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- PMID: 14730689
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Article: Identification of tumor-associated proteins in oral tongue squamous cell carcinoma by proteomics
Title | Identification of tumor-associated proteins in oral tongue squamous cell carcinoma by proteomics |
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Authors | |
Keywords | Mass spectrometry Protein profile Tongue cancer Two-dimensional gel electrophoresis |
Issue Date | 2004 |
Publisher | Wiley - 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? |
Abstract | Oral 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 Identifier | http://hdl.handle.net/10722/48519 |
ISSN | 2023 Impact Factor: 3.4 2023 SCImago Journal Rankings: 1.011 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | He, Q | en_HK |
dc.contributor.author | Chen, J | en_HK |
dc.contributor.author | Kung, H | en_HK |
dc.contributor.author | Yuen, PW | en_HK |
dc.contributor.author | Chiu, J | en_HK |
dc.date.accessioned | 2008-05-22T04:16:03Z | - |
dc.date.available | 2008-05-22T04:16:03Z | - |
dc.date.issued | 2004 | en_HK |
dc.identifier.citation | Proteomics, 2004, v. 4 n. 1, p. 271-278 | en_HK |
dc.identifier.issn | 1615-9853 | en_HK |
dc.identifier.uri | http://hdl.handle.net/10722/48519 | - |
dc.description.abstract | Oral 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.extent | 424356 bytes | - |
dc.format.extent | 254114 bytes | - |
dc.format.mimetype | application/pdf | - |
dc.format.mimetype | application/pdf | - |
dc.language | eng | en_HK |
dc.publisher | Wiley - V C H Verlag GmbH & Co KGaA. The Journal's web site is located at http://www.wiley-vch.de/home/proteomics | en_HK |
dc.rights | Published in Proteomics, 2004, v. 4 n. 1, p. 271-278 | en_HK |
dc.subject | Mass spectrometry | en_HK |
dc.subject | Protein profile | en_HK |
dc.subject | Tongue cancer | en_HK |
dc.subject | Two-dimensional gel electrophoresis | en_HK |
dc.title | Identification of tumor-associated proteins in oral tongue squamous cell carcinoma by proteomics | en_HK |
dc.type | Article | en_HK |
dc.identifier.openurl | http://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+proteomics | en_HK |
dc.identifier.email | He, Q: qyhe@hkucc.hku.hk | en_HK |
dc.identifier.email | Kung, H: hkung@hkucc.hku.hk | en_HK |
dc.identifier.email | Yuen, PW: pwyuen@hkucc.hku.hk | en_HK |
dc.identifier.email | Chiu, J: jfchiu@hkucc.hku.hk | en_HK |
dc.description.nature | postprint | en_HK |
dc.identifier.doi | 10.1002/pmic.200300550 | en_HK |
dc.identifier.pmid | 14730689 | en_HK |
dc.identifier.scopus | eid_2-s2.0-0942297968 | - |
dc.identifier.hkuros | 91781 | - |
dc.identifier.isi | WOS:000188591100025 | - |
dc.identifier.issnl | 1615-9853 | - |