Identification of molecules which regulate the podocyte morphology tightly associated with the glomerular filtration.
| Project/Area Number |
15K09275
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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 |
Kidney internal medicine
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| Research Institution | Juntendo University |
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Principal Investigator |
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| Co-Investigator(Kenkyū-buntansha) |
長瀬 美樹 杏林大学, 医学部, 教授 (60302733)
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| Project Period (FY) |
2015-04-01 – 2018-03-31
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| Project Status |
Completed (Fiscal Year 2017)
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| Budget Amount *help |
¥4,810,000 (Direct Cost: ¥3,700,000、Indirect Cost: ¥1,110,000)
Fiscal Year 2017: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2016: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2015: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
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| Keywords | 腎臓学 / 足細胞 / 糸球体濾過 / 形態形成 / 細胞骨格 / ミオシン |
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| Outline of Final Research Achievements |
The localization of myosin IIA heavy chain (NMMHCIIA) in cultured podocyte was analyzed. Cell process formation was induced in cultured podocytes by the treatment with cytochalasin-D. We found that NMMHCIIA was translocated to the bundle of vimentin filaments along the newly formed protrusions from the actin filaments beneath the cell membrane in the resting cell. Plectin was colocalized with the binding site between NMMHCIIA and vimentin. R702C mutation of NMMHCIIA, which causes Epstein syndrome, showed the decreased binding ability with vimentin and suppressed protrusion formation. The segregation between NMMHCIIA and vimentin was observed in both Epstein kidney and R702C knock-in mouse kidney. Our results indicate that NMMHCIIA binds to the intermediate filaments in the podocyte and play an important role in maintaining the unique cell structure of this cell. R702C mutation induces the change of binding ability with vimentin and results in the morphological change of the podocyte.
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Report
(4 results)
Research Products
(17 results)
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[Journal Article] Lipoarabinomannan binding to lactosylceramide in lipid rafts is essential for the phagocytosis of mycobacteria by human neutrophils2016
Author(s)
Nakayama H, Kurihara H, Morita YS, Kinoshita T, Mauri L, Prinetti A, Sonnino S, Yokoyama N, Ogawa H, Takamori K, Iwabuchi K
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Journal Title
Sci Signal
Volume: 11
Issue: 449
Pages: 0-0
DOI
Related Report
Peer Reviewed / Open Access / Int'l Joint Research
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