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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
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?
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
2015 Impact Factor: 2.371
2015 SCImago Journal Rankings: 1.152
ISI Accession Number ID
References

 

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

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