Redox Regulatory Mechanism of Transnitrosylation by Thioredoxin
نویسندگان
چکیده
منابع مشابه
Redox Regulatory Mechanism of Transnitrosylation by Thioredoxin*
Transnitrosylation and denitrosylation are emerging as key post-translational modification events in regulating both normal physiology and a wide spectrum of human diseases. Thioredoxin 1 (Trx1) is a conserved antioxidant that functions as a classic disulfide reductase. It also catalyzes the transnitrosylation or denitrosylation of caspase 3 (Casp3), underscoring its central role in determining...
متن کاملRedox Regulatory Mechanism of Transnitrosylation by Thioredoxin*□S
Transnitrosylation and denitrosylation are emerging as key post-translational modification events in regulating both normal physiology and a wide spectrum of human diseases. Thioredoxin 1 (Trx1) is a conserved antioxidant that functions as a classic disulfide reductase. It also catalyzes the transnitrosylation or denitrosylation of caspase 3 (Casp3), underscoring its central role in determining...
متن کاملCell growth stimulation by the redox protein thioredoxin occurs by a novel helper mechanism.
Thioredoxins are a class of low molecular weight redox proteins that undergo reversible reduction-oxidation of two active-site cysteine residues with reduction catalyzed by the NADPH-dependent flavoenzyme thioredoxin reductase. Human thioredoxin has been shown to be identical to a previously reported leukemic cell growth factor. We now report that recombinant human thioredoxin added to minimal ...
متن کاملDistinction of thioredoxin transnitrosylation and denitrosylation target proteins by the ICAT quantitative approach.
S-Nitrosylation is a reversible PTM for regulating protein function. Thioredoxin-1 (Trx1) catalyzes either transnitrosylation or denitrosylation of specific proteins, depending on the redox status of the cysteines within its conserved oxidoreductase CXXC motif. With a disulfide bond formed between the two catalytic cysteines, Trx1 is not only inactive as a denitrosylase, but it may also be nitr...
متن کاملRole of the redox protein thioredoxin in cytoprotective mechanism evoked by (-)-deprenyl.
Through the inhibition of monoamine oxidase type B (MAO-B), (-)-deprenyl (selegiline) prevents the conversion of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) to the toxic metabolite 1-methyl-4-phenylpyridinium ion (MPP+) and also prevents the neurotoxicity in the dopaminergic neurons in animal models. Cumulative observations suggest that selegiline may also protect against MPP+-induced n...
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ژورنال
عنوان ژورنال: Molecular & Cellular Proteomics
سال: 2010
ISSN: 1535-9476
DOI: 10.1074/mcp.m110.000034