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Titolo:
Phenylarsine oxide inhibits nitric oxide synthase in pulmonary artery endothelial cells
Autore:
Su, YC; Block, ER;
Indirizzi:
Univ Florida, Coll Med, Dept Med, Gainesville, FL USA Univ Florida Gainesville FL USA Coll Med, Dept Med, Gainesville, FL USA Malcom Randall Vet Affairs Med Ctr, Res Serv, Gainesville, FL USA Malcom Randall Vet Affairs Med Ctr Gainesville FL USA ainesville, FL USA
Titolo Testata:
FREE RADICAL BIOLOGY AND MEDICINE
fascicolo: 2, volume: 28, anno: 2000,
pagine: 167 - 173
SICI:
0891-5849(20000115)28:2<167:POINOS>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-TYROSINE PHOSPHORYLATION; CATALYTIC ACTIVITY; SHEAR-STRESS; LOCALIZATION; CAVEOLIN-1; KINASE; THIOLS;
Keywords:
nitric oxide synthase; endothelial cell; pulmonary; phenylarsine oxide; free radicals;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
24
Recensione:
Indirizzi per estratti:
Indirizzo: Block, ER Vet Affairs Med Ctr, Res Serv 151, 1601 SW Archer Rd, Gainesville, FL 32608 USA Vet Affairs Med Ctr 1601 SW Archer Rd Gainesville FL USA 32608 A
Citazione:
Y.C. Su e E.R. Block, "Phenylarsine oxide inhibits nitric oxide synthase in pulmonary artery endothelial cells", FREE RAD B, 28(2), 2000, pp. 167-173

Abstract

The role of protein tyrosine phosphorylation during regulation of NO synthase (eNOS) activity in endothelial cells is poorly understood. Studies to define this role have used inhibitors of tyrosine kinase or tyrosine phosphatase (TP). Phenylarsine oxide (PAO), an inhibitor of TP, has been reported to bind thiol groups, and recent work from our laboratory demonstrates thateNOS activity depends on thiol groups at its catalytic site. Therefore, wehypothesized that PAO may have a direct effect on eNOS activity. To test this, we measured (i) TP and eNOS activities both in total membrane fractions and in purified eNOS prepared from porcine pulmonary artery endothelial cells and (ii) sulfhydryl content and eNOS activity in purified bovine aortic eNOS expressed in Escherichia coli. High TP activity was detected in total membrane fractions, but no TP activity was detected in purified eNOS fractions. PAO caused a dose-dependent decrease in eNOS activity in total membrane and in purified eNOS fractions from porcine pulmonary artery endothelial cells, even though the latter had no detectable TP activity. PAO also caused a decrease in sulfhydryl content and eNOS activity in purified bovine eNOS. The reduction in eNOS sulfhydryl content and the inhibitory effect of PAO on eNOS activity were prevented by dithiothreitol, a disulfide-reducingagent. These results indicate that (i) PAO directly inhibits eNOS activityin endothelial cells by binding to thiol groups in the eNOS protein and (ii) results of studies using PAO to assess the role of protein tyrosine phosphorylation in regulating eNOS activity must be interpreted with great caution. (C) 2000 Elsevier Science Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/09/20 alle ore 06:52:52