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Vol. 289, Issue 3, 1293-1300, June 1999
Georgetown University Medical Center, Department of Surgery,
Washington, DC
The aim of this study was to determine the effect of ethanol on
endothelial nitric oxide synthase (eNOS), the enzyme responsible for
the production of the important vasoactive agent nitric oxide. The
effect of ethanol (0.8-160 mM) on both basal and flow-stimulated eNOS
activity was determined using cultured bovine aortic endothelial cells
(EC). In "static" EC ethanol dose-dependently increased basal eNOS
activity with a maximum response (~2.0-fold increase) achieved at 40 mM in the absence of any effect on cell viability or nitric oxide
synthase protein expression. Pertussis toxin (PTX) pretreatment
significantly inhibited the ethanol-induced increase in basal eNOS
activity. EC exposed to steady laminar flow exhibited a flow- and
time-dependent increase in eNOS activity. Ethanol significantly
enhanced the laminar flow-induced eNOS response from 0.62 ± 0.1 to 1.06 ± 0.06 pmol [14C]citrulline/mg/min, a
response that was inhibited by PTX. PTX-catalyzed ribosylation of Gi
substrates, an index of G-protein functional activity, was increased in
laminar flow-exposed EC compared with static controls and was further
enhanced by ethanol treatment. Likewise, EC exposed to low (~0.5
dynes/cm2) and high (~12 dynes/cm2) pulsatile
flow demonstrated increased eNOS activity, an effect that was
associated with increased PTX-catalyzed ribosylation of Gi
substrates. Ethanol enhanced the low flow response in a PTX-sensitive
manner. These data demonstrate a stimulatory effect of ethanol on basal
and flow-stimulated eNOS activity, mediated in part by a mechanism
involving a PTX-sensitive G protein.
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