Mechanism of oxidative stress in skeletal muscle atrophied by immobilization

H Kondo, I Nakagaki, S Sasaki, S Hori, Y Itokawa

研究成果: ジャーナルへの寄稿記事

134 引用 (Scopus)

抄録

To clarify the mechanism of oxidative stress in skeletal muscle atrophied by immobilization, we measured the activities of antioxidant enzymes and xanthine oxidase (XOD) and carried out the cytochemical study of hydrogen peroxide in a typical slow red muscle, the soleus. Male Wistar rats (15 wk old), of which ankle joints of one hindlimb were immobilized in the fully extended position, were killed after 4, 8, or 12 days. The activities of Mn-containing superoxide dismutase (Mn-SOD), Cu-Zn-containing superoxide dismutase (Cu-Zn-SOD), Se-dependent glutathione peroxidase (Se-GSHPx), glutathione S-transferase, catalase, and glutathione reductase were measured spectrophotometrically. The XOD activity and the concentrations of hypoxanthine, xanthine, and urate were measured using a high-performance liquid chromatography. The cytochemical study of hydrogen peroxide in short-term organ culture was performed using an electron microscope. Increased Cu-Zn-SOD and decreased Mn-SOD in atrophy might reflect increased generation of superoxide anions in the cytoplasm rather than in the mitochondria. The source of superoxide anions in the cytoplasm might be the increased superoxide-producing XOD. Enhanced generation of superoxide anions and increased Cu-Zn-SOD activity in atrophy suggested the enhanced generation of hydrogen peroxide in the cytoplasm. Due to the unchanged activity of Se-GSHPx and the unchanged or slightly increased activity of catalase in atrophy, the ability to degrade hydrogen peroxide might not increase so much. Hence, hydrogen peroxide is expected to be increased in atrophy. The cytochemical study supported this expectation.(ABSTRACT TRUNCATED AT 250 WORDS)

元の言語英語
ページ(範囲)E839-44
ジャーナルAmerican Journal of Physiology - Cell Physiology
265
発行部数6 Pt 1
出版物ステータス出版済み - 12 1993

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Immobilization
Hydrogen Peroxide
Skeletal Muscle
Oxidative Stress
Superoxides
Atrophy
Xanthine Oxidase
Cytoplasm
Catalase
Superoxide Dismutase
Hypoxanthine
Xanthine
Ankle Joint
Glutathione Reductase
Organ Culture Techniques
Hindlimb
Glutathione Peroxidase
Uric Acid
Glutathione Transferase
Wistar Rats

これを引用

Mechanism of oxidative stress in skeletal muscle atrophied by immobilization. / Kondo, H; Nakagaki, I; Sasaki, S; Hori, S; Itokawa, Y.

:: American Journal of Physiology - Cell Physiology, 巻 265, 番号 6 Pt 1, 12.1993, p. E839-44.

研究成果: ジャーナルへの寄稿記事

Kondo, H, Nakagaki, I, Sasaki, S, Hori, S & Itokawa, Y 1993, 'Mechanism of oxidative stress in skeletal muscle atrophied by immobilization', American Journal of Physiology - Cell Physiology, 巻. 265, 番号 6 Pt 1, pp. E839-44.
Kondo, H ; Nakagaki, I ; Sasaki, S ; Hori, S ; Itokawa, Y. / Mechanism of oxidative stress in skeletal muscle atrophied by immobilization. :: American Journal of Physiology - Cell Physiology. 1993 ; 巻 265, 番号 6 Pt 1. pp. E839-44.
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AB - To clarify the mechanism of oxidative stress in skeletal muscle atrophied by immobilization, we measured the activities of antioxidant enzymes and xanthine oxidase (XOD) and carried out the cytochemical study of hydrogen peroxide in a typical slow red muscle, the soleus. Male Wistar rats (15 wk old), of which ankle joints of one hindlimb were immobilized in the fully extended position, were killed after 4, 8, or 12 days. The activities of Mn-containing superoxide dismutase (Mn-SOD), Cu-Zn-containing superoxide dismutase (Cu-Zn-SOD), Se-dependent glutathione peroxidase (Se-GSHPx), glutathione S-transferase, catalase, and glutathione reductase were measured spectrophotometrically. The XOD activity and the concentrations of hypoxanthine, xanthine, and urate were measured using a high-performance liquid chromatography. The cytochemical study of hydrogen peroxide in short-term organ culture was performed using an electron microscope. Increased Cu-Zn-SOD and decreased Mn-SOD in atrophy might reflect increased generation of superoxide anions in the cytoplasm rather than in the mitochondria. The source of superoxide anions in the cytoplasm might be the increased superoxide-producing XOD. Enhanced generation of superoxide anions and increased Cu-Zn-SOD activity in atrophy suggested the enhanced generation of hydrogen peroxide in the cytoplasm. Due to the unchanged activity of Se-GSHPx and the unchanged or slightly increased activity of catalase in atrophy, the ability to degrade hydrogen peroxide might not increase so much. Hence, hydrogen peroxide is expected to be increased in atrophy. The cytochemical study supported this expectation.(ABSTRACT TRUNCATED AT 250 WORDS)

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