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- Publisher Website: 10.1074/jbc.272.49.30952
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- PMID: 9388242
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Article: Regulatory role for a novel human thioredoxin peroxidase in NF-κB activation
Title | Regulatory role for a novel human thioredoxin peroxidase in NF-κB activation |
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Authors | |
Issue Date | 1997 |
Publisher | American 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? |
Abstract | Reduction-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 Identifier | http://hdl.handle.net/10722/147510 |
ISSN | 2020 Impact Factor: 5.157 2023 SCImago Journal Rankings: 1.766 |
ISI Accession Number ID | |
References |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Jin, DY | en_US |
dc.contributor.author | Chae, HZ | en_US |
dc.contributor.author | Rhee, SG | en_US |
dc.contributor.author | Jeang, KT | en_US |
dc.date.accessioned | 2012-05-29T06:04:14Z | - |
dc.date.available | 2012-05-29T06:04:14Z | - |
dc.date.issued | 1997 | en_US |
dc.identifier.citation | Journal Of Biological Chemistry, 1997, v. 272 n. 49, p. 30952-30961 | en_US |
dc.identifier.issn | 0021-9258 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/147510 | - |
dc.description.abstract | Reduction-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.language | eng | en_US |
dc.publisher | American Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/ | en_US |
dc.relation.ispartof | Journal of Biological Chemistry | en_US |
dc.subject.mesh | Amino Acid Sequence | en_US |
dc.subject.mesh | Antioxidants - Metabolism | en_US |
dc.subject.mesh | Base Sequence | en_US |
dc.subject.mesh | Cytoplasm - Metabolism | en_US |
dc.subject.mesh | Dna-Binding Proteins - Metabolism | en_US |
dc.subject.mesh | Dimerization | en_US |
dc.subject.mesh | Hiv Infections - Enzymology | en_US |
dc.subject.mesh | Hiv-1 | en_US |
dc.subject.mesh | Hela Cells | en_US |
dc.subject.mesh | Heat-Shock Proteins - Metabolism | en_US |
dc.subject.mesh | Humans | en_US |
dc.subject.mesh | I-Kappa B Proteins | en_US |
dc.subject.mesh | Molecular Sequence Data | en_US |
dc.subject.mesh | Molecular Weight | en_US |
dc.subject.mesh | Nf-Kappa B - Metabolism | en_US |
dc.subject.mesh | Neoplasm Proteins - Metabolism | en_US |
dc.subject.mesh | Oxidation-Reduction | en_US |
dc.subject.mesh | Peroxidases | en_US |
dc.subject.mesh | Peroxiredoxin Iii | en_US |
dc.subject.mesh | Peroxiredoxins | en_US |
dc.subject.mesh | Phosphorylation | en_US |
dc.subject.mesh | Protein Binding | en_US |
dc.subject.mesh | Proteins - Chemistry - Genetics - Physiology | en_US |
dc.subject.mesh | Rna, Messenger - Biosynthesis | en_US |
dc.subject.mesh | Tissue Distribution | en_US |
dc.title | Regulatory role for a novel human thioredoxin peroxidase in NF-κB activation | en_US |
dc.type | Article | en_US |
dc.identifier.email | Jin, DY:dyjin@hkucc.hku.hk | en_US |
dc.identifier.authority | Jin, DY=rp00452 | en_US |
dc.description.nature | link_to_subscribed_fulltext | en_US |
dc.identifier.doi | 10.1074/jbc.272.49.30952 | en_US |
dc.identifier.pmid | 9388242 | en_US |
dc.identifier.scopus | eid_2-s2.0-1842295744 | en_US |
dc.relation.references | http://www.scopus.com/mlt/select.url?eid=2-s2.0-1842295744&selection=ref&src=s&origin=recordpage | en_US |
dc.identifier.volume | 272 | en_US |
dc.identifier.issue | 49 | en_US |
dc.identifier.spage | 30952 | en_US |
dc.identifier.epage | 30961 | en_US |
dc.identifier.isi | WOS:000071640800055 | - |
dc.publisher.place | United States | en_US |
dc.identifier.scopusauthorid | Jin, DY=7201973614 | en_US |
dc.identifier.scopusauthorid | Chae, HZ=7103251724 | en_US |
dc.identifier.scopusauthorid | Rhee, SG=7401852092 | en_US |
dc.identifier.scopusauthorid | Jeang, KT=7004824803 | en_US |
dc.identifier.issnl | 0021-9258 | - |