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Volumn 139, Issue 2, 1996, Pages 180-186

Extraocular, limb and diaphragm muscle group-specific antioxidant enzyme activity patterns in control and mdx mice

Author keywords

Antioxidant enzyme; Mdx mouse; Muscular dystrophy; Skeletal muscle

Indexed keywords

ANTIOXIDANT; COPPER ZINC SUPEROXIDE DISMUTASE; GLUTATHIONE PEROXIDASE; GLUTATHIONE REDUCTASE; MANGANESE SUPEROXIDE DISMUTASE;

EID: 0030218009     PISSN: 0022510X     EISSN: None     Source Type: Journal    
DOI: 10.1016/0022-510X(96)00066-4     Document Type: Article
Times cited : (54)

References (65)
  • 1
    • 0024359181 scopus 로고
    • Lipid peroxide and antioxidant enzymes in muscle and non-muscle of dystrophic mouse
    • Asayama, K., Hayashiba, H., Dobashi, K. and Kato, K. (1989) Lipid peroxide and antioxidant enzymes in muscle and non-muscle of dystrophic mouse. Muscle Nerve, 12: 742-748.
    • (1989) Muscle Nerve , vol.12 , pp. 742-748
    • Asayama, K.1    Hayashiba, H.2    Dobashi, K.3    Kato, K.4
  • 2
    • 0026777351 scopus 로고
    • Potential oxyradical damage and energy status in individual muscle fibers from degenerating muscle diseases
    • Austin, L., DeNiese, M., McGregor, A., Arthur, W., Gurusinghe, A. and Gould, M.K. (1992) Potential oxyradical damage and energy status in individual muscle fibers from degenerating muscle diseases. Neuromuscul. Disord., 2: 27-33.
    • (1992) Neuromuscul. Disord. , vol.2 , pp. 27-33
    • Austin, L.1    DeNiese, M.2    McGregor, A.3    Arthur, W.4    Gurusinghe, A.5    Gould, M.K.6
  • 3
    • 0024335821 scopus 로고
    • The pathological damage in Duchenne muscular dystrophy may be due to increased intracellular oxyradical generation caused by the absence of dystrophin and subsequent alterations in calcium metabolism
    • Baker, M.S. and Austin, L. (1989) The pathological damage in Duchenne muscular dystrophy may be due to increased intracellular oxyradical generation caused by the absence of dystrophin and subsequent alterations in calcium metabolism. Med. Hypotheses, 29: 187-193.
    • (1989) Med. Hypotheses , vol.29 , pp. 187-193
    • Baker, M.S.1    Austin, L.2
  • 4
    • 0027340242 scopus 로고
    • Calcium levels in myotubes grown from the skeletal muscle of dystrophic (mdx) and normal mice
    • Bakker, A.J., Head, S.I., Williams, D.A. and Stephenson, D.G. (1993) Calcium levels in myotubes grown from the skeletal muscle of dystrophic (mdx) and normal mice. J. Physiol. (Lond.), 460: 1-13.
    • (1993) J. Physiol. (Lond.) , vol.460 , pp. 1-13
    • Bakker, A.J.1    Head, S.I.2    Williams, D.A.3    Stephenson, D.G.4
  • 7
    • 0029149471 scopus 로고
    • Nitric oxide synthase complexed with dystrophin and absent from skeletal muscle sarcolemma in Duchenne muscular dystrophy
    • Brenman, J.E., Chao, D.S., Xia, H., Aldape, K. and Bredt, D.S. (1995) Nitric oxide synthase complexed with dystrophin and absent from skeletal muscle sarcolemma in Duchenne muscular dystrophy. Cell, 82: 743-752.
    • (1995) Cell , vol.82 , pp. 743-752
    • Brenman, J.E.1    Chao, D.S.2    Xia, H.3    Aldape, K.4    Bredt, D.S.5
  • 8
    • 0018963739 scopus 로고
    • Rat hepatic cytosolic glutathione dependent enzyme protection against lipid peroxidation in the NADPH-microsomal lipid peroxidation system
    • Burk, R.F., Trumble, M.J. and Lawrence, R.A. (1980) Rat hepatic cytosolic glutathione dependent enzyme protection against lipid peroxidation in the NADPH-microsomal lipid peroxidation system. Biochim. Biophys. Acta, 618: 35-41.
    • (1980) Biochim. Biophys. Acta , vol.618 , pp. 35-41
    • Burk, R.F.1    Trumble, M.J.2    Lawrence, R.A.3
  • 9
    • 0023125464 scopus 로고
    • Superoxide dismutase, glutathione peroxidase and catalase in neuromuscular disease
    • Burr, I.M., Asayama, K. and Fenichel, G.M. (1987) Superoxide dismutase, glutathione peroxidase and catalase in neuromuscular disease. Muscle Nerve, 10: 150-154.
    • (1987) Muscle Nerve , vol.10 , pp. 150-154
    • Burr, I.M.1    Asayama, K.2    Fenichel, G.M.3
  • 10
    • 0025931224 scopus 로고
    • The subcellular distribution of dystrophin in mouse skeletal, cardiac and smooth muscle
    • Byers, T.J., Kunkel, L.M. and Watkins, S.C. (1991) The subcellular distribution of dystrophin in mouse skeletal, cardiac and smooth muscle. J. Cell Biol., 115: 411-421.
    • (1991) J. Cell Biol. , vol.115 , pp. 411-421
    • Byers, T.J.1    Kunkel, L.M.2    Watkins, S.C.3
  • 12
    • 0023244894 scopus 로고
    • Muscular dystrophy in the mdx mouse: Histopathology of the soleus and extensor digitorum longus muscles
    • Carnwath, J.W. and Shotton, D.M. (1987) Muscular dystrophy in the mdx mouse: histopathology of the soleus and extensor digitorum longus muscles. J. Neurol. Sci., 80: 39-54.
    • (1987) J. Neurol. Sci. , vol.80 , pp. 39-54
    • Carnwath, J.W.1    Shotton, D.M.2
  • 13
    • 0024674150 scopus 로고
    • The effect of ischemia-reperfusion derived oxygen free radicals on skeletal muscle calcium metabolism
    • Cronenwett, J.L., Lee, K.R., Shlafer, M. and Zelenock, G.B. (1989) The effect of ischemia-reperfusion derived oxygen free radicals on skeletal muscle calcium metabolism. Microcirc. Endothelium Lymphatics, 5: 171-187.
    • (1989) Microcirc. Endothelium Lymphatics , vol.5 , pp. 171-187
    • Cronenwett, J.L.1    Lee, K.R.2    Shlafer, M.3    Zelenock, G.B.4
  • 14
    • 0027946294 scopus 로고
    • Development of central nervous system pathology in a murine transgenic model of human amyotrophic lateral sclerosis
    • Dal Canto, M.C. and Gurney, M.E. (1994) Development of central nervous system pathology in a murine transgenic model of human amyotrophic lateral sclerosis. Am. J. Pathol., 145: 1271-1279.
    • (1994) Am. J. Pathol. , vol.145 , pp. 1271-1279
    • Dal Canto, M.C.1    Gurney, M.E.2
  • 15
    • 0021713536 scopus 로고
    • Muscle development in mdx mutant mice
    • Dangain, J. and Vrbova, G. (1984) Muscle development in mdx mutant mice. Muscle Nerve, 7: 700-704.
    • (1984) Muscle Nerve , vol.7 , pp. 700-704
    • Dangain, J.1    Vrbova, G.2
  • 16
    • 0019264856 scopus 로고
    • An approach to free radicals in medicine and biology
    • DelMaestro, R.F. (1980) An approach to free radicals in medicine and biology. Acta Physiol. Scand. Suppl., 492: 153-168.
    • (1980) Acta Physiol. Scand. Suppl. , vol.492 , pp. 153-168
    • DelMaestro, R.F.1
  • 17
    • 0026038987 scopus 로고
    • Fiber regeneration is not persistent in dystrophic (mdx) mouse skeletal muscle
    • DiMario, J.X., Uzman, A. and Strohman, R.C. (1991) Fiber regeneration is not persistent in dystrophic (mdx) mouse skeletal muscle. Dev. Biol., 148: 314-321.
    • (1991) Dev. Biol. , vol.148 , pp. 314-321
    • DiMario, J.X.1    Uzman, A.2    Strohman, R.C.3
  • 18
    • 0024515328 scopus 로고
    • Lipid peroxidation and superoxide dismutase activity in muscle and erythrocytes in adult muscular dystrophies and neurogenic atrophies
    • Dioszeghy, P., Imre, S. and Mechler, F. (1989) Lipid peroxidation and superoxide dismutase activity in muscle and erythrocytes in adult muscular dystrophies and neurogenic atrophies. Eur. Arch. Psychiatr. Neurol. Sci., 238: 175-177.
    • (1989) Eur. Arch. Psychiatr. Neurol. Sci. , vol.238 , pp. 175-177
    • Dioszeghy, P.1    Imre, S.2    Mechler, F.3
  • 19
    • 0027479430 scopus 로고
    • Free radicals and calcium homeostasis: Relevance to malignant hyperthermia?
    • Duthie, G.C. and Arthur, J.R. (1993) Free radicals and calcium homeostasis: relevance to malignant hyperthermia? Free Radic. Biol. Med., 14: 435-442.
    • (1993) Free Radic. Biol. Med. , vol.14 , pp. 435-442
    • Duthie, G.C.1    Arthur, J.R.2
  • 20
    • 0022684839 scopus 로고
    • Overproduction of human Cu, Zn-superoxide dismutase in transfected cells: Extenuation of paraquat-mediated cytotoxicity and enhancement of lipid peroxidation
    • Elroy-Stein, O., Bernstein, Y. and Groner, Y. (1986) Overproduction of human Cu, Zn-superoxide dismutase in transfected cells: extenuation of paraquat-mediated cytotoxicity and enhancement of lipid peroxidation. EMBO J., 5:615-622.
    • (1986) EMBO J. , vol.5 , pp. 615-622
    • Elroy-Stein, O.1    Bernstein, Y.2    Groner, Y.3
  • 21
    • 0025222219 scopus 로고
    • Increased activity of calcium leak channels in myotubes of Duchenne human and mdx mouse origin
    • Fong, P., Turner, P.R., Denetclaw, W.F. and Steinhardt, R.A. (1990) Increased activity of calcium leak channels in myotubes of Duchenne human and mdx mouse origin. Science, 250: 673-676.
    • (1990) Science , vol.250 , pp. 673-676
    • Fong, P.1    Turner, P.R.2    Denetclaw, W.F.3    Steinhardt, R.A.4
  • 22
    • 0025317892 scopus 로고
    • Calcium entry through stretch-inactivated ion channels in mdx myotubes
    • Franco, A. and Lansman, J.B. (1990) Calcium entry through stretch-inactivated ion channels in mdx myotubes. Nature, 344: 670-673.
    • (1990) Nature , vol.344 , pp. 670-673
    • Franco, A.1    Lansman, J.B.2
  • 23
    • 0019403539 scopus 로고
    • Prolonged survival after paraquat: Role of the lung antioxidant systems
    • Frank, L. (1981) Prolonged survival after paraquat: role of the lung antioxidant systems. Biochem. Pharmacol., 30: 2319-2324.
    • (1981) Biochem. Pharmacol. , vol.30 , pp. 2319-2324
    • Frank, L.1
  • 24
    • 0022466140 scopus 로고
    • The activation of protein degradation in muscle by calcium or muscle injury does not involve a lysosomal mechanism
    • Furono, K. and Goldberg, A.L. (1986) The activation of protein degradation in muscle by calcium or muscle injury does not involve a lysosomal mechanism. Biochem. J., 237: 859-864.
    • (1986) Biochem. J. , vol.237 , pp. 859-864
    • Furono, K.1    Goldberg, A.L.2
  • 25
    • 0023614188 scopus 로고
    • Dystrophin: The protein product of the Duchenne muscular dystrophy locus
    • Hoffman, E.P., Brown, R.J. and Kunkel, L.M. (1987) Dystrophin: the protein product of the Duchenne muscular dystrophy locus. Cell, 51: 919-928.
    • (1987) Cell , vol.51 , pp. 919-928
    • Hoffman, E.P.1    Brown, R.J.2    Kunkel, L.M.3
  • 26
    • 0019497980 scopus 로고
    • Design of the mammalian respiratory system. VI. Distribution of mitochondria and capillaries in various muscles
    • Hoppeler, H., Mathieu, O., Krover, R., Claassen, H., Armstrong, R.B. and Weibel, E.R. (1981) Design of the mammalian respiratory system. VI. Distribution of mitochondria and capillaries in various muscles. Resp. Physiol., 44: 87-111.
    • (1981) Resp. Physiol. , vol.44 , pp. 87-111
    • Hoppeler, H.1    Mathieu, O.2    Krover, R.3    Claassen, H.4    Armstrong, R.B.5    Weibel, E.R.6
  • 28
    • 0018758714 scopus 로고
    • Catalase, superoxide dismutase, glutathione reductase and thiobarbituric reactive products in normal and dystrophic human muscle
    • Kar, N.C. and Pearson, C.M. (1979) Catalase, superoxide dismutase, glutathione reductase and thiobarbituric reactive products in normal and dystrophic human muscle. Clin. Chim. Acta, 94: 277-280.
    • (1979) Clin. Chim. Acta , vol.94 , pp. 277-280
    • Kar, N.C.1    Pearson, C.M.2
  • 29
    • 0023697916 scopus 로고
    • Small caliber skeletal muscle fibers do not suffer necrosis in mdx mouse dystrophy
    • Karpati, G., Carpenter, S. and Prescott, S. (1988) Small caliber skeletal muscle fibers do not suffer necrosis in mdx mouse dystrophy. Muscle Nerve, 11: 795-803.
    • (1988) Muscle Nerve , vol.11 , pp. 795-803
    • Karpati, G.1    Carpenter, S.2    Prescott, S.3
  • 30
    • 0024429460 scopus 로고
    • Glutathione transferases: A possible role in the detoxication and repair of DNA and lipid hydroperoxides
    • Ketterer, B. and Meyer, D.J. (1989) Glutathione transferases: a possible role in the detoxication and repair of DNA and lipid hydroperoxides. Mut. Res., 214: 33-40.
    • (1989) Mut. Res. , vol.214 , pp. 33-40
    • Ketterer, B.1    Meyer, D.J.2
  • 31
    • 0029143830 scopus 로고
    • Absence of extraocular muscle pathology in Duchenne muscular dystrophy: Role for calcium homeostasis in extraocular muscle sparing
    • Khurana, T.S., Prendergast, R.A., Alameddine, H., Tome, M.S., Fardeau, M., Arahata, K., Sugita, H. and Kunkel, L.M. (1995) Absence of extraocular muscle pathology in Duchenne muscular dystrophy: role for calcium homeostasis in extraocular muscle sparing. J. Exp. Med., 182: 467-475.
    • (1995) J. Exp. Med. , vol.182 , pp. 467-475
    • Khurana, T.S.1    Prendergast, R.A.2    Alameddine, H.3    Tome, M.S.4    Fardeau, M.5    Arahata, K.6    Sugita, H.7    Kunkel, L.M.8
  • 32
    • 0023901508 scopus 로고
    • Superoxide mediates the toxicity of paraquat for cultured mammalian cells
    • Krall, J., Bagley, A.C., Mullenbach, G.T., Halliwell, R.A. and Lynch, R.E. (1988) Superoxide mediates the toxicity of paraquat for cultured mammalian cells. J. Biol. Chem., 263: 1910-1914.
    • (1988) J. Biol. Chem. , vol.263 , pp. 1910-1914
    • Krall, J.1    Bagley, A.C.2    Mullenbach, G.T.3    Halliwell, R.A.4    Lynch, R.E.5
  • 33
    • 0018248040 scopus 로고
    • Hepatic cytosolic non-selenium dependent glutathione peroxidase activity. Its nature and the effect of selenium deficiency
    • Lawrence, R.A., Parkhill, L.K. and Burk, R.F. (1978) Hepatic cytosolic non-selenium dependent glutathione peroxidase activity. Its nature and the effect of selenium deficiency. J. Nutr., 108: 981-987.
    • (1978) J. Nutr. , vol.108 , pp. 981-987
    • Lawrence, R.A.1    Parkhill, L.K.2    Burk, R.F.3
  • 34
    • 0029001953 scopus 로고
    • Phenotype of dystrophinopathy in old mdx mice
    • LeFaucheur, J.P., Pastoret, C. and Sebille, A. (1995) Phenotype of dystrophinopathy in old mdx mice. Anat. Rec., 242: 70-76.
    • (1995) Anat. Rec. , vol.242 , pp. 70-76
    • LeFaucheur, J.P.1    Pastoret, C.2    Sebille, A.3
  • 35
    • 0014422738 scopus 로고
    • An intracellular glutathione peroxidase with a lipid peroxide substrate
    • Little, C. and O'Brien, P.J. (1968) An intracellular glutathione peroxidase with a lipid peroxide substrate. Biochem. Biophys. Res. Commun., 31: 145-150.
    • (1968) Biochem. Biophys. Res. Commun. , vol.31 , pp. 145-150
    • Little, C.1    O'Brien, P.J.2
  • 36
    • 0025810590 scopus 로고
    • Effects of calcium on protein turnover of incubated muscles from mdx mice
    • MacLennan, P.A., McArdle, A. and Edwards, R.H.T. (1991) Effects of calcium on protein turnover of incubated muscles from mdx mice. Am. J. Physiol., 260: E594-E598.
    • (1991) Am. J. Physiol. , vol.260
    • MacLennan, P.A.1    McArdle, A.2    Edwards, R.H.T.3
  • 37
    • 0014691242 scopus 로고
    • Superoxide dismutase: An enzymatic function for erythrocuprein (hemocuprein)
    • McCord, J.M. and Fridovich, I. (1969) Superoxide dismutase: an enzymatic function for erythrocuprein (hemocuprein). J. Biol. Chem., 244: 6049-6055.
    • (1969) J. Biol. Chem. , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 38
    • 0021245923 scopus 로고
    • Lipid peroxidation and superoxide dismutase activity in muscle and erythrocytes in Duchenne muscular dystrophy
    • Mechler, F., Imre, S. and Dioszeghy, P. (1984) Lipid peroxidation and superoxide dismutase activity in muscle and erythrocytes in Duchenne muscular dystrophy. J. Neurol. Sci., 63: 279-283.
    • (1984) J. Neurol. Sci. , vol.63 , pp. 279-283
    • Mechler, F.1    Imre, S.2    Dioszeghy, P.3
  • 39
    • 0021811837 scopus 로고
    • Histochemical and physiological characteristics of the rat diaphragm
    • Metzger, J.M., Scheidt, K.B. and Fitts, R.H. (1985) Histochemical and physiological characteristics of the rat diaphragm. J. Appl. Physiol., 58: 1085-1091.
    • (1985) J. Appl. Physiol. , vol.58 , pp. 1085-1091
    • Metzger, J.M.1    Scheidt, K.B.2    Fitts, R.H.3
  • 40
    • 0028170326 scopus 로고
    • Importance of Se-glutathione peroxidase, catalase and Cu/ZnSOD for cell survival against oxidative stress
    • Michiels, C., Raes, M., Toussaint, O. and Remacle, J. (1994) Importance of Se-glutathione peroxidase, catalase and Cu/ZnSOD for cell survival against oxidative stress. Free Radic. Biol. Med., 17: 235-248.
    • (1994) Free Radic. Biol. Med. , vol.17 , pp. 235-248
    • Michiels, C.1    Raes, M.2    Toussaint, O.3    Remacle, J.4
  • 41
    • 0021849577 scopus 로고
    • Glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase and glyceraldehyde-3-phosphate dehydrogenase activities in early stages of development in dystrophic chickens
    • Mizuno, Y. (1985) Glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase and glyceraldehyde-3-phosphate dehydrogenase activities in early stages of development in dystrophic chickens. J. Neurol. Sci., 68: 47-60.
    • (1985) J. Neurol. Sci. , vol.68 , pp. 47-60
    • Mizuno, Y.1
  • 42
    • 0022480606 scopus 로고
    • Activities of antioxidant enzymes in muscle, liver and lung of chickens with inherited muscular dystrophy
    • Murphy, M.E. and Kehrer, J.P. (1986) Activities of antioxidant enzymes in muscle, liver and lung of chickens with inherited muscular dystrophy. Biochem. Biophys. Res. Commun., 134: 550-556.
    • (1986) Biochem. Biophys. Res. Commun. , vol.134 , pp. 550-556
    • Murphy, M.E.1    Kehrer, J.P.2
  • 43
    • 0021899162 scopus 로고
    • Direct toxic effects of paraquat and oxygen on cultured endothelial cells
    • Ody, C. and Junod, A.F. (1985) Direct toxic effects of paraquat and oxygen on cultured endothelial cells. Lab. Invest., 52: 77-84.
    • (1985) Lab. Invest. , vol.52 , pp. 77-84
    • Ody, C.1    Junod, A.F.2
  • 44
    • 0023873385 scopus 로고
    • Pathogenesis of progressive muscular dystrophy: Studies on free radical metabolism in an animal model
    • Ohta, K. and Mizuno, Y. (1988) Pathogenesis of progressive muscular dystrophy: studies on free radical metabolism in an animal model. Acta Neurol. Scand., 77: 108-114.
    • (1988) Acta Neurol. Scand. , vol.77 , pp. 108-114
    • Ohta, K.1    Mizuno, Y.2
  • 45
    • 0016243171 scopus 로고
    • Glutathione peroxidase, glutathione reductase and thiobarbituric reactive products in muscles of chickens and mice with genetic muscular dystrophy
    • Omaye, S.T. and Tappel, A.L. (1974) Glutathione peroxidase, glutathione reductase and thiobarbituric reactive products in muscles of chickens and mice with genetic muscular dystrophy. Life Sci., 15: 137-145.
    • (1974) Life Sci. , vol.15 , pp. 137-145
    • Omaye, S.T.1    Tappel, A.L.2
  • 46
    • 0014108436 scopus 로고
    • Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase
    • Paglia, D.E. and Valentine, W.N. (1967) Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase. J. Lab. Clin. Med., 70: 158-169.
    • (1967) J. Lab. Clin. Med. , vol.70 , pp. 158-169
    • Paglia, D.E.1    Valentine, W.N.2
  • 47
    • 0025993130 scopus 로고
    • Animal models of muscular dystrophy - What can they teach us?
    • Partridge, T. (1991) Animal models of muscular dystrophy - What can they teach us? Neuropath. Appl. Neurobiol., 17: 353-363.
    • (1991) Neuropath. Appl. Neurobiol. , vol.17 , pp. 353-363
    • Partridge, T.1
  • 48
    • 0028906307 scopus 로고
    • Mdx mice show progressive weakness and muscle deterioration with age
    • Pastoret, C. and Sebille, A. (1995) Mdx mice show progressive weakness and muscle deterioration with age. J. Neurol. Sci., 129: 97-105.
    • (1995) J. Neurol. Sci. , vol.129 , pp. 97-105
    • Pastoret, C.1    Sebille, A.2
  • 49
    • 0028999265 scopus 로고
    • Extraocular muscles: Basic and clinical aspects of structure and function
    • Porter, J.D., Baker, R.S., Ragusa, R.J. and Brueckner, J.K. (1995) Extraocular muscles: basic and clinical aspects of structure and function. Surv. Opthalmol., 39: 451-483.
    • (1995) Surv. Opthalmol. , vol.39 , pp. 451-483
    • Porter, J.D.1    Baker, R.S.2    Ragusa, R.J.3    Brueckner, J.K.4
  • 50
    • 0019322029 scopus 로고
    • The glutathione peroxidase activity of glutathione-S-transferases
    • Prohaska, J.R. (1980) The glutathione peroxidase activity of glutathione-S-transferases. Biochim. Biophys. Acta, 611: 87-98
    • (1980) Biochim. Biophys. Acta , vol.611 , pp. 87-98
    • Prohaska, J.R.1
  • 51
    • 0017380842 scopus 로고
    • Glutathione peroxidase activity of glutathione-S-transferases purified from rat liver
    • Prohaska, J.R. and Ganther, H.E. (1977) Glutathione peroxidase activity of glutathione-S-transferases purified from rat liver. Biochem. Biophys. Res. Commun., 76: 437-445.
    • (1977) Biochem. Biophys. Res. Commun. , vol.76 , pp. 437-445
    • Prohaska, J.R.1    Ganther, H.E.2
  • 52
    • 0021890995 scopus 로고
    • 2 + treatment mimics effect of vitamin E deficiency on sarcoplasmic calcium ATPase of rabbit muscle
    • 2 + treatment mimics effect of vitamin E deficiency on sarcoplasmic calcium ATPase of rabbit muscle. Biochem. Int., 10: 937-943.
    • (1985) Biochem. Int. , vol.10 , pp. 937-943
    • Promkhatkaew, D.1    Komaratat, P.2    Wilairat, P.3
  • 53
    • 0028081525 scopus 로고
    • Effects of efonidipine hydrochloride (NZ-105), a new calcium antagonist, against acute renal failure in rats
    • Shudo, C., Masuda, Y., Sugita, H., Tanaka, S. and Tomita, K. (1994) Effects of efonidipine hydrochloride (NZ-105), a new calcium antagonist, against acute renal failure in rats. Gen. Pharmacol., 25: 1451-1458.
    • (1994) Gen. Pharmacol. , vol.25 , pp. 1451-1458
    • Shudo, C.1    Masuda, Y.2    Sugita, H.3    Tanaka, S.4    Tomita, K.5
  • 54
    • 4244041828 scopus 로고
    • Oxidative potential in developing rat diaphragm, extensor digitorum longus and soleus muscle fibers
    • Smith, D., Green, H., Thomson, J. and Sharratt, M. (1988) Oxidative potential in developing rat diaphragm, extensor digitorum longus and soleus muscle fibers. Am. J. Physiol., 254: C661-C668.
    • (1988) Am. J. Physiol. , vol.254
    • Smith, D.1    Green, H.2    Thomson, J.3    Sharratt, M.4
  • 55
    • 0024402834 scopus 로고
    • An assay for superoxide dismutase activity in mammalian tissue homogenates
    • Spitz, D.R. and Oberley, L.W. (1989) An assay for superoxide dismutase activity in mammalian tissue homogenates. Anal. Biochem., 179: 8-18.
    • (1989) Anal. Biochem. , vol.179 , pp. 8-18
    • Spitz, D.R.1    Oberley, L.W.2
  • 57
    • 0021269048 scopus 로고
    • Inhibition of microsomal lipid peroxidation by glutathione and glutathione transferases B and AA
    • Tan, K.H., Meyer, D.J., Belin, J. and Ketterer, B. (1984) Inhibition of microsomal lipid peroxidation by glutathione and glutathione transferases B and AA. Biochem. J., 220: 243-252.
    • (1984) Biochem. J. , vol.220 , pp. 243-252
    • Tan, K.H.1    Meyer, D.J.2    Belin, J.3    Ketterer, B.4
  • 58
    • 0022638233 scopus 로고
    • Skeletal muscle pathology in X chromosome linked muscular dystrophy (mdx) mouse
    • Tanabe, Y., Esaki, K. and Nomura, T. (1986) Skeletal muscle pathology in X chromosome linked muscular dystrophy (mdx) mouse. Acta Neuropathol. (Berl.), 69: 91-95.
    • (1986) Acta Neuropathol. (Berl.) , vol.69 , pp. 91-95
    • Tanabe, Y.1    Esaki, K.2    Nomura, T.3
  • 59
    • 0011782459 scopus 로고
    • Lipid peroxidation and calcium pump function of the sarcoplasmic reticulum of skeletal muscles in hypercholesterolemia
    • Timofeev, A.A., Azizova, O.A. and Chernysheva, G.V. (1985) Lipid peroxidation and calcium pump function of the sarcoplasmic reticulum of skeletal muscles in hypercholesterolemia. Bull. Exp. Biol. Med., 99: 67-70.
    • (1985) Bull. Exp. Biol. Med. , vol.99 , pp. 67-70
    • Timofeev, A.A.1    Azizova, O.A.2    Chernysheva, G.V.3
  • 61
    • 0023739851 scopus 로고
    • Increased protein degradation results from elevated free calcium levels found in muscle from mdx mice
    • Turner, P.R., Westwood, T., Regan, C.M. and Steinhardt, R.A. (1988) Increased protein degradation results from elevated free calcium levels found in muscle from mdx mice. Nature (London), 335: 558-561.
    • (1988) Nature (London) , vol.335 , pp. 558-561
    • Turner, P.R.1    Westwood, T.2    Regan, C.M.3    Steinhardt, R.A.4
  • 62
    • 0015848173 scopus 로고
    • Superoxide dismutase: Organelle specificity
    • Weisiger, R.A. and Fridovich, I. (1973a) Superoxide dismutase: Organelle specificity. J. Biol. Chem., 248: 3582-3592.
    • (1973) J. Biol. Chem. , vol.248 , pp. 3582-3592
    • Weisiger, R.A.1    Fridovich, I.2
  • 63
    • 0015694842 scopus 로고
    • Mitochondrial superoxide dismutase: Site of synthesis and intramitochondrial localization
    • Weisiger, R.A. and Fridovich, I. (1973b) Mitochondrial superoxide dismutase: Site of synthesis and intramitochondrial localization. J. Biol. Chem., 248: 4793-4796.
    • (1973) J. Biol. Chem. , vol.248 , pp. 4793-4796
    • Weisiger, R.A.1    Fridovich, I.2
  • 64
    • 0025082933 scopus 로고
    • Resting calcium concentrations in isolated skeletal muscle fibers of dystrophic mice
    • Williams, D.A., Head, S.I., Bakker, A.J. and Stephenson, D.G. (1990) Resting calcium concentrations in isolated skeletal muscle fibers of dystrophic mice. J. Physiol., 428: 243-256.
    • (1990) J. Physiol. , vol.428 , pp. 243-256
    • Williams, D.A.1    Head, S.I.2    Bakker, A.J.3    Stephenson, D.G.4
  • 65
    • 0023472169 scopus 로고
    • Muscle fiber growth and necrosis in dystrophic muscles: A comparative study between dy and mdx mice
    • Woo, M., Tanabe, Y., Ishii, H., Nonaka, I., Yokoyama, M. and Esaki, K. (1987) Muscle fiber growth and necrosis in dystrophic muscles: a comparative study between dy and mdx mice. J. Neurol. Sci., 82: 111-122.
    • (1987) J. Neurol. Sci. , vol.82 , pp. 111-122
    • Woo, M.1    Tanabe, Y.2    Ishii, H.3    Nonaka, I.4    Yokoyama, M.5    Esaki, K.6


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