2002 Fiscal Year Final Research Report Summary
Inhibition of N-end rule-dependent proteolysis by dipeptide
| Project/Area Number |
13670065
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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 |
Environmental physiology (including Physical medicine and Nutritional physiology)
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| Research Institution | The University of Tokushima |
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Principal Investigator |
NIKAWA Takeshi The University of Tokushima School of Medicine Assistant Professor, 医学部, 助手 (20263824)
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| Co-Investigator(Kenkyū-buntansha) |
SHIBAHARA Susumu Ajinomoto Co.Research Institute for Health Fundamentals, Associate General Manager and Section Manager, 栄養健康科学研究班, 主任研究員
ROKUTAN Kazuhito The University of Tokushima School of Medicine AssociateProfessor, 医学部, 助教授 (10230898)
KISHI Kyoichi The University of Tokushima School of Medicine Professor, 医学部, 教授 (80035435)
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| Project Period (FY) |
2001 – 2002
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| Keywords | ubiquitin system / dipepide / L6 cells / oxidatiye stress / disuse muscle atrophy |
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| Research Abstract |
In the joint project with National Space Development Agency of Japan (NASDA), we found that ubiquitin - dependent proteolysis plays an important role in muscle atrophy caused by spaceflight. The essential component of one degradation signal in this proteolytic pathway is a destabilizing N-terminal residue of a protein (the N-end rule). Interestingly, the protein degradation in this system is inhibited by dipeptide. In the present study, we examine suppressive effect of various dipeptides on protein - ubiquitination induced by oxidative stress, which triggers ubiquitination of muscle proteins in space. In rat myoblastic L6 cells treated with 0.5 Mm hydrogen peroxide, many proteins with low molecular masses were ubiquitinated. By a micro-sequencing analysis, we identified a ubiquitinated protein with a molecular mass of 37 kDa as an enzyme in glycolytic pathway. We also found that several dipeptides, such as Ala-X and Ala-Y, affect its ubiquitination : the former significantly suppressed the ubiquitination, while the latter further enhanced it. Our results suggest that some dipeptides could affect glycolysis in skeletal muscle by regulating the ubiquitin system.
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Research Products
(18 results)
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[Publications] Kano M, Kitado M, Hirosaka K , Sanoma Y, Ogawa T, Takeda S, Konaka I, Adams GR, Baldwin KM, Oarads M, Kishi K, Nikawa T: "Isolation and characterization oh a novel gene Sfig in rat skeletal muscle up-regulated by spaceflight (STS-90)"J Med Invest. 50(1-2). 39-47 (2003)
Description
「研究成果報告書概要(欧文)」より
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[Publications] Ikemoto M, Nikawa T, Takeda S, Watanabe C, Kitano T, Baldwin KM, Izumi R, Nonaka I, Towatari T, Teshima S, Rokutan K, Kishi K: "Space shuttle flight (STS-90) enhances degradation of rat myosin heavy chain in association with activation of ubiquitin-proteasome pathway"FASEB J. 15(7). 1279-1281 (2001)
Description
「研究成果報告書概要(欧文)」より
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