2005 Fiscal Year Final Research Report Summary
The function of ubiquitin in intralysosomal protein degradation.
Project/Area Number |
16590235
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
General medical chemistry
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Research Institution | Tokushima Bunri University |
Principal Investigator |
ISHIDOH Kazumi Tokushima Bunri University, Intsitute for Health Sciences, Division of Molecular Biology, Professor, 健康科学研究所・分子生物学部門, 教授 (40212906)
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Project Period (FY) |
2004 – 2005
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Keywords | lysosome / protein degradation / ubiquitin / insulin receptor / epidermal growth factor receptor / platelet derived growth factor receptor / LDH-A |
Research Abstract |
HA-c-Cbl was expressed in HEK293 cells and immunoprecipitated. Insulin receptor expressed in HIRc cells was immunoprecipitaed. Then Both immunoprecipitants were mixed with E1,UbcH7 as an E2,ATP and its regenerating system, ubiquitin or its mutants. These mixtures were reacted in pH6.0, 6.5 and 7.2. Ubiquitinated insulin receptor were detected by immunoblot. When the reaction was done at pH7.2, insulin receptor were monoubiquitinated with multiple lysine residues in insulin receptor, whereas when the reaction was carried out at pH6.0, the insulin receptor was subjected to polyubiqutination through Lys-48 in ubiquitin molecules. Therefore, I projected next to analyze the structural change of recombinant c-Cbl between neutral pH and acidic pH. Next, I was planed to analyze the ubiquitination profiles of epidermal growth factor receptor and platelet derived growth factor receptor. These projects would be under going. Recently, I identified the monoubiquitination of LDH-A, a cytosolic protein, under oxidative stress was sequestered into and degraded in lysosomes. Now, I would search the ubiquitin receptor on the cytosolic surface of lysosomal membranes.
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Research Products
(24 results)
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[Journal Article] Identification of mono-ubiquitinated LDH-A in skeletal muscle cells exposed to oxidative stress.2005
Author(s)
Onishi Y, Hirasaka K, Ishihara I, Oarada M, Goto J, Ogawa T, Suzue N, Nakano S, Furochi H, Ishidoh K, Kishi K, Nikawa T.
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Journal Title
Biochem.Biophys.Res.Commun. 336
Pages: 799-806
Description
「研究成果報告書概要(欧文)」より
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[Journal Article] Skeltal muscle gene expression in space-flown rats.2004
Author(s)
Nikawa, T., Ishidoh, K., Hirasaka, K., Ishihara, K., Ikemoto, M., Kano, K., Kominami, E., NOnaka, I., Ogawa, T., Adam, G.R., Baldwin, K.M., Yasui, N., Kishi, K., Takeda, S.
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Journal Title
FASEB.J. 18
Pages: 522-524
Description
「研究成果報告書概要(欧文)」より
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[Journal Article] Inflammatory response and cathepsins in silica-exposed Hermansky-Pudlock syndrome medel pale year mice.2004
Author(s)
Yoshioka, Y., Kumasaka, T., Ishidoh, K., Kominami, E., Mitani, K., Hosokawa, Y., Fukuchi, Y.
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Journal Title
Pathology Int. 54
Pages: 322-331
Description
「研究成果報告書概要(欧文)」より
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[Journal Article] Mammalian class E Vps proteins, SBP1 and mVps2/CHMP2A, interact with and regulate the function of an AAA-ATPase SKD1/Vps4B.2004
Author(s)
Fujita, H., Umezaki, Y., Imamura, K., Ishikawa, D., Uchimura, S., Nara, A., Yoshimori, T., Hayashizaki, Y., Kawai, J., Ishidoh, K., Tanaka Y., Himeno, M.
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Journal Title
J.Cell Sci. 117
Pages: 2997-3009
Description
「研究成果報告書概要(欧文)」より
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[Journal Article] Podocyte migration during nephrotic syndrome requires a coordinated interplay between cathepsin L and a3 integrin.2004
Author(s)
Reiser J, Oh J, Shirato I, Asanuma K, Hug A, Mundel TM, Honey K, Ishidoh K, Kominami E, Kreidberg JA, Tomino Y, Mundel P.
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Journal Title
J.Biol.Chem. 279
Pages: 34827-34832
Description
「研究成果報告書概要(欧文)」より
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[Journal Article] Ubiquitin ligase Cbl-b downregulates bone formation through suppression of IGF-I signaling in osteoblasts during denervation.
Author(s)
Suzue N, Nikawa T, Onishi Y, Yamada, C, Hirasaka K, Ogawa T, Furochi H, Kosaka H, Ishidoh K, Gu H, Takeda S, Ishimaru N, Hayashi Y, Yamamoto H, Kishi K, Yasui N
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Journal Title
J.Bone Mineral Res. (In press)
Description
「研究成果報告書概要(欧文)」より
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