The role of multimerin1 and VacA, an exotoxin released by H. pylori on ITP.
| Project/Area Number |
23591378
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Hematology
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| Research Institution | University of Yamanashi |
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Principal Investigator |
OZAKI Yukio 山梨大学, 医学工学総合研究部, 教授 (30134539)
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| Co-Investigator(Kenkyū-buntansha) |
SATOH Kaneo 山梨大学, 医学部, 助手 (20242662)
TAKANO Katsuhiro 山梨大学, 医学部附属病院, 助教 (60382925)
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| Project Period (FY) |
2011 – 2013
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| Project Status |
Completed (Fiscal Year 2013)
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| Budget Amount *help |
¥5,330,000 (Direct Cost: ¥4,100,000、Indirect Cost: ¥1,230,000)
Fiscal Year 2013: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2012: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2011: ¥3,120,000 (Direct Cost: ¥2,400,000、Indirect Cost: ¥720,000)
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| Keywords | VacA / Helicobactor pylori / 特発性血小板減少性紫斑病 / multimerin1 / platelet / 血液内科学 / multimerin 1 / 特発性血小板減少症 / ヘリコバクターピロリ / マルチメリン / 毒素 |
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| Research Abstract |
Platelets were activated under the infection with H. pylori in human and mice. We investigated the role of VacA, an exotoxin released by H. pylori in this context. Acid-activated VacA, but not heated VacA, induced platelet CD62P expression. However, VacA reacted with none of the alleged VacA receptors present on platelet membranes. We therefore analyzed VacA associated proteins obtained through VacA affinity chromatography, using MALDI-TOF-MS. Multimerin1 was detected in two consecutive experiments, as the binding protein for VacA. Plasmon resonance confirmed their binding, and dot print analysis revealed that the peptide sequence AA 321-340 of multimerin 1 is the binding site for VacA. In conclusion, we propose a new interaction between multimerin1 and VacA , which may give another insight into H. pylori-induced platelet activations under H. pylori infection.
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Report
(4 results)
Research Products
(9 results)
