin kinase KN 62 brain ischemia hippo-campus

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Ca2+-dependent regulation of cardiac Ca2+ channel and its molecular mechanism

Ca2+-dependent regulation of cardiac Ca2+ channel and its mo...

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中国生理学会第24届全国会员代表大会暨生理学学术大会

作者：郝丽英中国医科大学药学院药物毒理学教研室

Voltage-gated Ca2+channels（CaVs）control cellular Ca2+entry in response to changes in the membrane potential,and play essential roles in the generation of cardiac action potentials,excitation-contraction coupling,hormone and neurotransmitter release and activity-dependent gene *** of the interesting characteristics of Cavs is that their openings are regulated by Ca2+,the ion that passes through the channels,including both a negative mechanism and a positive feedback mechanism:Ca2+-dependent facilitation（CDF）and inactivation（CDI）.CDF will enhance channel opening when basal Ca2+levels are increased or repeated transient depolarization *** will enforce channel closing when the entry of Ca2+is further *** is believed that both CDF and CDI require calmodulin（Ca M）to bind to theα1 subunit of *** Ca M molecule is composed of two connected lobes,the N-terminal lobe（N-lobe）and the C-terminal lobe（C-lobe）.We detected the binding of Ca M and its C and N-lobe mutants with the Cav1.2 channel at different Ca2+.Our data suggested that at low and middle levels of[Ca2+],Cav1.2 channel may usually bind one Ca M molecule.A Ca2+-dependent increase in the extent of Ca M-bound channel may underlie CDF of the *** Ca2+and Ca M concentrations increased,the channel may bind with the second Ca M molecule,and this may be related to CDI of the *** also investigated the dynamic changes in Cav1.2,Ca M,and Ca MKⅡ（calmodulin-dependent protein kinase）m RNA and protein expression levels in the left ventricles of the heart following in vitro MI（myocardial ischemia）in *** were no observable differences in the Cav1.2 m RNA and protein levels at the early stages of MI,but these levels decreased at MI-2 *** the m RNA and protein levels of Ca M increased at MI-6h,peaked at MI-24h,and then reduced to normal levels at *** MKⅡ m RNA and protein levels decreased at MI-6h and reached their lowest level at *** data demonstrate that the

关键词： calcium channel calmodulin calmodulin kinase binding

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