| Project/Area Number |
16590320
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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 |
Experimental pathology
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| Research Institution | Oita University |
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Principal Investigator |
MORIYAMA Masatsugu Oita University, Department of Molecular Pathology, Faculty of Medicine, Professor, 医学部, 教授 (90239707)
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| Co-Investigator(Kenkyū-buntansha) |
MATSUURA Keiko Oita University, Department of Molecular Pathology, Faculty of Medicine, Assistant Professor, 医学部, 助手 (00291542)
HIJIYA Naoki Oita University, Department of Molecular Pathology, Faculty of Medicine, Assistant Professor, 医学部, 助手 (80305036)
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| Project Period (FY) |
2004 – 2005
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| Project Status |
Completed (Fiscal Year 2005)
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| Budget Amount *help |
¥3,000,000 (Direct Cost: ¥3,000,000)
Fiscal Year 2005: ¥1,400,000 (Direct Cost: ¥1,400,000)
Fiscal Year 2004: ¥1,600,000 (Direct Cost: ¥1,600,000)
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| Keywords | ARPP / insulin / skeletal muscle / Diabetes Melitus / glucose / Knock-out mouse |
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| Research Abstract |
Recently, we identified a novel human protein, ankyrin-repeated protein with PEST and praline-rich region (ARPP). ARPP is characterized structurally by the presence of four ankyrin-repeated domains in its central portion. The amino acid sequence of ARPP is highly homologous with that of cardiac restricted ankyrin-repeated protein (CARP ; 52%). We observed high expression levels of ARPP in skeletal muscle and the heart. ARPP was selectively expressed in type 1 myofibers of skeletal muscle and, therefore, ARPP-positive myofibers were arranged in a checkerboard-like pattern. In this study, we analyzed the function of ARPP. Our findings are as follows ;
1)ARPP was found to be colocalized with microtubules in HeLa cells transfected with EGFP-ARPP
2)When KB cells were transfected with EGFP-ARPP and stimulated with insulin, EGFP was found to move to cell periphery.
3)ARPP was bound to kinesin, known as a molecular motor.
These findings suggest that ARPP bound to kinesin may be conveyed to cell periphery through microtubules.
Furthermore, we found that glucose-uptake was enhanced when C2 myofibers were treated with insulin, suggesting that ARPP may play a part in insulin-mediated glucose uptake in myofibers. Next, we generated Arpp gene-disrupted mice and analyzed their phenotypes. We found that these mice exhibited impaired glucose-tolerant. These findings suggest that ARPP may be involved in insulin-mediated glucose uptake.
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