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Titolo:
Phosphorylation and activation of the endothelial nitric oxide synthase byfluid shear stress
Autore:
Fisslthaler, B; Dimmeler, S; Hermann, C; Busse, R; Fleming, I;
Indirizzi:
Univ Frankfurt Klinikum, Inst Kardiovask Physiol, D-60590 Frankfurt, Germany Univ Frankfurt Klinikum Frankfurt Germany D-60590 590 Frankfurt, Germany Univ Frankfurt Klinikum, Med Klin 4, D-60590 Frankfurt, Germany Univ Frankfurt Klinikum Frankfurt Germany D-60590 590 Frankfurt, Germany
Titolo Testata:
ACTA PHYSIOLOGICA SCANDINAVICA
fascicolo: 1, volume: 168, anno: 2000,
pagine: 81 - 88
SICI:
0001-6772(200001)168:1<81:PAAOTE>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
CELL ADHESION MOLECULE-1; TYROSINE PHOSPHORYLATION; CALCIUM; MECHANOTRANSDUCTION; CALMODULIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
27
Recensione:
Indirizzi per estratti:
Indirizzo: Fisslthaler, B Univ Frankfurt Klinikum, Inst Kardiovask Physiol, Theodor-Stern-Kai 7, D-60590 Frankfurt, Germany Univ Frankfurt Klinikum Theodor-Stern-Kai 7 Frankfurt Germany D-60590
Citazione:
B. Fisslthaler et al., "Phosphorylation and activation of the endothelial nitric oxide synthase byfluid shear stress", ACT PHYSL S, 168(1), 2000, pp. 81-88

Abstract

Fluid shear stress activates the endothelial nitric oxide (NO) synthase (eNOS) by a mechanism which does not require an increase in the intracellularconcentration of free Ca2+ ([Ca2+](i)), and is sensitive to several kinaseinhibitors. Although phosphorylation of eNOS has been suggested to regulate enzyme activity, the mechanism of eNOS activation is still unclear. Here we demonstrate that fluid shear stress elicits the phosphorylation of eNOS on tyrosine and serine residues. Inhibition of phosphatidylinositol 3-kinase (PI3K), using wortmannin or a dominant negative mutant of its downstream target, Akt (protein kinase B), prevented the maintained serine phosphorylation and activation of eNOS. Enhancing eNOS phosphorylation by inhibiting serine/threonine phosphatases, increased eNOS activity by approximately twofold, as assessed by the accumulation of intracellular cyclic GMP, without increasing the intracellular concentration of free Ca2+. These data suggest that shear stress activates a pathway involving PI3K and the serine/threonine kinase Akt, which phosphorylates eNOS. This phosphorylation directly increases eNOS activity at resting [Ca2+](i), thus rendering the shear stress-induced activation of eNOS apparently Ca2+-independent.

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Documento generato il 10/07/20 alle ore 12:07:26