Adriamycin-Fe^<3+>-Induced Mitochondrial Protein Damage with Lipid Peroxidation
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概要
- 論文の詳細を見る
Exposure of mitochondria to adriamycin (ADM)-Fe^<3+> induced formation of thiobarbituric acid reactive substances and fluorescent substances. Butylated hydroxytoluene (BHT) and the water soluble vitamin E analogue, trolox, not only strongly inhibited fluorescence formation but also mitochondrial lipid peroxidation. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis indicated the formation of high molecular weight proteins when mitochondria were exposed to ADM-Fe^<3+>. A mitochondrial protein with a molecular weight of approximately 30 kDa was very sensitive to ADM-Fe^<3+>. BHT and trolox strongly inhibited mitochondrial protein cross-linking, indicating that the protein modification was due to ADM-Fe^<3+>-induced lipid peroxidation. In addition, the susceptibility of ADM-Fe^<3+>-exposed mitochondrial protein to proteases was unchanged. Bovine serum albumin (BSA) inhibited ADM-Fe^<3+>-induced mitochondrial lipid peroxidation. Fluorescence emmited from BSA was detected during ADM-Fe^<3+>-induced mitochondrial lipid peroxidation, and BHT strongly inhibited the oxidative modification of BSA. These results suggest that the oxidative modification of mitochondrial proteins and BSA is due to ADM-Fe^<3+>-induced lipid peroxidation.
- 公益社団法人日本薬学会の論文
- 1995-04-15
著者
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小木曽 健人
Hokkaido Institute Of Pharmaceutical Sciences
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三浦 俊明
Department of Biochemistry, Hokkaido Institute of Pharmaceutical Sciences
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村岡 早苗
Department of Biochemistry, Hokkaido Institute of Pharmaceutical Sciences
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小木曽 健人
Department of Biochemistry, Hokkaido Institute of Pharmaceutical Sciences
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三浦 俊明
北海道薬科大学
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Ogiso T
Hokkaido Institute Of Pharmaceutical Sciences
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村岡 早苗
Department Of Biochemistry Hokkaido Institute Of Pharmaceutical Sciences
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