File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
  • Find via Find It@HKUL
Supplementary

Conference Paper: Dyregulation of chaperone proteins Hsp27, Hsp70 and Grp78 in hepatocellular carcinoma (Abstract)

TitleDyregulation of chaperone proteins Hsp27, Hsp70 and Grp78 in hepatocellular carcinoma (Abstract)
Authors
Issue Date2004
PublisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.mcponline.org/
Citation
The 3rd HUPO Annual World Congress, Beijing, China, 25-27 October 2004. In Molecular and Cellular Proteomics, 2004, v. 3 n. 10 suppl., p. S114, abstract no. 8.19 How to Cite?
AbstractThe purpose of this study is to establish differential protein expression profiles between hepatocellular carcinoma (HCC) and normal liver tissues by 2-D gel electrophoresis and MALDI-TOF. We aim to identify potentially useful tumor-associated markers that are dysregulated in HCC specimens. Fifty-two HCC surgical specimens and paired peritumor tissues were collected from patients underwent hepatectomy at Queen Mary Hospital, Pokfulam, Hong Kong, with approved protocol from the Institutional Ethics Committee. Cellular proteins were fractionated by differential extraction buffer system, and subjected to two-dimensional gel electrophoresis followed by MALDI-ToF analysis. Three chaperone heat shock proteins Hsp70, Hsp27 and GRP78 were found significantly dysregulated in 52 pairs of HCC tissues by proteomic analysis. These chaperon proteins are believed to play important roles in protein folding, transport and assembly as well as anti-apoptotic pathways in hepatocarcinogenesis. One-way ANOVA was used for statistical analysis, and p < 0.05 considered to be significant. Over expression of the chaperone proteins were confirmed by western blot. Clinical correlation of these chaperone proteins indicated their potential pathogenic roles in advanced tumor staging and metastasis, hinting for poor prognosis of patients with HCC. Supported by grants from the Research Grants Council of Hong Kong: HKU7320/02M; N_HKU718/03.
DescriptionSession 8: Liver Proteomics 1: no. 8.19
This free journal suppl. entitled: HUPO 3rd Annual World Congress, October 25–27, Beijing
Persistent Identifierhttp://hdl.handle.net/10722/96966
ISSN
2015 Impact Factor: 5.912
2015 SCImago Journal Rankings: 3.213

 

DC FieldValueLanguage
dc.contributor.authorLuk, JM-
dc.contributor.authorLam, CT-
dc.contributor.authorLam, BH-
dc.contributor.authorSiu, A-
dc.contributor.authorChe, CM-
dc.contributor.authorFan, ST-
dc.date.accessioned2010-09-25T16:51:32Z-
dc.date.available2010-09-25T16:51:32Z-
dc.date.issued2004-
dc.identifier.citationThe 3rd HUPO Annual World Congress, Beijing, China, 25-27 October 2004. In Molecular and Cellular Proteomics, 2004, v. 3 n. 10 suppl., p. S114, abstract no. 8.19-
dc.identifier.issn1535-9476-
dc.identifier.urihttp://hdl.handle.net/10722/96966-
dc.descriptionSession 8: Liver Proteomics 1: no. 8.19-
dc.descriptionThis free journal suppl. entitled: HUPO 3rd Annual World Congress, October 25–27, Beijing-
dc.description.abstractThe purpose of this study is to establish differential protein expression profiles between hepatocellular carcinoma (HCC) and normal liver tissues by 2-D gel electrophoresis and MALDI-TOF. We aim to identify potentially useful tumor-associated markers that are dysregulated in HCC specimens. Fifty-two HCC surgical specimens and paired peritumor tissues were collected from patients underwent hepatectomy at Queen Mary Hospital, Pokfulam, Hong Kong, with approved protocol from the Institutional Ethics Committee. Cellular proteins were fractionated by differential extraction buffer system, and subjected to two-dimensional gel electrophoresis followed by MALDI-ToF analysis. Three chaperone heat shock proteins Hsp70, Hsp27 and GRP78 were found significantly dysregulated in 52 pairs of HCC tissues by proteomic analysis. These chaperon proteins are believed to play important roles in protein folding, transport and assembly as well as anti-apoptotic pathways in hepatocarcinogenesis. One-way ANOVA was used for statistical analysis, and p < 0.05 considered to be significant. Over expression of the chaperone proteins were confirmed by western blot. Clinical correlation of these chaperone proteins indicated their potential pathogenic roles in advanced tumor staging and metastasis, hinting for poor prognosis of patients with HCC. Supported by grants from the Research Grants Council of Hong Kong: HKU7320/02M; N_HKU718/03.-
dc.languageeng-
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.mcponline.org/-
dc.relation.ispartofMolecular and Cellular Proteomics-
dc.rightsMolecular and Cellular Proteomics. Copyright © American Society for Biochemistry and Molecular Biology, Inc.-
dc.rightsThis research was originally published in [Journal Name]. Author(s). Title. Journal Name. Year. Vol:pp-pp. © the American Society for Biochemistry and Molecular Biology-
dc.titleDyregulation of chaperone proteins Hsp27, Hsp70 and Grp78 in hepatocellular carcinoma (Abstract)-
dc.typeConference_Paper-
dc.identifier.emailLuk, JM: jmluk@hku.hk-
dc.identifier.emailLam, CT: ctlam88@hkucc.hku.hk-
dc.identifier.emailChe, CM: cmche@hku.hk-
dc.identifier.emailFan, ST: stfan@hku.hk-
dc.identifier.authorityLuk, JM=rp00349-
dc.identifier.authorityChe, CM=rp00670-
dc.identifier.authorityFan, ST=rp00355-
dc.identifier.hkuros104132-
dc.identifier.hkuros104140-
dc.identifier.volume3-
dc.identifier.issue10 suppl.-
dc.identifier.spageS114, abstract no. 8.19-
dc.identifier.epageS114, abstract no. 8.19-
dc.publisher.placeUnited States-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats