File Download
  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Comparative proteomic analysis of esophageal squamous cell carcinoma

TitleComparative proteomic analysis of esophageal squamous cell carcinoma
Authors
KeywordsEsophageal cancer
Peroxiredoxin
Protein profiling
Squamous cell carcinoma antigen 1
Transgelin
Tumor-associated proteins
Two-dimensional gel electrophoresis
Issue Date2005
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, 2005, v. 5 n. 11, p. 2960-2971 How to Cite?
AbstractRanking as the fourth commonest cancer, esophageal squamous cell carcinoma (ESCC) represents one of the leading causes of cancer death in China. One of the main reasons for the low survival rate is that neoplasms in esophagus are not detected until they have invaded into surrounding tissues or spread throughout the body at advanced stages. A better understanding of the malignant mechanism and early diagnosis are important for fighting ESCC. In this study, we used proteomics to analyze ESCC tissues, aiming at defining the proteomic features implicated in the multistage progression of esophageal carcinogenesis. Proteins that exhibited significantly different expressions were identified by peptide mass fingerprinting and validated by Western blotting and reverse transcriptase-polymerase chain reaction. The protein changes were then correlated to the different grades of disease differentiation. Compared to those in adjacent normal epitheliums, the expression of 15 proteins including enolase, elongation factor Tu, isocitrate dehydrogenase, tubulin alpha-1 chain, tubulin beta-5 chain, actin (cytoplasmic 1), glyceraldehyde-3 phosphate dehydrogenase, tropomyosin isoform 4 (TPM4), prohibitin, peroxiredoxin 1 (PRX1), manganese-containing superoxide dismutase (MnSOD), neuronal protein, and transgelin was up-regulated; and the expression of five proteins including TPM1, squamous cell carcinoma antigen 1 (SCCA1), stratifin, peroxiredoxin 2 isoform a, and alpha B crystalline was down-regulated in cancer tissues with a statistical significance (p < 0.05). In addition, the differential expression of SCCA1, PRX1, MnSOD, TPM4, and prohibitin can be observed in precancerous lesions of ESCC. The expression of stratifin, prohibitin, and SCCA1 dropped with increasing dedifferentiation of ESCC. These data may suggest that these proteins contribute to the multistage process of carcinogenesis, tumor progression, and invasiveness of ESCC. © 2005 WILEY-VCH Verlag GmbH & Co. KGaA.
Persistent Identifierhttp://hdl.handle.net/10722/48510
ISSN
2015 Impact Factor: 4.079
2015 SCImago Journal Rankings: 1.476
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorQi, Yen_HK
dc.contributor.authorChiu, JFen_HK
dc.contributor.authorWang, Len_HK
dc.contributor.authorKwong, DLWen_HK
dc.contributor.authorHe, QYen_HK
dc.date.accessioned2008-05-22T04:15:50Z-
dc.date.available2008-05-22T04:15:50Z-
dc.date.issued2005en_HK
dc.identifier.citationProteomics, 2005, v. 5 n. 11, p. 2960-2971en_HK
dc.identifier.issn1615-9853en_HK
dc.identifier.urihttp://hdl.handle.net/10722/48510-
dc.description.abstractRanking as the fourth commonest cancer, esophageal squamous cell carcinoma (ESCC) represents one of the leading causes of cancer death in China. One of the main reasons for the low survival rate is that neoplasms in esophagus are not detected until they have invaded into surrounding tissues or spread throughout the body at advanced stages. A better understanding of the malignant mechanism and early diagnosis are important for fighting ESCC. In this study, we used proteomics to analyze ESCC tissues, aiming at defining the proteomic features implicated in the multistage progression of esophageal carcinogenesis. Proteins that exhibited significantly different expressions were identified by peptide mass fingerprinting and validated by Western blotting and reverse transcriptase-polymerase chain reaction. The protein changes were then correlated to the different grades of disease differentiation. Compared to those in adjacent normal epitheliums, the expression of 15 proteins including enolase, elongation factor Tu, isocitrate dehydrogenase, tubulin alpha-1 chain, tubulin beta-5 chain, actin (cytoplasmic 1), glyceraldehyde-3 phosphate dehydrogenase, tropomyosin isoform 4 (TPM4), prohibitin, peroxiredoxin 1 (PRX1), manganese-containing superoxide dismutase (MnSOD), neuronal protein, and transgelin was up-regulated; and the expression of five proteins including TPM1, squamous cell carcinoma antigen 1 (SCCA1), stratifin, peroxiredoxin 2 isoform a, and alpha B crystalline was down-regulated in cancer tissues with a statistical significance (p < 0.05). In addition, the differential expression of SCCA1, PRX1, MnSOD, TPM4, and prohibitin can be observed in precancerous lesions of ESCC. The expression of stratifin, prohibitin, and SCCA1 dropped with increasing dedifferentiation of ESCC. These data may suggest that these proteins contribute to the multistage process of carcinogenesis, tumor progression, and invasiveness of ESCC. © 2005 WILEY-VCH Verlag GmbH & Co. KGaA.en_HK
dc.format.extent1446200 bytes-
dc.format.extent254114 bytes-
dc.format.mimetypeapplication/pdf-
dc.format.mimetypeapplication/pdf-
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.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.rightsPublished in Proteomics, 2005, v. 5 n. 11, p. 2960-2971en_HK
dc.subjectEsophageal canceren_HK
dc.subjectPeroxiredoxinen_HK
dc.subjectProtein profilingen_HK
dc.subjectSquamous cell carcinoma antigen 1en_HK
dc.subjectTransgelinen_HK
dc.subjectTumor-associated proteinsen_HK
dc.subjectTwo-dimensional gel electrophoresisen_HK
dc.titleComparative proteomic analysis of esophageal squamous cell carcinomaen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=1615-9853&volume=5&issue=11&spage=2960&epage=2971&date=2005&atitle=Comparative+proteomic+analysis+of+esophageal+squamous+cell+carcinomaen_HK
dc.identifier.emailKwong, DLW:dlwkwong@hku.hken_HK
dc.identifier.authorityKwong, DLW=rp00414en_HK
dc.description.naturepostprinten_HK
dc.identifier.doi10.1002/pmic.200401175en_HK
dc.identifier.pmid15986332en_HK
dc.identifier.scopuseid_2-s2.0-23044457352en_HK
dc.identifier.hkuros101420-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-23044457352&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume5en_HK
dc.identifier.issue11en_HK
dc.identifier.spage2960en_HK
dc.identifier.epage2971en_HK
dc.identifier.isiWOS:000231036100024-
dc.publisher.placeGermanyen_HK
dc.identifier.scopusauthoridQi, Y=47461520800en_HK
dc.identifier.scopusauthoridChiu, JF=7201501692en_HK
dc.identifier.scopusauthoridWang, L=12242861000en_HK
dc.identifier.scopusauthoridKwong, DLW=15744231600en_HK
dc.identifier.scopusauthoridHe, QY=34770287900en_HK

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats