The Overexpression Catalase Reduces NO-Mediated Inhibition of Endothelial NO Synthase
نویسندگان
چکیده
منابع مشابه
Spironolactone Inhibits NADPH Oxidase-Mediated Oxidative Stress and Dysregulation of the Endothelial NO Synthase in Human Endothelial Cells
Accumulating evidence indicates that aldosterone plays a critical role in the mediation of oxidative stress and vascular damage. NADPH oxidase has been recognized as a major source of oxidative stress in vasculature. However, the relation between NADPH oxidase in aldosterone-mediated oxidative stress in endothelial cells remains to be ascertained. The present study aimed to investigate the rel...
متن کاملSpironolactone Inhibits NADPH Oxidase-Mediated Oxidative Stress and Dysregulation of the Endothelial NO Synthase in Human Endothelial Cells
Accumulating evidence indicates that aldosterone plays a critical role in the mediation of oxidative stress and vascular damage. NADPH oxidase has been recognized as a major source of oxidative stress in vasculature. However, the relation between NADPH oxidase in aldosterone-mediated oxidative stress in endothelial cells remains to be ascertained. The present study aimed to investigate the rel...
متن کاملspironolactone inhibits nadph oxidase-mediated oxidative stress and dysregulation of the endothelial no synthase in human endothelial cells
accumulating evidence indicates that aldosterone plays a critical role in the mediation of oxidative stress and vascular damage. nadph oxidase has been recognized as a major source of oxidative stress in vasculature. however, the relation between nadph oxidase in aldosterone-mediated oxidative stress in endothelial cells remains to be ascertained. the present study aimed to investigate the rele...
متن کاملThioredoxin overexpression prevents NO-induced reduction of NO synthase activity in lung endothelial cells.
We recently reported that nitric oxide (NO) induces posttranscriptional modulation of lung endothelial cell NO synthase (ecNOS) that results in loss of activity. The loss of activity can be reversed by the redox regulatory proteins thioredoxin (Thx)/thioredoxin reductase (Thx-R). The present study was designed to examine whether diminished expression of endogenous Thx and Thx-R may account for ...
متن کاملHistone deacetylase 1 reduces NO production in endothelial cells via lysine deacetylation of NO synthase 3.
The lysine acetylation state of nonhistone proteins may be regulated through histone deacetylases (HDACs). Evidence suggests that nitric oxide (NO) synthase 3 (NOS3; endothelial NOS) is posttranslationally lysine acetylated, leading to increased NO production in the endothelium. We tested the hypothesis that NOS3 is lysine acetylated and that upregulated HDAC1-mediated deacetylation leads to re...
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ژورنال
عنوان ژورنال: IUBMB Life (International Union of Biochemistry and Molecular Biology: Life)
سال: 2002
ISSN: 1521-6543,1521-6551
DOI: 10.1080/15216540215679