MV Wenzl

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Aldehyde dehydrogenase-2 (ALDH2) catalyzes the bioactivation of nitroglycerin (glyceryl trinitrate, GTN) in blood vessels, resulting in vasodilation by nitric oxide (NO) or a related species. Because the mechanism of this reaction is still unclear we determined the three-dimensional structures of wild-type (WT) ALDH2 and of a triple mutant of the protein(More)
BACKGROUND AND PURPOSE L-gulonolactone oxidase-deficient (Gulo((-/-))) mice were used to study the effects of ascorbate deficiency on aortic relaxation by nitroglycerin (GTN) with focus on changes in the expression and activity of vascular aldehyde dehydrogenase-2 (ALDH2), which catalyses GTN bioactivation. EXPERIMENTAL APPROACH Ascorbate deficiency was(More)
Mitochondrial aldehyde dehydrogenase-2 (ALDH2) plays an essential role in nitroglycerin (GTN) bioactivation, resulting in formation of NO or a related activator of soluble guanylate cyclase. ALDH2 denitrates GTN to 1,2-glyceryl dinitrate and nitrite but also catalyzes reduction of GTN to NO. To elucidate the relationship between ALDH2-catalyzed GTN(More)
Background Aldehdyde dehydrogenase-2 (ALDH2) is essential for the detoxification of ethanol in the liver but also catalyzes vas-cular bioactivation of nitroglycerin (glycerol trinitrate, GTN) to its active metabolite nitric oxide (NO), which causes vasodilation through accumulation of cyclic GMP. The clinical use of GTN as a vasodilator is hampered by loss(More)
Background The East Asian variant of mitochondrial aldehyde dehy-drogenase (ALDH2) exhibits significantly reduced dehy-drogenase, esterase and nitroglycerin (GTN) reductase activities [1]. The small molecule Alda-1 was reported to partly restore low acetaldehyde dehydrogenase activity of this variant [2]. In the present study we compared the wild-type(More)
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