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Article: Diverse proteomic alterations in gastric adenocarcinoma

TitleDiverse proteomic alterations in gastric adenocarcinoma
Authors
KeywordsGastric cancer
Protein profiling
Tumor biomarkers
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. 10, p. 3276-3287 How to Cite?
AbstractGastric adenocarcinoma is one of the most common cancers in Asian countries including China. Although its incidence rates in the West are lower than that in Asia, gastric cancer is still a major health problem worldwide, being second only to lung cancers in the number of deaths it causes. Helicobacter pylori infection has been identified as the major pathogen, but the detailed pathogenesis of gastric carcinoma remains elusive. Due to the lack of suitable and specific biomarkers for early detection, most cases of the disease are diagnosed at late stages and the survival rate is low. In this study, we used a proteomic approach to globally analyze the protein profiles of paired surgical specimens of primary gastric adenocarcinoma and nontumor mucosa aiming at identifying specific disease-associated proteins as potential clinical biomarkers and for carcinogenetic study. Compared to nontumor tissues, multiple protein alterations were found in tumor tissues. Some of these alterations involve variations in the expression of cytoskeleton proteins, including an increase in cytokeratin 8 and tropomyosin isoform and a decrease in cytokeratin 20. Co-up-regulations of heat-shock proteins and glycolytic enzymes were observed in tumor tissues, indicating self-protective efforts of cells and the growing energy requirement during malignant transformation. Diverse regulations also occurred with proteins involved in cell proliferation and differentiation, such as GMP reductase 2 and creatine kinase B, and proteins bearing potential tumor suppressor activities, including prohibitin and selenium binding protein 1. More interestingly, a human stomach-specific protein, 18 kDa antrum mucosa protein, was found to be dramatically under-expressed in cancer tissues, implicating a possible special pathological role for this protein in gastric carcinogenesis. Further comprehensive evaluation by globally considering the altered factors may result in the discovery of a biomarker index for effective assessment of the disease and may provide in-depth information for better understanding the pathogenesis of gastric cancer.
Persistent Identifierhttp://hdl.handle.net/10722/48520
ISSN
2015 Impact Factor: 4.079
2015 SCImago Journal Rankings: 1.476
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorHe, QYen_HK
dc.contributor.authorCheung, YHen_HK
dc.contributor.authorLeung, SYen_HK
dc.contributor.authorYuen, STen_HK
dc.contributor.authorChu, KMen_HK
dc.contributor.authorChiu, JFen_HK
dc.date.accessioned2008-05-22T04:16:04Z-
dc.date.available2008-05-22T04:16:04Z-
dc.date.issued2004en_HK
dc.identifier.citationProteomics, 2004, v. 4 n. 10, p. 3276-3287en_HK
dc.identifier.issn1615-9853en_HK
dc.identifier.urihttp://hdl.handle.net/10722/48520-
dc.description.abstractGastric adenocarcinoma is one of the most common cancers in Asian countries including China. Although its incidence rates in the West are lower than that in Asia, gastric cancer is still a major health problem worldwide, being second only to lung cancers in the number of deaths it causes. Helicobacter pylori infection has been identified as the major pathogen, but the detailed pathogenesis of gastric carcinoma remains elusive. Due to the lack of suitable and specific biomarkers for early detection, most cases of the disease are diagnosed at late stages and the survival rate is low. In this study, we used a proteomic approach to globally analyze the protein profiles of paired surgical specimens of primary gastric adenocarcinoma and nontumor mucosa aiming at identifying specific disease-associated proteins as potential clinical biomarkers and for carcinogenetic study. Compared to nontumor tissues, multiple protein alterations were found in tumor tissues. Some of these alterations involve variations in the expression of cytoskeleton proteins, including an increase in cytokeratin 8 and tropomyosin isoform and a decrease in cytokeratin 20. Co-up-regulations of heat-shock proteins and glycolytic enzymes were observed in tumor tissues, indicating self-protective efforts of cells and the growing energy requirement during malignant transformation. Diverse regulations also occurred with proteins involved in cell proliferation and differentiation, such as GMP reductase 2 and creatine kinase B, and proteins bearing potential tumor suppressor activities, including prohibitin and selenium binding protein 1. More interestingly, a human stomach-specific protein, 18 kDa antrum mucosa protein, was found to be dramatically under-expressed in cancer tissues, implicating a possible special pathological role for this protein in gastric carcinogenesis. Further comprehensive evaluation by globally considering the altered factors may result in the discovery of a biomarker index for effective assessment of the disease and may provide in-depth information for better understanding the pathogenesis of gastric cancer.en_HK
dc.format.extent1088921 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, 2004, v. 4 n. 10, p. 3276-3287en_HK
dc.subjectGastric canceren_HK
dc.subjectProtein profilingen_HK
dc.subjectTumor biomarkersen_HK
dc.subjectTwo-dimensional gel electrophoresisen_HK
dc.titleDiverse proteomic alterations in gastric adenocarcinomaen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=1615-9853&volume=4&issue=10&spage=3276&epage=3287&date=2004&atitle=Diverse+proteomic+alterations+in+gastric+adenocarcinomaen_HK
dc.identifier.emailLeung, SY: suetyi@hkucc.hku.hken_HK
dc.identifier.emailChu, KM: chukm@hkucc.hku.hken_HK
dc.identifier.authorityLeung, SY=rp00359en_HK
dc.identifier.authorityChu, KM=rp00435en_HK
dc.description.naturepostprinten_HK
dc.identifier.doi10.1002/pmic.200300916en_HK
dc.identifier.pmid15378696-
dc.identifier.scopuseid_2-s2.0-5644266041en_HK
dc.identifier.hkuros94914-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-5644266041&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume4en_HK
dc.identifier.issue10en_HK
dc.identifier.spage3276en_HK
dc.identifier.epage3287en_HK
dc.identifier.isiWOS:000224487500038-
dc.publisher.placeGermanyen_HK
dc.identifier.scopusauthoridHe, QY=34770287900en_HK
dc.identifier.scopusauthoridCheung, YH=7202111455en_HK
dc.identifier.scopusauthoridLeung, SY=7202044886en_HK
dc.identifier.scopusauthoridYuen, ST=7103160927en_HK
dc.identifier.scopusauthoridChu, KM=7402453538en_HK
dc.identifier.scopusauthoridChiu, JF=7201501692en_HK

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