|Title:||Subcellular and functional proteomic analysis of the cellular responses induced by Helicobacter pylori||Authors:||LU-PING CHOW
|Issue Date:||2006||Journal Volume:||5||Journal Issue:||4||Start page/Pages:||702-713||Source:||Molecular and Cellular Proteomics||Abstract:||
Helicobacter pylori infection is a crucial factor in the pathogenesis of several digestive disorders, including peptic ulcers, chronic gastritis, and gastric cancer. Moreover H. pylori induces disease-specific protein expression in gastric epithelial cells. The aim of the present study was to characterize proteins differentially expressed in H. pylori-infected gastric epithelial AGS cells. An in vitro model was established using a multiplicity of infection of 100 and evaluating the effectiveness of H. pylori infection by functional analyses. Changes in protein patterns were identified using a proteomic approach consisting of two-dimensional fluorescence difference gel electrophoresis and mass spectrometry. The expression of many proteins was found to be altered, and 28 of these were identified and classified as protein synthesis- and folding-related proteins, cytoskeleton proteins, metabolic enzymes, transcription- and translation-related proteins, angiogenesis/metastasis-related proteins, cell communication/signal transduction-related proteins, or others (oxygen-regulated protein and oncoprotein). The expression profiles of eight of these proteins, laminin γ-1 chain precursor, valosin-containing protein, heat shock 70-kDa protein, mitochondrial matrix protein P1, FK506-binding protein 4, T-complex protein 1, enolase α, and 14-3-3 β were further examined in cancerous and paired surrounding normal tissues by immunoblot assay and immunohistochemical staining to identify molecular targets that may be involved in the pathogenesis of H. pylori-induced gastric diseases. On the basis of our results, valosin-containing protein, mitochondrial matrix protein P1, T-complex protein 1, enolase α, and 14-3-3 β may play a crucial role in H. pylori-induced gastric carcinogenesis by mediating antiapoptotic and proliferative responses. ? 2006 by The American Society for Biochemistry and Molecular Biology, Inc.
|DOI:||10.1074/mcp.M500029-MCP200||metadata.dc.subject.other:||alpha enolase; cytoskeleton protein; fk 506 binding protein; heat shock protein 70; laminin 1; matrix protein; mitochondrial protein; oncoprotein; protein 14 3 3; angiogenesis; article; cancer tissue; carcinogenesis; cell communication; cellular distribution; controlled study; epithelium cell; gastrointestinal disease; gene expression profiling; genetic transcription; Helicobacter infection; Helicobacter pylori; human; human cell; immunoblotting; immunohistochemistry; in vitro study; mass spectrometry; nonhuman; nucleotide sequence; priority journal; protein analysis; protein expression; protein folding; protein function; protein localization; protein synthesis; proteomics; RNA translation; stomach cancer; stomach epithelium; two dimensional gel electrophoresis; Blotting, Western; Cyclooxygenase 2; Electrophoresis, Gel, Two-Dimensional; Helicobacter pylori; Interleukin-8; Mass Spectrometry; Proteomics; Subcellular Fractions; Helicobacter; Helicobacter pylori
|Appears in Collections:||醫學系|
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