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Article: Proteomic profiling of hepatocellular carcinoma in Chinese cohort reveals heat-shock proteins (Hsp27, Hsp70, GRP78) up-regulation and their associated prognostic values

TitleProteomic profiling of hepatocellular carcinoma in Chinese cohort reveals heat-shock proteins (Hsp27, Hsp70, GRP78) up-regulation and their associated prognostic values
Authors
Keywords2-DE
Heat-shock protein
Hepatitis B virus
Hepatocellular carcinoma
Venous infiltration
Issue Date2006
PublisherWiley - V C H Verlag GmbH & Co KGaA. The Journal's web site is located at http://www.wiley-vch.de/home/proteomics
Citation
Proteomics, 2006, v. 6 n. 3, p. 1049-1057 How to Cite?
AbstractTo facilitate the identification of candidate molecular biomarkers that are linked to the pathogenesis of hepatocellular carcinoma (HCC), we investigated protein-expression profiles of 146 tissue specimens including 67 pairs of tumors and adjacent non-tumors resected from HCC patients as well as 12 normal livers by 2-DE. Among the 1800 spots displayed in the liver proteome, a total of 90 protein species were found to be significantly different between the three groups (P < 0.05). Three of the top candidate markers up-regulated in HCC, with high receiver operating characteristic (ROC) curves, were identified by MS/MS analysis and belonged to the chaperone members: heat-shock protein (Hsp)27, Hsp70 and glucose-regulated protein (GRP)78. Over-expression of these chaperone proteins in HCC tissues was confirmed by Western blotting and immunohistochemistry. In correlation with clinico-pathological parameters, expression of Hsp27 was linked to α-fetoprotein level (P = 0.007) whereas up-regulation of GRP78 was associated with tumor venous infiltration (P = 0.035). No significant association of Hsp70 with any pathologic features was observed. The present HCC proteome analysis revealed that in response to the stressful cancerous microenvironment, tumor cells strived to increase the expression of chaperone proteins for cyto-protective function and to enhance tumor growth and metastasis. © 2006 Wiley-VCH Verlag GmbH & Co. KGaA.
Persistent Identifierhttp://hdl.handle.net/10722/69165
ISSN
2015 Impact Factor: 4.079
2015 SCImago Journal Rankings: 1.476
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLuk, JMen_HK
dc.contributor.authorLam, CTen_HK
dc.contributor.authorSiu, AFMen_HK
dc.contributor.authorLam, BYen_HK
dc.contributor.authorNg, IOLen_HK
dc.contributor.authorHu, MYen_HK
dc.contributor.authorChe, CMen_HK
dc.contributor.authorFan, STen_HK
dc.date.accessioned2010-09-06T06:11:10Z-
dc.date.available2010-09-06T06:11:10Z-
dc.date.issued2006en_HK
dc.identifier.citationProteomics, 2006, v. 6 n. 3, p. 1049-1057en_HK
dc.identifier.issn1615-9853en_HK
dc.identifier.urihttp://hdl.handle.net/10722/69165-
dc.description.abstractTo facilitate the identification of candidate molecular biomarkers that are linked to the pathogenesis of hepatocellular carcinoma (HCC), we investigated protein-expression profiles of 146 tissue specimens including 67 pairs of tumors and adjacent non-tumors resected from HCC patients as well as 12 normal livers by 2-DE. Among the 1800 spots displayed in the liver proteome, a total of 90 protein species were found to be significantly different between the three groups (P < 0.05). Three of the top candidate markers up-regulated in HCC, with high receiver operating characteristic (ROC) curves, were identified by MS/MS analysis and belonged to the chaperone members: heat-shock protein (Hsp)27, Hsp70 and glucose-regulated protein (GRP)78. Over-expression of these chaperone proteins in HCC tissues was confirmed by Western blotting and immunohistochemistry. In correlation with clinico-pathological parameters, expression of Hsp27 was linked to α-fetoprotein level (P = 0.007) whereas up-regulation of GRP78 was associated with tumor venous infiltration (P = 0.035). No significant association of Hsp70 with any pathologic features was observed. The present HCC proteome analysis revealed that in response to the stressful cancerous microenvironment, tumor cells strived to increase the expression of chaperone proteins for cyto-protective function and to enhance tumor growth and metastasis. © 2006 Wiley-VCH Verlag GmbH & Co. KGaA.en_HK
dc.languageengen_HK
dc.publisherWiley - V C H Verlag GmbH & Co KGaA. The Journal's web site is located at http://www.wiley-vch.de/home/proteomicsen_HK
dc.relation.ispartofProteomicsen_HK
dc.subject2-DEen_HK
dc.subjectHeat-shock proteinen_HK
dc.subjectHepatitis B virusen_HK
dc.subjectHepatocellular carcinomaen_HK
dc.subjectVenous infiltrationen_HK
dc.subject.meshAdolescenten_HK
dc.subject.meshAdulten_HK
dc.subject.meshAgeden_HK
dc.subject.meshBlotting, Westernen_HK
dc.subject.meshCarcinoma, Hepatocellular - metabolism - pathologyen_HK
dc.subject.meshChinaen_HK
dc.subject.meshCohort Studiesen_HK
dc.subject.meshElectrophoresis, Gel, Two-Dimensionalen_HK
dc.subject.meshFemaleen_HK
dc.subject.meshHSP27 Heat-Shock Proteinsen_HK
dc.subject.meshHSP70 Heat-Shock Proteins - metabolismen_HK
dc.subject.meshHeat-Shock Proteins - metabolismen_HK
dc.subject.meshHumansen_HK
dc.subject.meshLiver - metabolismen_HK
dc.subject.meshLiver Neoplasms - metabolism - pathologyen_HK
dc.subject.meshMaleen_HK
dc.subject.meshMiddle Ageden_HK
dc.subject.meshMolecular Chaperones - metabolismen_HK
dc.subject.meshNeoplasm Proteins - metabolismen_HK
dc.subject.meshPrognosisen_HK
dc.subject.meshProteome - metabolismen_HK
dc.subject.meshProteomicsen_HK
dc.subject.meshSpectrometry, Mass, Matrix-Assisted Laser Desorption-Ionizationen_HK
dc.subject.meshTumor Markers, Biological - metabolismen_HK
dc.subject.meshUp-Regulationen_HK
dc.titleProteomic profiling of hepatocellular carcinoma in Chinese cohort reveals heat-shock proteins (Hsp27, Hsp70, GRP78) up-regulation and their associated prognostic valuesen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=1615-9853&volume=6&issue=3&spage=1049&epage=1057&date=2006&atitle=Proteomic+profiling+of+hepatocellular+carcinoma+in+Chinese+cohort+reveals+heat-shock+proteins+(Hsp27,+Hsp70,+GRP78)+up-regulation+and+their+associated+prognostic+valuesen_HK
dc.identifier.emailLuk, JM: jmluk@hkucc.hku.hken_HK
dc.identifier.emailSiu, AFM: fmsiu@hku.hken_HK
dc.identifier.emailNg, IOL: iolng@hkucc.hku.hken_HK
dc.identifier.emailChe, CM: cmche@hku.hken_HK
dc.identifier.emailFan, ST: stfan@hku.hken_HK
dc.identifier.authorityLuk, JM=rp00349en_HK
dc.identifier.authoritySiu, AFM=rp00776en_HK
dc.identifier.authorityNg, IOL=rp00335en_HK
dc.identifier.authorityChe, CM=rp00670en_HK
dc.identifier.authorityFan, ST=rp00355en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1002/pmic.200500306en_HK
dc.identifier.pmid16400691-
dc.identifier.scopuseid_2-s2.0-32944457371en_HK
dc.identifier.hkuros114074en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-32944457371&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume6en_HK
dc.identifier.issue3en_HK
dc.identifier.spage1049en_HK
dc.identifier.epage1057en_HK
dc.identifier.eissn1615-9861-
dc.identifier.isiWOS:000235414600031-
dc.publisher.placeGermanyen_HK
dc.identifier.scopusauthoridLuk, JM=7006777791en_HK
dc.identifier.scopusauthoridLam, CT=7402989860en_HK
dc.identifier.scopusauthoridSiu, AFM=6701518489en_HK
dc.identifier.scopusauthoridLam, BY=7102023588en_HK
dc.identifier.scopusauthoridNg, IOL=7102753722en_HK
dc.identifier.scopusauthoridHu, MY=7402639252en_HK
dc.identifier.scopusauthoridChe, CM=7102442791en_HK
dc.identifier.scopusauthoridFan, ST=7402678224en_HK

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