메뉴 건너뛰기




Volumn 10, Issue 2, 2000, Pages 144-149

Immunolabelling of mitochondrial superoxide dismutase and of Hsp60 in muscles harbouring a respiratory chain deficiency

Author keywords

Heat shock protein; Mitochondria; Ragged red fibre; Reactive oxygen species; Respiratory chain deficiency

Indexed keywords

HEAT SHOCK PROTEIN 60; REACTIVE OXYGEN METABOLITE; SUPEROXIDE DISMUTASE;

EID: 0033965891     PISSN: 09608966     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-8966(99)00070-X     Document Type: Article
Times cited : (9)

References (32)
  • 3
    • 0029656055 scopus 로고    scopus 로고
    • Molecular histology of mitochondrial and nuclear transcripts in the muscle of patients harbouring a single mitochondrial DNA deletion
    • Carrier H., Burt-Pichat B., Flocard F., et al. Molecular histology of mitochondrial and nuclear transcripts in the muscle of patients harbouring a single mitochondrial DNA deletion. Acta Neuropathol. 91:1996;104-111.
    • (1996) Acta Neuropathol , vol.91 , pp. 104-111
    • Carrier, H.1    Burt-Pichat, B.2    Flocard, F.3
  • 6
    • 0029071509 scopus 로고
    • Oxidants in mitochondria: From physiology to diseases
    • Richter C., Gogvadze V., Laffranchi R., et al. Oxidants in mitochondria: from physiology to diseases. Biochim Biophys Acta. 1271:1995;67-74.
    • (1995) Biochim Biophys Acta , vol.1271 , pp. 67-74
    • Richter, C.1    Gogvadze, V.2    Laffranchi, R.3
  • 7
    • 0015363173 scopus 로고
    • The cellular production of hydrogen peroxide
    • Boveris A., Oshino N., Chance B. The cellular production of hydrogen peroxide. Biochem J. 128:1972;617-630.
    • (1972) Biochem J , vol.128 , pp. 617-630
    • Boveris, A.1    Oshino, N.2    Chance, B.3
  • 8
    • 0032496159 scopus 로고    scopus 로고
    • Intracellular signalling by reactive oxygen species during hypoxia in cardiomyocytes
    • Duranteau J., Chandel N.S., Kulioz A., Shao Z., Schumaker P.T. Intracellular signalling by reactive oxygen species during hypoxia in cardiomyocytes. J Biol Chem. 273:1998;11619-11624.
    • (1998) J Biol Chem , vol.273 , pp. 11619-11624
    • Duranteau, J.1    Chandel, N.S.2    Kulioz, A.3    Shao, Z.4    Schumaker, P.T.5
  • 9
    • 0027730117 scopus 로고
    • Decreased expression of ubiquinol-cytochrome c reductase subunits in patients exhibiting mitochondrial myopathy with progressive exercise intolerance
    • Bouzidi M.F., Schägger H., Collombet J.M., et al. Decreased expression of ubiquinol-cytochrome c reductase subunits in patients exhibiting mitochondrial myopathy with progressive exercise intolerance. Neuromusc Disord. 3:1993;599-604.
    • (1993) Neuromusc Disord , vol.3 , pp. 599-604
    • Bouzidi, M.F.1    Schägger, H.2    Collombet, J.M.3
  • 10
    • 0342598201 scopus 로고    scopus 로고
    • Detection of mitochondrial DNA deletions by a screening procedure using the polymerase chain reaction
    • Ferlin T., Guironnet G., Barnoux M.C., Dumoulin R., Stepien G., Mousson B. Detection of mitochondrial DNA deletions by a screening procedure using the polymerase chain reaction. Mol Cell Biochem. 168:1997;73-85.
    • (1997) Mol Cell Biochem , vol.168 , pp. 73-85
    • Ferlin, T.1    Guironnet, G.2    Barnoux, M.C.3    Dumoulin, R.4    Stepien, G.5    Mousson, B.6
  • 11
    • 0001698695 scopus 로고
    • Rapid examination of muscle tissue: An improved trichrome method for rapid diagnosis of muscle biopsy fresh-frozen section
    • Engel W.K., Cunningham G.G. Rapid examination of muscle tissue: an improved trichrome method for rapid diagnosis of muscle biopsy fresh-frozen section. Neurology. 13:1963;919-923.
    • (1963) Neurology , vol.13 , pp. 919-923
    • Engel, W.K.1    Cunningham, G.G.2
  • 12
    • 72849184174 scopus 로고
    • Effect of coenzyme Q10 and menadione on succinic dehydrogenase activity as measured by tetrazolium salt reduction
    • Wattenberg L.W., Leong J.L. Effect of coenzyme Q10 and menadione on succinic dehydrogenase activity as measured by tetrazolium salt reduction. J Histochem Cytochem. 8:1960;296-300.
    • (1960) J Histochem Cytochem , vol.8 , pp. 296-300
    • Wattenberg, L.W.1    Leong, J.L.2
  • 13
    • 0014311556 scopus 로고
    • Non-droplet ultrastructural demonstration of cytochrome oxidase activity with a polymerizing osmiophilic reagent, diaminobenzidine (DAB)
    • Seligman A.M., Karnowsky M.J., Wasserkrug H., Hanker J.S. Non-droplet ultrastructural demonstration of cytochrome oxidase activity with a polymerizing osmiophilic reagent, diaminobenzidine (DAB). J Cell Biol. 38:1968;1-14.
    • (1968) J Cell Biol , vol.38 , pp. 1-14
    • Seligman, A.M.1    Karnowsky, M.J.2    Wasserkrug, H.3    Hanker, J.S.4
  • 14
    • 0031793192 scopus 로고    scopus 로고
    • Expression of heat shock proteins in mouse skin during wound healing
    • Laplante A.F., Moulin V., Auger F.A., et al. Expression of heat shock proteins in mouse skin during wound healing. J Histochem Cytochem. 46:1998;1291-1301.
    • (1998) J Histochem Cytochem , vol.46 , pp. 1291-1301
    • Laplante, A.F.1    Moulin, V.2    Auger, F.A.3
  • 15
    • 0023697402 scopus 로고
    • Dynamic changes in the structure and intracellular localisation of the mammalian low molecular weight heat shock proteins
    • Arrigo A.P., Suhan J.P., Welch W.J. Dynamic changes in the structure and intracellular localisation of the mammalian low molecular weight heat shock proteins. Mol Cell Biol. 8:1988;5059-5071.
    • (1988) Mol Cell Biol , vol.8 , pp. 5059-5071
    • Arrigo, A.P.1    Suhan, J.P.2    Welch, W.J.3
  • 16
    • 0002241311 scopus 로고
    • Expression and function of low molecular weight heat shock proteins
    • R. Morimoto, A. Tissières, & C. Georgopoulos. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Arrigo A.P., Landry J. Expression and function of low molecular weight heat shock proteins. Morimoto R., Tissières A., Georgopoulos C. The biology of heat shock proteins and molecular chaperones. 1994;335-373 Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones , pp. 335-373
    • Arrigo, A.P.1    Landry, J.2
  • 18
    • 0030200795 scopus 로고    scopus 로고
    • Oxidative damage to skeletal muscle DNA from patients with mitochondrial encephalomyopathies
    • Mitsui T., Kawai H., Nagasawa M., et al. Oxidative damage to skeletal muscle DNA from patients with mitochondrial encephalomyopathies. J Neurol Sci. 139:1996;111-116.
    • (1996) J Neurol Sci , vol.139 , pp. 111-116
    • Mitsui, T.1    Kawai, H.2    Nagasawa, M.3
  • 19
    • 0027298244 scopus 로고
    • Expression of human Mn SOD in Chinese hamster ovary cells confers protection from oxidant injury
    • Warner B., Papes R., Heile M., Spitz D., Wispe J. Expression of human Mn SOD in Chinese hamster ovary cells confers protection from oxidant injury. Am J Physiol. 264:1993;L598-L605.
    • (1993) Am J Physiol , vol.264
    • Warner, B.1    Papes, R.2    Heile, M.3    Spitz, D.4    Wispe, J.5
  • 20
    • 0031974368 scopus 로고    scopus 로고
    • Mitochondrial susceptibility to oxidative stress exacerbates cerebral infarction that follows permanent focal cerebral ischemia in mutant mice with manganese superoxide dismutase deficiency
    • Murakami K., Kondo T., Kawase M., et al. Mitochondrial susceptibility to oxidative stress exacerbates cerebral infarction that follows permanent focal cerebral ischemia in mutant mice with manganese superoxide dismutase deficiency. J Neurosci. 18:1998;205-213.
    • (1998) J Neurosci , vol.18 , pp. 205-213
    • Murakami, K.1    Kondo, T.2    Kawase, M.3
  • 21
    • 0028296508 scopus 로고
    • Age-dependent increase of mitochondrial DNA deletions together with lipid peroxides and superoxide dismutase in human liver mitochondria
    • Yen T.C., King K.L., Lee H.C., Yeh S.H., Wei Y.H. Age-dependent increase of mitochondrial DNA deletions together with lipid peroxides and superoxide dismutase in human liver mitochondria. Free Radic Biol Med. 16:1994;207-214.
    • (1994) Free Radic Biol Med , vol.16 , pp. 207-214
    • Yen, T.C.1    King, K.L.2    Lee, H.C.3    Yeh, S.H.4    Wei, Y.H.5
  • 22
    • 0026446343 scopus 로고
    • Prevention of protein denaturation under heat stress by the chaperonin Hsp60
    • Martin J., Horwich A.L., Hartl F.U. Prevention of protein denaturation under heat stress by the chaperonin Hsp60. Science. 258:1992;995-998.
    • (1992) Science , vol.258 , pp. 995-998
    • Martin, J.1    Horwich, A.L.2    Hartl, F.U.3
  • 23
    • 0023882106 scopus 로고
    • Two types of mitochondrial crystals in diseased human skeletal muscle fibers
    • Farrants G.W., Hovmöller S., Stadhouders A.M. Two types of mitochondrial crystals in diseased human skeletal muscle fibers. Muscle Nerve. 11:1988;45-55.
    • (1988) Muscle Nerve , vol.11 , pp. 45-55
    • Farrants, G.W.1    Hovmöller, S.2    Stadhouders, A.M.3
  • 24
    • 0027322582 scopus 로고
    • Immunolocalization of heat shock proteins in ragged-red fibers of patients with mitochondrial encephalomyopathies
    • Sparaco M., Rosaklija G., Tanji K., et al. Immunolocalization of heat shock proteins in ragged-red fibers of patients with mitochondrial encephalomyopathies. Neuromusc Disord. 3:1993;71-76.
    • (1993) Neuromusc Disord , vol.3 , pp. 71-76
    • Sparaco, M.1    Rosaklija, G.2    Tanji, K.3
  • 25
    • 0027246118 scopus 로고
    • A fatal, systemic mitochondrial disease with decreased mitochondrial enzyme activities, abnormal ultrastructure of the mitochondria and deficiency of heat shock protein 60
    • Agsteribbe E., Huckriede A., Veenhuis M., et al. A fatal, systemic mitochondrial disease with decreased mitochondrial enzyme activities, abnormal ultrastructure of the mitochondria and deficiency of heat shock protein 60. Biochem Biophys Res Commun. 193:1993;146-154.
    • (1993) Biochem Biophys Res Commun , vol.193 , pp. 146-154
    • Agsteribbe, E.1    Huckriede, A.2    Veenhuis, M.3
  • 26
    • 0028131509 scopus 로고
    • Decreased synthesis and inefficient mitochondrial import of hsp60 in a patient with a mitochondrial encephalomyopathy
    • Huckriede A., Agsteribbe E. Decreased synthesis and inefficient mitochondrial import of hsp60 in a patient with a mitochondrial encephalomyopathy. Biochim Biophys Acta. 1227:1994;200-206.
    • (1994) Biochim Biophys Acta , vol.1227 , pp. 200-206
    • Huckriede, A.1    Agsteribbe, E.2
  • 28
    • 0029937415 scopus 로고    scopus 로고
    • Immunostaining of mitochondrial heat shock proteins (mtHSPs) in skeletal muscle fibers of mitochondrial cytopathy
    • Ibi T., Sahashi K., Ling J., Marui K., Mitsuma T. Immunostaining of mitochondrial heat shock proteins (mtHSPs) in skeletal muscle fibers of mitochondrial cytopathy. Rinsho Shinkeigaku. 36:1996;61-64.
    • (1996) Rinsho Shinkeigaku , vol.36 , pp. 61-64
    • Ibi, T.1    Sahashi, K.2    Ling, J.3    Marui, K.4    Mitsuma, T.5
  • 29
    • 0343144858 scopus 로고    scopus 로고
    • Simultaneous overexpression of two stress proteins in rat cardiomyocytes and myogenic cells confers protection against ischemic-induced injury
    • Lau S., Patnaik N., Sayen M.R., Mestril R. Simultaneous overexpression of two stress proteins in rat cardiomyocytes and myogenic cells confers protection against ischemic-induced injury. Circulation. 96:1997;2287-2294.
    • (1997) Circulation , vol.96 , pp. 2287-2294
    • Lau, S.1    Patnaik, N.2    Sayen, M.R.3    Mestril, R.4
  • 30
    • 0029825891 scopus 로고    scopus 로고
    • Selective induction of mitochondrial chaperones in response to loss of the mitochondrial genome
    • Martinus R.D., Garth G.P., Webster T.L., et al. Selective induction of mitochondrial chaperones in response to loss of the mitochondrial genome. Eur J Biochem. 240:1996;98-103.
    • (1996) Eur J Biochem , vol.240 , pp. 98-103
    • Martinus, R.D.1    Garth, G.P.2    Webster, T.L.3
  • 31
    • 0029157324 scopus 로고
    • Expression of stress proteins and mitochondrial chaperonins in chronically stimulated skeletal muscle
    • Ornatsky O.I., Connor M.K., Hood D.A. Expression of stress proteins and mitochondrial chaperonins in chronically stimulated skeletal muscle. Biochem J. 311:1995;119-123.
    • (1995) Biochem J , vol.311 , pp. 119-123
    • Ornatsky, O.I.1    Connor, M.K.2    Hood, D.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.