@article{oai:repo.qst.go.jp:00057190,
 author = {續, 輝久 and 山内, 一己 and 磯田, 拓郎 and 江頭, 明典 and 藏, 忍 and 中津, 可道 and 山内 一己},
 issue = {2},
 journal = {環境変異原研究},
 month = {Oct},
 note = {Oxygen radicals are produced through normal cellular metabolism, and formation of such radicals is further
enhanced by ionizing radiation and by various chemicals. Among various classes of oxidative DNA damage,
8-oxo-7,8-dihydroguanine (8-oxoG) is the most abundant, and appears to play important roles in mutagenesis
and carcinogenesis. Enzymatic activities that may be responsible for preventing 8-oxoG-evoked
mutations were identified in mammalian cells. We have focused on following the two enzymes. MTH1
(Mth1) protein is the mammalian counterpart of E. coli MutT protein, which hydrolyzes 8-oxo-dGTP to its
monophosphate form in the nucleotide pool, thereby preventing the incorporation of the mutagenic substrate
into DNA. On the other hand, MUTYH (Mutyh) protein, a counterpart of E. coli MutY protein, having
adenine/2-hydroxyadenine DNA glycosylase activity, is expected to prevent G:C to T:A transversions, by
excising adenine from G:A mismatches induced by 8-oxoG and 2-OH-A. To analyze the function of the mammalian
Mth1 and Mutyh proteins in vivo, we established gene-knockout mice for these two enzymes by gene
targeting, and investigated spontaneous tumorigenesis as well as mutagenesis. Here we discuss our recent
progress on spontaneous and oxidative stress-induced mutagenesis with these mutant mouse lines.},
 pages = {101--110},
 title = {酸化的DNA損傷誘発突然変異を回避する分子機構 ─DNA修復欠損マウスにおける突然変異と発がんの解析─},
 volume = {27},
 year = {2005}
}