pubmed-article:18362137 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:18362137 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
pubmed-article:18362137 | lifeskim:mentions | umls-concept:C0085508 | lld:lifeskim |
pubmed-article:18362137 | lifeskim:mentions | umls-concept:C0014597 | lld:lifeskim |
pubmed-article:18362137 | lifeskim:mentions | umls-concept:C1704242 | lld:lifeskim |
pubmed-article:18362137 | lifeskim:mentions | umls-concept:C0010840 | lld:lifeskim |
pubmed-article:18362137 | lifeskim:mentions | umls-concept:C1420536 | lld:lifeskim |
pubmed-article:18362137 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
pubmed-article:18362137 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
pubmed-article:18362137 | pubmed:issue | 6 | lld:pubmed |
pubmed-article:18362137 | pubmed:dateCreated | 2008-5-20 | lld:pubmed |
pubmed-article:18362137 | pubmed:abstractText | Helicobacter pylori-produced cytotoxin VacA induces intracellular vacuolation. The VacA-induced vacuole is assumed to represent the pathological status of intracellular trafficking. The fusion mechanism of the endosomes requires the formation of a tight complex between the Q-SNAREs and the R-SNAREs. We recently reported that syntaxin 7, a family member of the Q-SNARE protein, is involved in VacA-induced vacuole formation. In order to further elucidate the molecular mechanism, we identified the participation of vesicle-associated membrane protein 7 (VAMP7) as a partner of syntaxin 7. Immunocytochemistry revealed endogenous VAMP7 to be localized to the vacuoles induced by VacA. A Northern blotting study demonstrated that VacA intoxication increased VAMP7 mRNA in a time-dependent manner. VAMP7 was coimmunoprecipitated with syntaxin 7, and the amounts of endogenous VAMP7 and syntaxin 7 bound to syntaxin 7 and VAMP7, respectively, increased in response to VacA. The down-regulation of VAMP7 using small interfering RNA inhibited VacA-induced vacuolation, and the transient transfection of dominant-negative mutant VAMP7, the N-terminal domain of VAMP7, also inhibited the vacuolation. We therefore conclude that R-SNARE VAMP7 plays an important role in VacA-induced vacuolation as a partner of Q-SNARE syntaxin 7. | lld:pubmed |
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pubmed-article:18362137 | pubmed:language | eng | lld:pubmed |
pubmed-article:18362137 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18362137 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:18362137 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:18362137 | pubmed:month | Jun | lld:pubmed |
pubmed-article:18362137 | pubmed:issn | 1098-5522 | lld:pubmed |
pubmed-article:18362137 | pubmed:author | pubmed-author:SuzukiJunkoJ | lld:pubmed |
pubmed-article:18362137 | pubmed:author | pubmed-author:FujitaToshiro... | lld:pubmed |
pubmed-article:18362137 | pubmed:author | pubmed-author:OmataMasaoM | lld:pubmed |
pubmed-article:18362137 | pubmed:author | pubmed-author:HirayamaToshi... | lld:pubmed |
pubmed-article:18362137 | pubmed:author | pubmed-author:YasudaHiroshi... | lld:pubmed |
pubmed-article:18362137 | pubmed:author | pubmed-author:OhnoHidekiH | lld:pubmed |
pubmed-article:18362137 | pubmed:author | pubmed-author:OhnishiHirohi... | lld:pubmed |
pubmed-article:18362137 | pubmed:author | pubmed-author:MashimaHirosa... | lld:pubmed |
pubmed-article:18362137 | pubmed:author | pubmed-author:YoshikumiYuka... | lld:pubmed |
pubmed-article:18362137 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:18362137 | pubmed:volume | 76 | lld:pubmed |
pubmed-article:18362137 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:18362137 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:18362137 | pubmed:pagination | 2296-303 | lld:pubmed |
pubmed-article:18362137 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:18362137 | pubmed:meshHeading | pubmed-meshheading:18362137... | lld:pubmed |
pubmed-article:18362137 | pubmed:year | 2008 | lld:pubmed |
pubmed-article:18362137 | pubmed:articleTitle | Involvement of vesicle-associated membrane protein 7 in human gastric epithelial cell vacuolation induced by Helicobacter pylori-produced VacA. | lld:pubmed |
pubmed-article:18362137 | pubmed:affiliation | Department of Gastroenterology, Graduate School of Medicine, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8655, Japan. hmashima1-tky@umin.ac.jp | lld:pubmed |
pubmed-article:18362137 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:18362137 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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