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Biochem Biophys Res Commun. 2000 Jul 21;274(1):177-82.

Nucleoredoxin, glutaredoxin, and thioredoxin differentially regulate NF-kappaB, AP-1, and CREB activation in HEK293 cells.

Author information

1
Department of Anesthesia, Kyoto University Hospital, Kyoto University, 54 Shogoin-Kawaharacho, Sakyo-Ku, Kyoto, 606-8507, Japan. khirota@kuhp.kyoto-u.ac.jp

Erratum in

  • Biochem Biophys Res Commun 2000 Aug 18;275(1):247. Junji, Y [corrected to Yodoi, J].

Abstract

Well-established mechanisms for regulation of protein activity include thiol-mediated oxidoreduction in addition to protein-protein interactions and phosphorylation. Nucleoredoxin (NRX), glutaredoxin (GRX), and thioredoxin (TRX) have been shown to act as a potent thiol reductase and reactive oxygen species regulator. They constitute a oxidoreductase superfamily and have been suggested as a candidate operating in the redox regulation of gene expression. We demonstrated here that intracellular localization of these redox molecules differ from each other and that the redox molecules differentially regulate NF-kappaB, AP-1, and CREB activation induced by TNFalpha, PMA, and forskolin and by expression of signaling intermediate kinases, NIK, MEKK, and PKA in HEK293 cells. This is a first report that describes involvement of NRX and GRX and differences from TRX in transcriptional regulation of NF-kappaB, AP-1, and CREB in living cells.

PMID:
10903915
DOI:
10.1006/bbrc.2000.3106
[Indexed for MEDLINE]
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