Open AccessDetection of a mouse OGG1 fragment during caspase‐dependent apoptosis: Oxidative DNA damage and apoptosis
Author(s) -
Hirano Takeshi,
Kawai Kazuaki,
Ootsuyama Yuko,
Orimo Hiroshi,
Kasai Hiroshi
Publication year - 2004
Publication title -
cancer science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.035
H-Index - 141
eISSN - 1349-7006
pISSN - 1347-9032
DOI - 10.1111/j.1349-7006.2004.tb03321.x
Subject(s) - dna fragmentation , apoptosis , apoptotic dna fragmentation , fragmentation (computing) , etoposide , dna damage , dna glycosylase , dna , microbiology and biotechnology , biology , dna repair , programmed cell death , chemistry , biochemistry , genetics , ecology , chemotherapy
We investigated the expression of mouse 8‐oxoguanine DNA glycosylase 1 (mOGG1) in mouse non‐parenchymal hepatocytes (NCTC) during etoposide‐ or mitomycin C (MMC‐induced apoptosis. We observed mOGG1 fragmentation in apoptotic cells. The apoptosis accompanying the fragmentation of mOGG1 was caspase‐dependent. The mOGG1 fragment existed in both the cytoplasm and nucleus of the etoposide‐treated NCTC, indicating that the mOGG1 fragment could be transferred into the nucleus. In addition, 8‐hydroxyguanine (8‐OH‐Gua, 7,8‐dihydro‐8‐oxoguanine) accumulated in the DNA of NCTC treated with etoposide, suggesting that the mOGG1 fragment might not function as a normal repair enzyme in etoposide‐treated NCTC. Although we have not clarified in detail the mechanism and the significance of the mOGG1 fragmentation, further study of the fragmentation of DNA repair enzymes might provide insights into the relationship between oxidative DNA damage and apoptosis.