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Sökning: WFRF:(Pader I)

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  • Pader, I, et al. (författare)
  • Thioredoxin-related protein of 14 kDa is an efficient L-cystine reductase and S-denitrosylase
  • 2014
  • Ingår i: Proceedings of the National Academy of Sciences of the United States of America. - : Proceedings of the National Academy of Sciences. - 1091-6490. ; 111:19, s. 6964-6969
  • Tidskriftsartikel (refereegranskat)abstract
    • Several functions in cells require reductive processes, i.e., the enzymatic catalysis of a transfer of electrons to specific cellular substrates. One major reductive system in the cytosol of human cells depends upon thioredoxin 1 (Trx1), which in turn is kept reduced by thioredoxin reductase 1 (TrxR1) using NADPH. In the present study it is shown that another protein in addition to Trx1, called thioredoxin-related protein of 14 kDa (TRP14), is highly efficient together with TrxR1 in catalyzing reduction of L-cystine or nitric oxide-derivatized cysteine residues. It is also shown that TRP14, in contrast to Trx1, is resistant to inactivation by hydrogen peroxide. These findings reveal that several TrxR1-dependent functions in cells may not be propelled solely by Trx1, but instead relate to activities of TRP14.
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  • Xu, J., et al. (författare)
  • The conserved Trp114 residue of thioredoxin reductase 1 has a redox sensor-like function triggering oligomerization and crosslinking upon oxidative stress related to cell death
  • 2015
  • Ingår i: Cell Death and Disease. - : Springer Science and Business Media LLC. - 2041-4889. ; 6
  • Tidskriftsartikel (refereegranskat)abstract
    • The selenoprotein thioredoxin reductase 1 (TrxR1) has several key roles in cellular redox systems and reductive pathways. Here we discovered that an evolutionarily conserved and surface-exposed tryptophan residue of the enzyme (Trp114) is excessively reactive to oxidation and exerts regulatory functions. The results indicate that it serves as an electron relay communicating with the FAD moiety of the enzyme, and, when oxidized, it facilitates oligomerization of TrxR1 into tetramers and higher multimers of dimers. A covalent link can also be formed between two oxidized Trp114 residues of two subunits from two separate TrxR1 dimers, as found both in cell extracts and in a crystal structure of tetrameric TrxR1. Formation of covalently linked TrxR1 subunits became exaggerated in cells on treatment with the pro-oxidant p53-reactivating anticancer compound RITA, in direct correlation with triggering of a cell death that could be prevented by antioxidant treatment. These results collectively suggest that Trp114 of TrxR1 serves a function reminiscent of an irreversible sensor for excessive oxidation, thereby presenting a previously unrecognized level of regulation of TrxR1 function in relation to cellular redox state and cell death induction.
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  • Resultat 1-8 av 8

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