2012 Fiscal Year Final Research Report
Mechanism of abnormal protein aggregation and the study of the repair enzyme.
| Project/Area Number |
20350077
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Chemistry related to living body
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| Research Institution | Kyoto University |
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Principal Investigator |
FUJII Noriko 京都大学, 原子炉実験所, 教授 (90199290)
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| Co-Investigator(Kenkyū-buntansha) |
SUGIYAMA Masaaki 京都大学, 原子炉実験所, 教授 (10253395)
MORIMOTO Yukio 京都大学, 原子炉実験所, 教授 (80200450)
KINOUCHI Tadatoshi 京都大学, 原子炉実験所, 講師 (90301457)
SAITO Takeshi 京都大学, 原子炉実験所, 助教 (10274143)
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| Co-Investigator(Renkei-kenkyūsha) |
SADAKANE Yutaka 鈴鹿医療科学大学, 薬学部, 教授 (60293304)
KAJI Yuichi 筑波大学, 医学部, 准教授 (50361332)
SASAKI Horoshi 金沢医科大学, 医学部, 教授 (60260840)
GOTO Yuji 大阪大学, 蛋白質研究所, 教授 (40153770)
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| Project Period (FY) |
2008 – 2012
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| Keywords | 蛋白質の異常凝集 / D-アミノ酸 |
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| Research Abstract |
Abnormal aggregation in protein from age-related diseases such as cataracts, age-related macular degeneration and solar elastosis has been observed. In this study, we examined the biologically uncommon D-amino acids in the cataractous eye lens and UV-damaged skin of elderly individuals. The formation of the D- amino acids in the protein was accelerated by UV-irradiation and oxidative stress. We proposed that D-amino acids may be one of the triggers for abnormal aggregation of proteins and can induce the partial unfolding of the corresponding proteins, leading to a diseased state. We demonstrated a new method for the analysis of isomerization of individual Asp residues in proteins using LC-MS. This makes it possible to analyze isomers of Asp residues in proteins precisely and quickly.
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