Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Stimulation of receptor-mediated nitric oxide production by vanadate
Autore:
Hellermann, GR; Flam, BR; Eichler, DC; Solomonson, LP;
Indirizzi:
Univ S Florida, Coll Med, Dept Biochem & Mol Biol, Tampa, FL 33612 USA Univ S Florida Tampa FL USA 33612 Biochem & Mol Biol, Tampa, FL 33612 USA
Titolo Testata:
ARTERIOSCLEROSIS THROMBOSIS AND VASCULAR BIOLOGY
fascicolo: 9, volume: 20, anno: 2000,
pagine: 2045 - 2050
SICI:
1079-5642(200009)20:9<2045:SORNOP>2.0.ZU;2-5
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-TYROSINE PHOSPHORYLATION; FLUID SHEAR-STRESS; ENDOTHELIAL-CELLS; SYNTHASE; ACTIVATION; TRANSLOCATION; CAVEOLIN; AKT; INHIBITORS; KINASES;
Keywords:
nitric oxide; endothelial; vanadate; bradykinin; tyrosine phosphorylation;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
34
Recensione:
Indirizzi per estratti:
Indirizzo: Solomonson, LP Univ S Florida, Coll Med, Dept Biochem & Mol Biol, 12901 Bruce B Downs Blvd,MDC Box 7, Tampa, FL 33612 USA Univ S Florida 12901 Bruce B Downs Blvd,MDC Box 7 Tampa FL USA 33612
Citazione:
G.R. Hellermann et al., "Stimulation of receptor-mediated nitric oxide production by vanadate", ART THROM V, 20(9), 2000, pp. 2045-2050

Abstract

Nitric oxide (NO) production by endothelial cells in response to bradykinin (Bk) treatment was markedly and synergistically enhanced by cotreatment with sodium orthovanadate (vanadate), a phosphotyrosine phosphatase inhibitor. This enhancement was blocked by tyrosine kinase inhibitors. Calcium ionophore- (A23187) activated production of NO was also enhanced by cotreatmentwith vanadate. No significant changes were found in total endothelial NO synthase (eNOS) protein or in eNOS distribution between membrane (caveolae) and cytosolic fractions in response to the various treatments. Vanadate hadno direct effect on eNOS activity, and lysates prepared from cells treatedwith vanadate showed little change in specific activity of eNOS. Western blots of immunoprecipitated eNOS showed the presence of a major tyrosine-phosphorylated protein band at a mass corresponding to approximate to 125 kDa and 2 minor bands corresponding to approximate to 105 and 75 kDa after treatment with vanadate/Bk. No tyrosine phosphorylation of eNOS after treatmentwith vanadate/Bk was observed. Geldanamycin, an inhibitor of heat shock protein 90, also inhibited the enhancement of NO production by vanadate/Bk orvanadate/A23187, and there was an increase in the amount of heat shock protein 90 that coimmunoprecipitated with eNOS after treatment with vanadate/Bk, These results show that there is a clear link between tyrosine phosphorylation and stimulation of eNO production, which does not appear to involve direct modification of eNOS, changes in eNOS levels, or compartmentation, but rather appears to be due to changes in proteins associating with eNOS, thereby enhancing the state of activation of eNOS.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/09/20 alle ore 21:59:37