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Titolo:
GPROTEIN KINASE-C MODULATES RECEPTOR-INDEPENDENT ACTIVATION OF ENDOTHELIAL NITRIC-OXIDE SYNTHASE
Autore:
DAVDA RK; CHANDLER LJ; GUZMAN NJ;
Indirizzi:
UNIV FLORIDA,JHMHC,DEPT PHARM,POB 100267 GAINESVILLE FL 32610 UNIV FLORIDA,COLL MED,DIV NEPHROL HYPERTENS & TRANSPLANTAT GAINESVILLE FL 00000 UNIV FLORIDA,COLL MED,DEPT PHARMACOL GAINESVILLE FL 32610
Titolo Testata:
European journal of pharmacology. Molecular pharmacology section
fascicolo: 3, volume: 266, anno: 1994,
pagine: 237 - 244
SICI:
0922-4106(1994)266:3<237:GKMRAO>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
PHORBOL ESTER; MOLECULAR-CLONING; RELAXING FACTOR; SMOOTH-MUSCLE; PHOSPHORYLATION; RELAXATION; CELLS; ACETYLCHOLINE; RELEASE;
Keywords:
PROTEIN KINASE C; ENDOTHELIUM; NITRIC OXIDE SYNTHASE; EDRF (ENDOTHELIUM-DEPENDENT RELAXATION FACTOR); PHORBOL ESTER;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
21
Recensione:
Indirizzi per estratti:
Citazione:
R.K. Davda et al., "GPROTEIN KINASE-C MODULATES RECEPTOR-INDEPENDENT ACTIVATION OF ENDOTHELIAL NITRIC-OXIDE SYNTHASE", European journal of pharmacology. Molecular pharmacology section, 266(3), 1994, pp. 237-244

Abstract

The intracellular regulation of nitric oxide synthase has been the focus of intense investigation. Bioassay studies using vascular rings have suggested that protein kinase C inhibits endothelium-dependent vascular relaxation. However, information regarding the effects of proteinkinase C on the synthesis of nitric oxide in endothelial cells is notavailable. Therefore, we investigated the effects of protein kinase Cto regulate receptor-independent activation of nitric oxide synthase activity in cultured bovine pulmonary artery endothelial cells. Activation of protein kinase C by phorbol 12-myristate 13-acetate or 1,2-dioctanoyl-sn-glycerol inhibited receptor-dependent and receptor-independent nitric oxide synthase activity. The inhibition of nitric oxide synthase by protein kinase C was concentration dependent and markedly blunted by staurosporine. The inhibition of protein kinase C by staurosporine alone enhanced basal nitric oxide synthase activity. Furthermore,depletion of protein kinase C enhanced both basal and agonist-stimulated nitric oxide synthase activity. These studies indicate that protein kinase C modulates the activity of the constitutive Ca2+/calmodulin-dependent endothelial nitric oxide synthase in the basal state and following agonist stimulation through direct inhibition of the enzyme as well as receptor desensitization. These direct regulatory effects of protein kinase C on endothelial nitric oxide synthase activity may haveimportant implications in the physiologic regulation of vascular tone.

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Documento generato il 30/11/20 alle ore 09:57:51