外科Lin, Li-LingLi-LingLinCHIUNG-NIEN CHENWEI-CHOU LINPO-HUANG LEEKING-JEN CHANGYO-PING LAIJIN-TOWN WANGHSUEH-FEN JUAN2009-12-182018-07-112009-12-182018-07-112008http://ntur.lib.ntu.edu.tw//handle/246246/174628http://ntur.lib.ntu.edu.tw/bitstream/246246/174628/1/000007.pdfHelicobacter pylori was reported to be an important risk factor for the carcinogenesis of gastric cancer. Here, we used a proteomic approach to find differentially expressed proteins between the normal and tumor tissue of gastric cancer patients infected with H. pylori. In our results, we found annexin A4 was over-expressed in patients infected with H. pylori and was found in tumor cells, and over- expressed in gastric cancer SCM-1 cells after H. pylori infection. Ca2+ can be induced by H. pylori and interact with annexin A4 Ca2+ binding site to block the calmodulin- activated chloride conductance activation; therefore, it produces a new environment that benefits the malignant existence of H. pylori and raises the risk for gastric cancer. We also found interleuken-8 (IL-8) expression levels were increased in H. pylori infected SCM-1 cells. Combined with previous reports and our results, we summarize that the over-expression of annexin A4 in SCM-1 cells with H. pylori infection may subsequently induce IL-8 which can further cause tumor angiogenesis. In this paper, we show that annexin A4 is a potential novel molecular marker for gastric cancer with H. pylori infection, and our results may provide a new insight in the development of new anti-cancer drugs.en-US2-DEannexin A4gastric cancerhelicobacter pyloritructure modeling[SDGs]SDG3calcium ion; calmodulin; chloride; interleukin 8; lipocortin 2; lipocortin 4; molecular marker; amino acid sequence; article; binding site; cancer cell; cancer patient; cancer risk; chloride conductance; clinical article; controlled study; cytokine release; gastrectomy; Helicobacter infection; Helicobacter pylori; human; human cell; human tissue; immunohistochemistry; matrix assisted laser desorption ionization time of flight mass spectrometry; nonhuman; priority journal; protein analysis; protein expression; protein protein interaction; protein structure; proteomics; stomach cancer; stomach carcinogenesis; tandem mass spectrometry; tumor vascularization; two dimensional electrophoresis; Western blotting; Helicobacter pylorijournal article10.1002/prca.200780088http://ntur.lib.ntu.edu.tw/bitstream/246246/174628/1/000007.pdf