| Project/Area Number |
11680702
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Cell biology
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| Research Institution | SAPPORO MEDICAL UNIVERSITY SCHOOL OF MEDICINE |
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Principal Investigator |
KOKAI Yasuo Department of Pathology Sapporo Medical University School of Medicine, 医学部, 助教授 (20178239)
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| Co-Investigator(Kenkyū-buntansha) |
TOBIOKA Hirotoshi Department of Pathology Sapporo Medical University School of Medicine, 医学部, 助手 (90291559)
森 道夫 札幌医科大学, 医学部, 教授 (00045288)
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| Project Period (FY) |
1999 – 2000
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| Project Status |
Completed (Fiscal Year 2000)
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| Budget Amount *help |
¥3,700,000 (Direct Cost: ¥3,700,000)
Fiscal Year 2000: ¥1,400,000 (Direct Cost: ¥1,400,000)
Fiscal Year 1999: ¥2,300,000 (Direct Cost: ¥2,300,000)
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| Keywords | Tight junction / barmotin / occludin / gap junction / connexin 32 / barrier / H.pylori / 細胞バリア / タイト結合 / 7H6 / バーモチン / アクチン / バリア / フェンス / 疾患 |
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| Research Abstract |
Tight junctions localize uppermost of apposing epithelium and a class of endothelium. Tight junctions serve as a barrier for paracellular pathway and regulate traffics of ion, small molecules and cells. In the present projects, we studied molecular aspects of tight junction related proteins and its role in pathological conditions, such as bacterial gastritis by H.pylori. To perform this, we developed a model to study pathological role of tight junctions in human disease. Study using H.pylori adapted for murine stomach revealed tight junctions play an important role for these bacteria to colonize in the murine stomach. This observation suggests that up-regulation of paracellular barrier of gastric mucosa may prevent H.pylori colonization which leads to neutrophilic gastritis and strongly links to gastric carcinoma and lymphoma. We also elucidated that molecular regulation of tight junction related molecules by gap junction molecule, designated Cx32. This observation has opened up an opportunity to dissect how tight junctions develop and regulate as a member of junctional complex at the cell-cell contacts.
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