| Project/Area Number |
22790378
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Experimental pathology
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| Research Institution | Hamamatsu University School of Medicine |
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Principal Investigator |
GOTO Masanori 浜松医科大学, 医学部, 特別研究員 (00432203)
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| Project Period (FY) |
2010 – 2012
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| Project Status |
Completed (Fiscal Year 2012)
|
| Budget Amount *help |
¥4,030,000 (Direct Cost: ¥3,100,000、Indirect Cost: ¥930,000)
Fiscal Year 2012: ¥780,000 (Direct Cost: ¥600,000、Indirect Cost: ¥180,000)
Fiscal Year 2011: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2010: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
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| Keywords | 8-ヒドロキシグアニン / MUTYH / エテノアダクト / 塩基除去修復遺伝子 / 大腸がん / 活性酸素種 / 過酸化脂質 / 塩基除去修復酵素 / TDG / 塩基除去修復 / 胃がん |
|---|
| Research Abstract |
We successfully prepared highly homogeneous human MUTYH recombinant protein, and compared the repair activity of 14 variant proteins with that of the wild -type protein. Several variant proteins showed striking low activity, and their variants may contribute to the development of MUTYH-associated polyposis. To search new substrate of base excision repair enzymes, we prepared 8 enzymes, and examined the repair activity against an oligonucleotide containing etheno-DNA adducts, a lipid peroxidation-derived DNA adducts. The base excision repair enzyme, TDG, had activity that is capable of removing thymine mispaired with etheno-DNA adduct of cytosine or guanine.
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