Information de reference pour ce titreAccession Number: | 00043605-200612000-00014.
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Author: | Schulze, P Christian; Liu, Heling; Choe, Elizabeth; Yoshioka, Jun; Shalev, Anath; Bloch, Kenneth D.; Lee, Richard T.
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Institution: | From Cardiovascular Division (P.C.S., J.Y., R.T.L.), Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, Mass; Cardiovascular Research Center (H.L., E.C., K.D.B.), Massachusetts General Hospital, Harvard Medical School, Charlestown, Mass; Department of Medicine (A.S.), University of Wisconsin-Madison, Madison, Wis.
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Title: | |
Source: | Arteriosclerosis, Thrombosis & Vascular Biology. 26(12):2666-2672, December 2006.
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Abstract: | Objective-: Cellular redox balance is regulated by enzymatic and nonenzymatic systems and freely diffusible nitric oxide (NO) promotes antioxidative mechanisms. We show the NO-dependent transcriptional regulation of the antioxidative thioredoxin system.
Methods and Results-: Incubation of rat pulmonary artery smooth muscle cells (RPaSMC) with the NO donor compound S-nitroso-glutathione (GSNO, 100 [mu]mol/L) suppressed thioredoxin-interacting protein (Txnip), an inhibitor of thioredoxin function, by 71+/-18% and enhanced thioredoxin reductase 2.7+/-0.2 fold (n=6; both P<0.001 versus control). GSNO increased thioredoxin activity (1.9+/-0.5-fold after 4 hours; P<0.05 versus control). Promoter deletion analysis revealed that NO suppression of Txnip transcription is mediated by cis-regulatory elements between -1777 and -1127 bp upstream of the start codon. Hyperglycemia induced Txnip promoter activity (3.9+/-0.2-fold; P<0.001) and abolished NO effects (-37.4+/-1.0% at 5.6 mmol/L glucose versus 12.4+/-2.1% at 22.4 mmol/L glucose; P<0.05). Immunoprecipitation experiments demonstrated that GSNO stimulation and mutation of thioredoxin at Cys69, a site of nitrosylation, had no effect on the Txnip/thioredoxin interaction.
Conclusions-: NO can regulate cellular redox state by changing expression of Txnip and thioredoxin reductase. This represents a novel antioxidative mechanism of NO independent of posttranslational protein S-nitrosylation of thioredoxin.
(C) 2006 American Heart Association, Inc.
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Author Keywords: | atherosclerosis; diabetes mellitus; nitric oxide; oxidative stress; thioredoxin.
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Language: | English.
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Document Type: | Vascular Biology.
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Journal Subset: | Clinical Medicine.
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ISSN: | 1079-5642
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NLM Journal Code: | 9505803, B89
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DOI Number: | https://dx.doi.org/10.1161/01.AT...- ouverture dans une nouvelle fenêtre
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