S-nitrosation of thioredoxin in the nitrogen monoxide/superoxide system activates apoptosis signal-regulating kinase 1.

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Citation

Yasinska IM, Kozhukhar AV, Sumbayev VV

S-nitrosation of thioredoxin in the nitrogen monoxide/superoxide system activates apoptosis signal-regulating kinase 1.

Arch Biochem Biophys. 2004 Aug 15;428(2):198-203.

PubMed ID
15246877 [ View in PubMed
]
Abstract

In the present study, we have investigated S-nitrosation of reactive thioredoxin (Trx) thiol groups in nitric oxide/superoxide system. We have found that Trx thiol groups are the targets for S-nitrosation by N2O3-like species generated in the system containing xanthine/xanthine oxidase (superoxide producing system) and DEA/NO-the *NO donating compound, however, they have shown low sensitivity to the *NO derived from DEA/NO. N2O3-dependent S-nitrosation of Trx at approximately 2-fold of NO excess compared to the superoxide amount resulted in dissociation and activation of apoptosis signal regulating kinase 1 (ASK1). However, approximately 4-fold of NO excess compared to a superoxide production preserved the level of dissociated ASK1 but decreased its activity due to the enzyme S-nitrosation.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
ThioredoxinP10599Details