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Article: Regulatory role for a novel human thioredoxin peroxidase in NF-κB activation

TitleRegulatory role for a novel human thioredoxin peroxidase in NF-κB activation
Authors
Issue Date1997
PublisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/
Citation
Journal Of Biological Chemistry, 1997, v. 272 n. 49, p. 30952-30961 How to Cite?
AbstractReduction-oxidation (redox) plays a critical role in NF-κB activation. Diverse stimuli appear to utilize reactive oxygen species (e.g. hydrogen peroxide) as common effectors for activating NF-κB. Antioxidants govern intracellular redox status, and many such molecules can reduce H2O2. However, functionally, it does appear that different antioxidants are variously selective for redox regulation of certain transcription factors such as NF-κB. For NF-κB, thioredoxin has been described to be a more potent antioxidant than either glutathione or N-acetylcysteine. Thioredoxin peroxidase is the immediate enzyme that links reduction of H2O2 to thioredoxin. Several putative human thioredoxin peroxidases have been identified using recursive sequence searches/alignments with yeast or prokaryotic enzymes. None has been characterized in detail for intracellular function(s). Hero, we describe a new human thioredoxin peroxidase, antioxidant enzyme AOE372, identified by virtue of its protein-protein interaction with the product of a proliferation association gene, pag, which is also a thiol-specific antioxidant. In human cells, AOE372 defines a redox pathway that specifically regulates NF-κB activity via a modulation of IκB- α phosphorylation in the cytoplasm. We show that AOE372 activity is regulated through either homo- or heterodimerization with other thiol peroxidases, implicating subunit assortment as a mechanism for regulating antioxidant specificities. AOE372 function suggests thioredoxin peroxidase as an immediate regulator of H2O2-mediated activation of NF-κB.
Persistent Identifierhttp://hdl.handle.net/10722/147510
ISSN
2015 Impact Factor: 4.258
2015 SCImago Journal Rankings: 3.151
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorJin, DYen_US
dc.contributor.authorChae, HZen_US
dc.contributor.authorRhee, SGen_US
dc.contributor.authorJeang, KTen_US
dc.date.accessioned2012-05-29T06:04:14Z-
dc.date.available2012-05-29T06:04:14Z-
dc.date.issued1997en_US
dc.identifier.citationJournal Of Biological Chemistry, 1997, v. 272 n. 49, p. 30952-30961en_US
dc.identifier.issn0021-9258en_US
dc.identifier.urihttp://hdl.handle.net/10722/147510-
dc.description.abstractReduction-oxidation (redox) plays a critical role in NF-κB activation. Diverse stimuli appear to utilize reactive oxygen species (e.g. hydrogen peroxide) as common effectors for activating NF-κB. Antioxidants govern intracellular redox status, and many such molecules can reduce H2O2. However, functionally, it does appear that different antioxidants are variously selective for redox regulation of certain transcription factors such as NF-κB. For NF-κB, thioredoxin has been described to be a more potent antioxidant than either glutathione or N-acetylcysteine. Thioredoxin peroxidase is the immediate enzyme that links reduction of H2O2 to thioredoxin. Several putative human thioredoxin peroxidases have been identified using recursive sequence searches/alignments with yeast or prokaryotic enzymes. None has been characterized in detail for intracellular function(s). Hero, we describe a new human thioredoxin peroxidase, antioxidant enzyme AOE372, identified by virtue of its protein-protein interaction with the product of a proliferation association gene, pag, which is also a thiol-specific antioxidant. In human cells, AOE372 defines a redox pathway that specifically regulates NF-κB activity via a modulation of IκB- α phosphorylation in the cytoplasm. We show that AOE372 activity is regulated through either homo- or heterodimerization with other thiol peroxidases, implicating subunit assortment as a mechanism for regulating antioxidant specificities. AOE372 function suggests thioredoxin peroxidase as an immediate regulator of H2O2-mediated activation of NF-κB.en_US
dc.languageengen_US
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/en_US
dc.relation.ispartofJournal of Biological Chemistryen_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshAntioxidants - Metabolismen_US
dc.subject.meshBase Sequenceen_US
dc.subject.meshCytoplasm - Metabolismen_US
dc.subject.meshDna-Binding Proteins - Metabolismen_US
dc.subject.meshDimerizationen_US
dc.subject.meshHiv Infections - Enzymologyen_US
dc.subject.meshHiv-1en_US
dc.subject.meshHela Cellsen_US
dc.subject.meshHeat-Shock Proteins - Metabolismen_US
dc.subject.meshHumansen_US
dc.subject.meshI-Kappa B Proteinsen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshMolecular Weighten_US
dc.subject.meshNf-Kappa B - Metabolismen_US
dc.subject.meshNeoplasm Proteins - Metabolismen_US
dc.subject.meshOxidation-Reductionen_US
dc.subject.meshPeroxidasesen_US
dc.subject.meshPeroxiredoxin Iiien_US
dc.subject.meshPeroxiredoxinsen_US
dc.subject.meshPhosphorylationen_US
dc.subject.meshProtein Bindingen_US
dc.subject.meshProteins - Chemistry - Genetics - Physiologyen_US
dc.subject.meshRna, Messenger - Biosynthesisen_US
dc.subject.meshTissue Distributionen_US
dc.titleRegulatory role for a novel human thioredoxin peroxidase in NF-κB activationen_US
dc.typeArticleen_US
dc.identifier.emailJin, DY:dyjin@hkucc.hku.hken_US
dc.identifier.authorityJin, DY=rp00452en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1074/jbc.272.49.30952en_US
dc.identifier.pmid9388242en_US
dc.identifier.scopuseid_2-s2.0-1842295744en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-1842295744&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume272en_US
dc.identifier.issue49en_US
dc.identifier.spage30952en_US
dc.identifier.epage30961en_US
dc.identifier.isiWOS:000071640800055-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridJin, DY=7201973614en_US
dc.identifier.scopusauthoridChae, HZ=7103251724en_US
dc.identifier.scopusauthoridRhee, SG=7401852092en_US
dc.identifier.scopusauthoridJeang, KT=7004824803en_US

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