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Article: Heme oxygenase-1-derived carbon monoxide stimulates adenosine triphosphate generation in human hepatocyte

TitleHeme oxygenase-1-derived carbon monoxide stimulates adenosine triphosphate generation in human hepatocyte
Authors
KeywordsAdenosine triphosphate
Apoptosis
Energy metabolism
Hepatocyte
p38 mitogen-activated protein kinase
Soluble guanylyl cyclase
Issue Date2005
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, 2005, v. 336 n. 3, p. 898-902 How to Cite?
AbstractHeme oxygenases cleave the pro-oxidant heme molecule into carbon monoxide, ferrous iron, and biliverdin, which is subsequently converted to bilirubin. Increasing the enzymatic activities of heme oxygenase by expression of its inducible isoform, heme oxygenase-1, protects hepatocyte from apoptosis. In the present study, we investigated the mechanisms involving in heme oxygenase-1-mediated cytoprotection. Heme oxygenase-1 could induce the expression of anti-apoptotic protein-Bcl-xL in human hepatocyte. This effect is associated with the activation of p38 MAPK signaling pathway. Carbon monoxide derived from heme oxygenase activities significantly increased adenosine triphosphate levels in hepatocyte that was essential for potentiation of the activation of p38 MAPK signaling. Our demonstration of the importance of the energy status to maximize an anti-apoptotic response provides a new insight into HO-mediated cytoprotection. © 2005 Elsevier Inc. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/84480
ISSN
2015 Impact Factor: 2.371
2015 SCImago Journal Rankings: 1.152
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorTsui, TYen_HK
dc.contributor.authorSiu, YTen_HK
dc.contributor.authorSchlitt, HJen_HK
dc.contributor.authorFan, STen_HK
dc.date.accessioned2010-09-06T08:53:27Z-
dc.date.available2010-09-06T08:53:27Z-
dc.date.issued2005en_HK
dc.identifier.citationBiochemical And Biophysical Research Communications, 2005, v. 336 n. 3, p. 898-902en_HK
dc.identifier.issn0006-291Xen_HK
dc.identifier.urihttp://hdl.handle.net/10722/84480-
dc.description.abstractHeme oxygenases cleave the pro-oxidant heme molecule into carbon monoxide, ferrous iron, and biliverdin, which is subsequently converted to bilirubin. Increasing the enzymatic activities of heme oxygenase by expression of its inducible isoform, heme oxygenase-1, protects hepatocyte from apoptosis. In the present study, we investigated the mechanisms involving in heme oxygenase-1-mediated cytoprotection. Heme oxygenase-1 could induce the expression of anti-apoptotic protein-Bcl-xL in human hepatocyte. This effect is associated with the activation of p38 MAPK signaling pathway. Carbon monoxide derived from heme oxygenase activities significantly increased adenosine triphosphate levels in hepatocyte that was essential for potentiation of the activation of p38 MAPK signaling. Our demonstration of the importance of the energy status to maximize an anti-apoptotic response provides a new insight into HO-mediated cytoprotection. © 2005 Elsevier Inc. All rights reserved.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.subjectAdenosine triphosphateen_HK
dc.subjectApoptosisen_HK
dc.subjectEnergy metabolismen_HK
dc.subjectHepatocyteen_HK
dc.subjectp38 mitogen-activated protein kinaseen_HK
dc.subjectSoluble guanylyl cyclaseen_HK
dc.titleHeme oxygenase-1-derived carbon monoxide stimulates adenosine triphosphate generation in human hepatocyteen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0006-291X&volume=336&issue=3&spage=898&epage=902&date=2005&atitle=Heme+oxygenase-1-derived+carbon+monoxide+stimulates+adenosine+triphosphate+generation+in+human+hepatocyteen_HK
dc.identifier.emailFan, ST: stfan@hku.hken_HK
dc.identifier.authorityFan, ST=rp00355en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.bbrc.2005.08.187en_HK
dc.identifier.pmid16154535-
dc.identifier.scopuseid_2-s2.0-25144524703en_HK
dc.identifier.hkuros116936en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-25144524703&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume336en_HK
dc.identifier.issue3en_HK
dc.identifier.spage898en_HK
dc.identifier.epage902en_HK
dc.identifier.isiWOS:000232255000025-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridTsui, TY=7006622455en_HK
dc.identifier.scopusauthoridSiu, YT=8953557400en_HK
dc.identifier.scopusauthoridSchlitt, HJ=7005572464en_HK
dc.identifier.scopusauthoridFan, ST=7402678224en_HK

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