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Article: Identification of tumor-associated proteins in oral tongue squamous cell carcinoma by proteomics

TitleIdentification of tumor-associated proteins in oral tongue squamous cell carcinoma by proteomics
Authors
KeywordsMass spectrometry
Protein profile
Tongue cancer
Two-dimensional gel electrophoresis
Issue Date2004
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, 2004, v. 4 n. 1, p. 271-278 How to Cite?
AbstractOral tongue carcinoma is an aggressive tumor that particularly affects chronic smokers, drinkers and betel squid chewers. Patients often present symptoms at a late stage, and there is a high recurrence rate after treatment. In this article, we report the first proteomic analysis of oral tongue carcinoma to globally search for tumor related proteins. Apart from helping us to understand the molecular pathogenesis of the carcinoma, these proteins may also have potential clinical applications as biomarkers, enabling the tumor to be identified at an early stage in high risk individuals, treatment response to be predicted, and residual or recurrent carcinoma to be detected sooner after treatment. The protein expression profiles of ten oral tongue squamous cell carcinomas and their matched normal mucosal resection margins were examined by two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization-time of flight mass spectroscopy. A number of tumor-associated proteins including heat shock protein (HSP)60, HSP27, alpha B-crystalline, ATP synthase beta, calgranulin B, myosin, tropomyosin and galectin 1 were consistently found to be significantly altered in their expression levels in tongue carcinoma tissues, compared with their paired normal mucosae. The expression profile portrays a global protein alteration that appears specific to oral tongue cancer. The potential of utilizing these tumor related proteins for screening cancer and monitoring recurrence warrants further investigation.
Persistent Identifierhttp://hdl.handle.net/10722/48519
ISSN
2015 Impact Factor: 4.079
2015 SCImago Journal Rankings: 1.476
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorHe, Qen_HK
dc.contributor.authorChen, Jen_HK
dc.contributor.authorKung, Hen_HK
dc.contributor.authorYuen, PWen_HK
dc.contributor.authorChiu, Jen_HK
dc.date.accessioned2008-05-22T04:16:03Z-
dc.date.available2008-05-22T04:16:03Z-
dc.date.issued2004en_HK
dc.identifier.citationProteomics, 2004, v. 4 n. 1, p. 271-278en_HK
dc.identifier.issn1615-9853en_HK
dc.identifier.urihttp://hdl.handle.net/10722/48519-
dc.description.abstractOral tongue carcinoma is an aggressive tumor that particularly affects chronic smokers, drinkers and betel squid chewers. Patients often present symptoms at a late stage, and there is a high recurrence rate after treatment. In this article, we report the first proteomic analysis of oral tongue carcinoma to globally search for tumor related proteins. Apart from helping us to understand the molecular pathogenesis of the carcinoma, these proteins may also have potential clinical applications as biomarkers, enabling the tumor to be identified at an early stage in high risk individuals, treatment response to be predicted, and residual or recurrent carcinoma to be detected sooner after treatment. The protein expression profiles of ten oral tongue squamous cell carcinomas and their matched normal mucosal resection margins were examined by two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization-time of flight mass spectroscopy. A number of tumor-associated proteins including heat shock protein (HSP)60, HSP27, alpha B-crystalline, ATP synthase beta, calgranulin B, myosin, tropomyosin and galectin 1 were consistently found to be significantly altered in their expression levels in tongue carcinoma tissues, compared with their paired normal mucosae. The expression profile portrays a global protein alteration that appears specific to oral tongue cancer. The potential of utilizing these tumor related proteins for screening cancer and monitoring recurrence warrants further investigation.en_HK
dc.format.extent424356 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.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.rightsPublished in Proteomics, 2004, v. 4 n. 1, p. 271-278en_HK
dc.subjectMass spectrometryen_HK
dc.subjectProtein profileen_HK
dc.subjectTongue canceren_HK
dc.subjectTwo-dimensional gel electrophoresisen_HK
dc.titleIdentification of tumor-associated proteins in oral tongue squamous cell carcinoma by proteomicsen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=1615-9853&volume=4&issue=1&spage=271&epage=278&date=2004&atitle=Identification+of+tumor-associated+proteins+in+oral+tongue+squamous+cell+carcinoma+by+proteomicsen_HK
dc.identifier.emailHe, Q: qyhe@hkucc.hku.hken_HK
dc.identifier.emailKung, H: hkung@hkucc.hku.hken_HK
dc.identifier.emailYuen, PW: pwyuen@hkucc.hku.hken_HK
dc.identifier.emailChiu, J: jfchiu@hkucc.hku.hken_HK
dc.description.naturepostprinten_HK
dc.identifier.doi10.1002/pmic.200300550en_HK
dc.identifier.pmid14730689en_HK
dc.identifier.scopuseid_2-s2.0-0942297968-
dc.identifier.hkuros91781-
dc.identifier.isiWOS:000188591100025-

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