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Article: Mouse peroxiredoxin V is a thioredoxin peroxidase that inhibits p53-induced apoptosis

TitleMouse peroxiredoxin V is a thioredoxin peroxidase that inhibits p53-induced apoptosis
Authors
Zhou, YKok, KHChun, ACSWong, CMWu, HWLin, MCMFung, PCWKung, HFJin, DY
KeywordsApoptosis
p53
Peroxiredoxin
Reactive oxygen species (ROS)
Redox
Thioredoxin peroxidase
Issue Date2000
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/wps/find/journaldescription.cws_home/622790/description
Citation
Biochemical And Biophysical Research Communications, 2000, v. 268 n. 3, p. 921-927 How to Cite?
DOI: http://dx.doi.org/10.1006/bbrc.2000.2231
AbstractWe have identified human and mouse peroxiredoxin V (Prx-V) by virtue of the sequence homologies to yeast peroxisomal antioxidant enzyme PMP20. Prx-V represents the fifth of the six currently known subfamilies of mammalian peroxiredoxins. It is a novel organellar enzyme that has orthologs in bacteria. Biochemically, Prx-V is a thioredoxin peroxidase. One important aspect of p53 function in mammalian cells involves induction of apoptosis likely mediated by redox. We show that overexpression of Prx-V prevented the p53-dependent generation of reactive oxygen species. Likewise, Prx-V inhibited p53-induced apoptosis. Thus, Prx-V is critically involved in intracellular redox signaling. (C) 2000 Academic Press.
Persistent Identifierhttp://hdl.handle.net/10722/88048
ISSN
0006-291X
2023 Impact Factor: 2.5
2023 SCImago Journal Rankings: 0.770
ISI Accession Number ID
WOS:000085640000046
References
References in Scopus

 

DC FieldValueLanguage
dc.contributor.authorZhou, Yen_HK
dc.contributor.authorKok, KHen_HK
dc.contributor.authorChun, ACSen_HK
dc.contributor.authorWong, CMen_HK
dc.contributor.authorWu, HWen_HK
dc.contributor.authorLin, MCMen_HK
dc.contributor.authorFung, PCWen_HK
dc.contributor.authorKung, HFen_HK
dc.contributor.authorJin, DYen_HK
dc.date.accessioned2010-09-06T09:37:58Z-
dc.date.available2010-09-06T09:37:58Z-
dc.date.issued2000en_HK
dc.identifier.citationBiochemical And Biophysical Research Communications, 2000, v. 268 n. 3, p. 921-927en_HK
dc.identifier.issn0006-291Xen_HK
dc.identifier.urihttp://hdl.handle.net/10722/88048-
dc.description.abstractWe have identified human and mouse peroxiredoxin V (Prx-V) by virtue of the sequence homologies to yeast peroxisomal antioxidant enzyme PMP20. Prx-V represents the fifth of the six currently known subfamilies of mammalian peroxiredoxins. It is a novel organellar enzyme that has orthologs in bacteria. Biochemically, Prx-V is a thioredoxin peroxidase. One important aspect of p53 function in mammalian cells involves induction of apoptosis likely mediated by redox. We show that overexpression of Prx-V prevented the p53-dependent generation of reactive oxygen species. Likewise, Prx-V inhibited p53-induced apoptosis. Thus, Prx-V is critically involved in intracellular redox signaling. (C) 2000 Academic Press.en_HK
dc.languageengen_HK
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/wps/find/journaldescription.cws_home/622790/descriptionen_HK
dc.relation.ispartofBiochemical and Biophysical Research Communicationsen_HK
dc.subjectApoptosisen_HK
dc.subjectp53en_HK
dc.subjectPeroxiredoxinen_HK
dc.subjectReactive oxygen species (ROS)en_HK
dc.subjectRedoxen_HK
dc.subjectThioredoxin peroxidaseen_HK
dc.subject.meshAmino Acid Sequenceen_HK
dc.subject.meshAnimalsen_HK
dc.subject.meshApoptosis - drug effectsen_HK
dc.subject.meshBase Sequenceen_HK
dc.subject.meshDNA Primers - geneticsen_HK
dc.subject.meshGene Expressionen_HK
dc.subject.meshHeLa Cellsen_HK
dc.subject.meshHumansen_HK
dc.subject.meshMiceen_HK
dc.subject.meshMolecular Sequence Dataen_HK
dc.subject.meshNeoplasm Proteinsen_HK
dc.subject.meshOxidation-Reductionen_HK
dc.subject.meshPeroxidases - genetics - metabolism - pharmacologyen_HK
dc.subject.meshPeroxiredoxin IIIen_HK
dc.subject.meshPeroxiredoxinsen_HK
dc.subject.meshPhylogenyen_HK
dc.subject.meshReactive Oxygen Species - metabolismen_HK
dc.subject.meshSequence Homology, Amino Aciden_HK
dc.subject.meshSignal Transductionen_HK
dc.subject.meshTumor Suppressor Protein p53 - metabolism - pharmacologyen_HK
dc.titleMouse peroxiredoxin V is a thioredoxin peroxidase that inhibits p53-induced apoptosisen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0006-291X&volume=268&issue=3&spage=921&epage=927&date=2000&atitle=Mouse+Peroxiredoxin+V+is+a+Thioredoxin+Peroxidase+that+Inhibits+p53-Induced+Apoptosisen_HK
dc.identifier.emailKok, KH:khkok@hku.hken_HK
dc.identifier.emailWong, CM:wispwong@hkucc.hku.hken_HK
dc.identifier.emailLin, MCM:mcllin@hkucc.hku.hken_HK
dc.identifier.emailJin, DY:dyjin@hkucc.hku.hken_HK
dc.identifier.authorityKok, KH=rp01455en_HK
dc.identifier.authorityWong, CM=rp01489en_HK
dc.identifier.authorityLin, MCM=rp00746en_HK
dc.identifier.authorityJin, DY=rp00452en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1006/bbrc.2000.2231en_HK
dc.identifier.pmid10679306-
dc.identifier.scopuseid_2-s2.0-0034708217en_HK
dc.identifier.hkuros51514en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0034708217&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume268en_HK
dc.identifier.issue3en_HK
dc.identifier.spage921en_HK
dc.identifier.epage927en_HK
dc.identifier.isiWOS:000085640000046-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridZhou, Y=7405366890en_HK
dc.identifier.scopusauthoridKok, KH=7006862631en_HK
dc.identifier.scopusauthoridChun, ACS=7003650706en_HK
dc.identifier.scopusauthoridWong, CM=18134632400en_HK
dc.identifier.scopusauthoridWu, HW=7405581386en_HK
dc.identifier.scopusauthoridLin, MCM=7404816359en_HK
dc.identifier.scopusauthoridFung, PCW=7101613315en_HK
dc.identifier.scopusauthoridKung, HF=7402514190en_HK
dc.identifier.scopusauthoridJin, DY=7201973614en_HK
dc.identifier.issnl0006-291X-

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