| Systematic proteomic analysis of human hepotacellular carcinoma cells reveals molecular pathways and networks involved in metastasis. | |
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MedLine Citation:
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PMID: 21468425 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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Systematic proteomic studying of the mechanism of hepatocellular carcinoma (HCC) metastasis remains challenging. We performed comparative proteomic and pathway analysis of four human metastatic HCC cell lines to identify metastasis-associated proteins. These HCC cell lines had a similar genetic background but with an increasing potential of metastasis. Using a combination of two dimensional electrophoresis (2-DE) and MALDI-TOF mass spectrometry, a total of 125 proteins and their post-translational modification forms or isoforms were found to be differentially expressed in the cell lines. Among them, 29 were gradually up-regulated whereas 17 were down-regulated with increasing metastatic potential. Instead of a traditional single-gene readout, global bioinformatics analysis was carried out, which revealed that the glycolysis pathway was the most significantly enriched pathway. The heat shock proteins (HSPs) centered and NF-kappaB centered networks were also enriched in the result, which may imply the key function of inflaming on metastasis. Meanwhile, knockdown of HDGF, an up-regulated protein and a target of NF-kappaB, induced cell apoptosis in the metastatic HCC cells. This work provides a demonstration that a combination of bioinformatics and comparative proteomics can help in finding out potential biomarkers associated with HCC metastasis on the level of pathways. |
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Authors:
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Yanyan Yu; Huali Shen; Hongxiu Yu; Fan Zhong; Yang Zhang; Chen Zhang; Jian Zhao; Hong Li; Jie Chen; Yinkun Liu; Pengyuan Yang |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2011-4-6 |
Journal Detail:
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Title: Molecular bioSystems Volume: - ISSN: 1742-2051 ISO Abbreviation: - Publication Date: 2011 Apr |
Date Detail:
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Created Date: 2011-4-6 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 101251620 Medline TA: Mol Biosyst Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Affiliation:
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Department of Chemistry, Fudan University, Shanghai 200433, China. pyyang@fudan.edu.cn. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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