1997 Fiscal Year Final Research Report Summary
Analysis of human brain proteins by higy-resolution two dimensional gel electropheresis
| Project/Area Number |
07557051
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| Research Category |
Grant-in-Aid for Scientific Research (A)
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| Allocation Type | Single-year Grants |
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| Section | 展開研究 |
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| Research Field |
Neurology
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| Research Institution | KYOTO UNIVERSITY |
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Principal Investigator |
SHINOHARA Shun Kyoto University, Graduate Schoolof medicine, Assistant Professor, 医学研究科, 助手 (60235687)
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| Co-Investigator(Kenkyū-buntansha) |
KAKUNO Tomisaburo M & S instruments Trading Inc Director chief researcher, 主任研究員 (50029964)
FUJIMOTO Sadaki Kyoto Pharanaceatical University, Professor Science Professor, 薬学部, 教授 (80090182)
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| Project Period (FY) |
1995 – 1997
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| Keywords | Two-dimensional electrophoresis / data base / human brain / Alzheimer's disease / neurodgenerative disease / protein / GFAP / beta-actin |
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| Research Abstract |
Background and amims. Two-dimensional gel electrophoresis (2-DE), a method which can analyze expression of numeraous proteins, is a promising and powerful approach which we began to apply to characterization of the complex pathologic processes in Alzheimer's disease (AD).
Methods. In the present study, a reliable 2-DE database of human brain proteins was created by improving reproducibility of 2-DE images using an immobilized pH gradient (IPG) for the first dimension gel electrophoresis and Melanie II as the program for data analysis.
Results. Among 700 spots on a reference map, we identified three proteins, beta-actin and glial fibrillary acidic protein (GFAP). Comparing density of spots identified on the reference map between AD and control group, we found that 5 protein spots were significantly increased, 28 spots were significantly decreased and 7 spots were specifically detected in AD.Two spots among those significantly increased and one spot among those significantly decreased were identified as GFAP.
Conclusions. The pathophysiology of the changes found awaits forther study. The reference map constructed for the present study ahould be a useful beginning for a comprehensive human 2-DE database available via the Internet, which will facilitate futher investigation of pathogenic protein alterations in AD.
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