Methylglyoxal Causes Dysfunction of Thioredoxin and Thioredoxin Reductase in Endothelial Cells

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Cloning of thioredoxin h reductase and characterization of the thioredoxin reductase-thioredoxin h system from wheat.

Thioredoxins h are ubiquitous proteins reduced by NADPH- thioredoxin reductase (NTR). They are able to reduce disulphides in target proteins. In monocots, thioredoxins h accumulate at high level in seeds and show a predominant localization in the nucleus of seed cells. These results suggest that the NTR-thioredoxin h system probably plays an important role in seed physiology. To date, the study...

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Thioredoxin, thioredoxin reductase and NADPH form the thioredoxin system and are the major cellular protein disulphide reductase. We report here that Escherichia coli thioredoxin and thioredoxin reductase interact with unfolded and denatured proteins, in a manner similar to that of molecular chaperones that are involved in protein folding and protein renaturation after stress. Thioredoxin and/o...

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NADPH-Dependent Thioredoxin Reductase and a New Thioredoxin from Wheat

An albumin fraction extracted from wheat flour contains thioredoxin reductase (Mr = 65,000) and a heat-stable thioredoxin (Mr = 15,000) which are separated on DEAE cellulose and further purified by gel filtration. W heat thioredoxin stimulates E. coli ribonucleotide reductase but not chloroplast fructose-bis-phosphatase. The enzyme is NADPH-dependent (Km = 3.2 X 10 -6 m) . In presence of the th...

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The thioredoxin-thioredoxin reductase system: over-expression in human cancer.

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Recent publications make it evident that the thioredoxin± thioredoxin reductase system has come of age. The four minireviews presented here attempt to put this field in perspective. The system was first recognized in the early 1960s as the reductant of methionine sulfoxide and PAPS (3 0-phosphoadenosine-5 0-phosphosulfate) in yeast and of ribonucleotides in Escherichia coli [1±3]. It became cle...

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ژورنال

عنوان ژورنال: Journal of Pharmacological Sciences

سال: 2009

ISSN: 1347-8613,1347-8648

DOI: 10.1254/jphs.09131fp