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Volumn 72, Issue 2, 1999, Pages 693-699

Up-regulation of protein chaperones preserves viability of cells expressing toxic Cu/Zn-superoxide dismutase mutants associated with amyotrophic lateral sclerosis

Author keywords

Chaperones; Cu Zn superoxide dismutase; Familial amyotrophic lateral sclerosis; Heat shock proteins; Motor neurons; Neuroprotection; Preferential vulnerability; SOD 1; Stress proteins; Stress response

Indexed keywords

CATALASE; CHAPERONE; COPPER ZINC SUPEROXIDE DISMUTASE; HEAT SHOCK PROTEIN; MUTANT PROTEIN;

EID: 0344507132     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1999.0720693.x     Document Type: Article
Times cited : (226)

References (43)
  • 1
    • 0030888919 scopus 로고    scopus 로고
    • Upregulation of protein-tyrosine nitration in the anterior horn cells of amyotrophic lateral sclerosis
    • Abe K., Pan L. H., Watanabe M., Konno H., Kato T., and Itoyama Y. (1997) Upregulation of protein-tyrosine nitration in the anterior horn cells of amyotrophic lateral sclerosis. Neurol. Res. 19, 124-128.
    • (1997) Neurol. Res. , vol.19 , pp. 124-128
    • Abe, K.1    Pan, L.H.2    Watanabe, M.3    Konno, H.4    Kato, T.5    Itoyama, Y.6
  • 4
    • 0027359334 scopus 로고
    • Superoxide dismutase activity, oxidative damage, and mitochondrial energy metabolism in familial and sporadic amyotrophic lateral sclerosis
    • Bowling A. C., Schulz J. B., Brown R. H. Jr., and Beal M. F. (1993) Superoxide dismutase activity, oxidative damage, and mitochondrial energy metabolism in familial and sporadic amyotrophic lateral sclerosis. J. Neurochem. 61, 2322-2325.
    • (1993) J. Neurochem. , vol.61 , pp. 2322-2325
    • Bowling, A.C.1    Schulz, J.B.2    Brown R.H., Jr.3    Beal, M.F.4
  • 5
    • 0030806228 scopus 로고    scopus 로고
    • Elevated free nitrotyrosine levels, but not protein-bound nitrotyrosine or hydroxyl radicals, throughout amyotrophic lateral sclerosis (ALS)-like disease implicate tyrosine nitration as an aberrant in vivo property of one familial ALS-linked superoxide dismutase 1 mutant
    • Bruijn L. I., Beal M. F., Becher M. W., Schulz J. B., Wong P. C., Price D. L., and Cleveland D. W. (1997a) Elevated free nitrotyrosine levels, but not protein-bound nitrotyrosine or hydroxyl radicals, throughout amyotrophic lateral sclerosis (ALS)-like disease implicate tyrosine nitration as an aberrant in vivo property of one familial ALS-linked superoxide dismutase 1 mutant. Proc. Natl. Acad. Sci. USA 94, 7606-7611.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 7606-7611
    • Bruijn, L.I.1    Beal, M.F.2    Becher, M.W.3    Schulz, J.B.4    Wong, P.C.5    Price, D.L.6    Cleveland, D.W.7
  • 7
    • 0030027968 scopus 로고    scopus 로고
    • Supervising the fold: Functional principles of molecular chaperones
    • Buchner J. (1996) Supervising the fold: functional principles of molecular chaperones. FASEB J. 10, 10-19.
    • (1996) FASEB J. , vol.10 , pp. 10-19
    • Buchner, J.1
  • 8
    • 0028172052 scopus 로고
    • Impaired copper binding by the H46R mutant of human Cu,Zn superoxide dismutase, involved in amyotrophic lateral sclerosis
    • Carri M. T., Battistoni A., Polizio F., Desideri A., and Rotilio G. (1994) Impaired copper binding by the H46R mutant of human Cu,Zn superoxide dismutase, involved in amyotrophic lateral sclerosis. FEBS Lett. 356, 314-316.
    • (1994) FEBS Lett. , vol.356 , pp. 314-316
    • Carri, M.T.1    Battistoni, A.2    Polizio, F.3    Desideri, A.4    Rotilio, G.5
  • 9
    • 0030833449 scopus 로고    scopus 로고
    • Decreased zinc affinity of amyotrophic lateral sclerosis-associated superoxide dismutase mutants leads to enhanced catalysis of tyrosine nitration by peroxynitrite
    • Crow J. P., Sampson J. B., Zhuang Y. X., Thompson J. A., and Beckman J. S. (1997) Decreased zinc affinity of amyotrophic lateral sclerosis-associated superoxide dismutase mutants leads to enhanced catalysis of tyrosine nitration by peroxynitrite. J. Neurochem. 69, 1936-1944.
    • (1997) J. Neurochem. , vol.69 , pp. 1936-1944
    • Crow, J.P.1    Sampson, J.B.2    Zhuang, Y.X.3    Thompson, J.A.4    Beckman, J.S.5
  • 10
    • 0028933344 scopus 로고
    • Neuropathological changes in two lines of mice carrying a transgene for mutant human Cu,Zn SOD, and in mice overexpressing wild type human SOD: A model of familial amyotrophic lateral sclerosis (FALS)
    • Dal Canto M. C. and Gurney M. E. (1995) Neuropathological changes in two lines of mice carrying a transgene for mutant human Cu,Zn SOD, and in mice overexpressing wild type human SOD: a model of familial amyotrophic lateral sclerosis (FALS). Brain Res. 676, 25-40.
    • (1995) Brain Res. , vol.676 , pp. 25-40
    • Dal Canto, M.C.1    Gurney, M.E.2
  • 11
    • 0030014299 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis: Recent advances in understanding disease mechanisms
    • de Belleroche J., Orrell R. W., and Virgo L. (1996) Amyotrophic lateral sclerosis: recent advances in understanding disease mechanisms. J. Neuropathol. Exp. Neurol. 55, 747-757.
    • (1996) J. Neuropathol. Exp. Neurol. , vol.55 , pp. 747-757
    • De Belleroche, J.1    Orrell, R.W.2    Virgo, L.3
  • 13
    • 0030022780 scopus 로고    scopus 로고
    • Activation of protein kinase C induces neurofilament fragmentation, hyperphosphorylation of perikaryal neurofilaments and proximal dendritic swellings in cultured motor neurons
    • Doroudchi M. M. and Durham H. D. (1996) Activation of protein kinase C induces neurofilament fragmentation, hyperphosphorylation of perikaryal neurofilaments and proximal dendritic swellings in cultured motor neurons. J. Neuropathol. Exp. Neurol. 55, 246-256.
    • (1996) J. Neuropathol. Exp. Neurol. , vol.55 , pp. 246-256
    • Doroudchi, M.M.1    Durham, H.D.2
  • 14
    • 0030777650 scopus 로고    scopus 로고
    • Aggregation of mutant Cu/Zn superoxide dismutase proteins in a culture model of ALS
    • Durham H. D., Roy J., Dong L., and Figlewicz D. A. (1997) Aggregation of mutant Cu/Zn superoxide dismutase proteins in a culture model of ALS. J. Neuropathol. Exp. Neurol. 56, 523-530.
    • (1997) J. Neuropathol. Exp. Neurol. , vol.56 , pp. 523-530
    • Durham, H.D.1    Roy, J.2    Dong, L.3    Figlewicz, D.A.4
  • 16
    • 0030831352 scopus 로고    scopus 로고
    • Mutant superoxide dismutase-1-linked familial amyotrophic lateral sclerosis - Molecular mechanisms of neuronal death and protection
    • Ghadge G. D., Lee J. P., Bindokas V. P., Jordan J., Ma L., Miller R. J., and Roos R. P. (1997) Mutant superoxide dismutase-1-linked familial amyotrophic lateral sclerosis - molecular mechanisms of neuronal death and protection. J. Neurosci. 17, 8756-8766.
    • (1997) J. Neurosci. , vol.17 , pp. 8756-8766
    • Ghadge, G.D.1    Lee, J.P.2    Bindokas, V.P.3    Jordan, J.4    Ma, L.5    Miller, R.J.6    Roos, R.P.7
  • 18
    • 0030050727 scopus 로고    scopus 로고
    • Benefit of vitamin E. Riluzole, and gabapentin in a transgenic model of familial amyotrophic lateral sclerosis
    • Gurney M. E., Cutting F. B., Zhai P., Doble A., Taylor C. P., Andrus P. K., and Hall E. D. (1996) Benefit of vitamin E. riluzole, and gabapentin in a transgenic model of familial amyotrophic lateral sclerosis. Ann. Neurol. 39, 147-157.
    • (1996) Ann. Neurol. , vol.39 , pp. 147-157
    • Gurney, M.E.1    Cutting, F.B.2    Zhai, P.3    Doble, A.4    Taylor, C.P.5    Andrus, P.K.6    Hall, E.D.7
  • 19
    • 0031911637 scopus 로고    scopus 로고
    • Subunit asymmetry in the three-dimensional structure of a human CuZnSOD mutant found in familial amyotrophic lateral sclerosis
    • Hart P. J., Liu H. B., Pellegrini M., Nersissian A. M., Gralla E. B., Valentine J. S., and Eisenberg D. (1998) Subunit asymmetry in the three-dimensional structure of a human CuZnSOD mutant found in familial amyotrophic lateral sclerosis. Protein Sci. 7, 545-555.
    • (1998) Protein Sci. , vol.7 , pp. 545-555
    • Hart, P.J.1    Liu, H.B.2    Pellegrini, M.3    Nersissian, A.M.4    Gralla, E.B.5    Valentine, J.S.6    Eisenberg, D.7
  • 20
    • 0030200643 scopus 로고    scopus 로고
    • Proteasome inhibition enhances the stability of mouse Cu/Zn superoxide dismutase with mutations linked to familial amyotrophic lateral sclerosis
    • Hoffman E. K., Wilcox H. M., Scott R. W., and Siman R. (1996) Proteasome inhibition enhances the stability of mouse Cu/Zn superoxide dismutase with mutations linked to familial amyotrophic lateral sclerosis. J. Neurol. Sci. 139, 15-20.
    • (1996) J. Neurol. Sci. , vol.139 , pp. 15-20
    • Hoffman, E.K.1    Wilcox, H.M.2    Scott, R.W.3    Siman, R.4
  • 21
    • 0030758693 scopus 로고    scopus 로고
    • Molecular chaperones protect catalase against thermal stress
    • Hook D. W. A. and Harding J. (1997) Molecular chaperones protect catalase against thermal stress. Eur. J. Biochem. 247, 380-385.
    • (1997) Eur. J. Biochem. , vol.247 , pp. 380-385
    • Hook, D.W.A.1    Harding, J.2
  • 23
    • 0026740369 scopus 로고
    • Expression of heat shock genes (hsp70) in the rabbit spinal cord: Localization of constitutive and hyperthermia-inducible mRNA species
    • Manzerra P. and Brown I. R. (1992) Expression of heat shock genes (hsp70) in the rabbit spinal cord: localization of constitutive and hyperthermia-inducible mRNA species. J. Neurosci. Res. 31, 606-615.
    • (1992) J. Neurosci. Res. , vol.31 , pp. 606-615
    • Manzerra, P.1    Brown, I.R.2
  • 24
    • 0030749689 scopus 로고    scopus 로고
    • Normal binding and reactivity of copper in mutant superoxide dismutase isolated from amyotrophic lateral sclerosis patients
    • Marklund S. L., Andersen P. M., Forsgren L., Nilsson P., Ohlsson P.-I., Wikander G., and Öberg A. (1997) Normal binding and reactivity of copper in mutant superoxide dismutase isolated from amyotrophic lateral sclerosis patients. J. Neurochem. 69, 675-681.
    • (1997) J. Neurochem. , vol.69 , pp. 675-681
    • Marklund, S.L.1    Andersen, P.M.2    Forsgren, L.3    Nilsson, P.4    Ohlsson, P.-I.5    Wikander, G.6    Öberg, A.7
  • 26
    • 0030596537 scopus 로고    scopus 로고
    • Instability of mutant Cu/Zn superoxide dismutase (Ala4Thr) associated with familial amyotrophic lateral sclerosis
    • Nakano R., Inuzuka T., Kikugawa K., Takahashi H., Sakimura K., Fujii J., Taniguchi N., and Tsuji S. (1996) Instability of mutant Cu/Zn superoxide dismutase (Ala4Thr) associated with familial amyotrophic lateral sclerosis. Neurosci. Lett. 211, 129-131.
    • (1996) Neurosci. Lett. , vol.211 , pp. 129-131
    • Nakano, R.1    Inuzuka, T.2    Kikugawa, K.3    Takahashi, H.4    Sakimura, K.5    Fujii, J.6    Taniguchi, N.7    Tsuji, S.8
  • 27
    • 0031577722 scopus 로고    scopus 로고
    • Stability of mutant superoxide dismutase-1 associated with familial amyotrophic lateral sclerosis determines the manner of copper release and induction of thioredoxin in erythrocytes
    • Ogawa Y., Kosaka H., Nakanishi T., Shimizu A., Ohoi N., Shouji H., Yanagihara T., and Sakoda S. (1997) Stability of mutant superoxide dismutase-1 associated with familial amyotrophic lateral sclerosis determines the manner of copper release and induction of thioredoxin in erythrocytes. Biochem. Biophys. Res. Commun. 241, 251-257.
    • (1997) Biochem. Biophys. Res. Commun. , vol.241 , pp. 251-257
    • Ogawa, Y.1    Kosaka, H.2    Nakanishi, T.3    Shimizu, A.4    Ohoi, N.5    Shouji, H.6    Yanagihara, T.7    Sakoda, S.8
  • 28
    • 0030945491 scopus 로고    scopus 로고
    • Clinical and functional investigation of 10 missense mutations and a novel frameshift insertion mutation of the gene for copper-zinc superoxide dismutase in UK families with amyotrophic lateral sclerosis
    • Orrell R. W., Habgood J. J., Gardiner I., King A. W., Bowe F. A., Hallewell R. A., Markiund S. L., Greenwood J., Lane R. J. M., and de Belleroche J. (1997) Clinical and functional investigation of 10 missense mutations and a novel frameshift insertion mutation of the gene for copper-zinc superoxide dismutase in UK families with amyotrophic lateral sclerosis. Neurology 48, 746-751.
    • (1997) Neurology , vol.48 , pp. 746-751
    • Orrell, R.W.1    Habgood, J.J.2    Gardiner, I.3    King, A.W.4    Bowe, F.A.5    Hallewell, R.A.6    Markiund, S.L.7    Greenwood, J.8    Lane, R.J.M.9    De Belleroche, J.10
  • 29
    • 0000675009 scopus 로고
    • Heat shock proteins and stress tolerance
    • (Morimoto R. I., Tissières A., and Georgopoulos C., eds), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
    • Parsell D. A. and Lindquist S. (1994) Heat shock proteins and stress tolerance, in The Biology of Heat Shock Proteins and Molecular Chaperones (Morimoto R. I., Tissières A., and Georgopoulos C., eds), pp. 457-494. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones , pp. 457-494
    • Parsell, D.A.1    Lindquist, S.2
  • 34
    • 0032402093 scopus 로고    scopus 로고
    • Glutamate potentiates the toxicity of mutant Cu/Zn-superoxide dismutase in motor neurons by postsynaptic calcium-dependent mechanisms
    • in press
    • Roy J., Minotti S., Dong L., Figlewicz D. A., and Durham H. D. (1998) Glutamate potentiates the toxicity of mutant Cu/Zn-superoxide dismutase in motor neurons by postsynaptic calcium-dependent mechanisms. J. Neurosci. (in press).
    • (1998) J. Neurosci.
    • Roy, J.1    Minotti, S.2    Dong, L.3    Figlewicz, D.A.4    Durham, H.D.5
  • 35
    • 0029129276 scopus 로고
    • Differential expression of heat shock protein HSP27 in human neurons and glial cells in culture
    • Satoh J. I. and Kim S. U. (1995) Differential expression of heat shock protein HSP27 in human neurons and glial cells in culture. J. Neurosci. Res. 41, 805-818.
    • (1995) J. Neurosci. Res. , vol.41 , pp. 805-818
    • Satoh, J.I.1    Kim, S.U.2
  • 37
    • 0029082389 scopus 로고
    • Oxidative damage to protein in sporadic motor neuron disease spinal cord
    • Shaw P. J., Ince P. G., Falkous G., and Mantle D. (1995) Oxidative damage to protein in sporadic motor neuron disease spinal cord. Ann. Neurol. 38, 691-695.
    • (1995) Ann. Neurol. , vol.38 , pp. 691-695
    • Shaw, P.J.1    Ince, P.G.2    Falkous, G.3    Mantle, D.4
  • 38
    • 0029684296 scopus 로고    scopus 로고
    • Involvement of molecular chaperones in intracellular protein breakdown
    • Sherman M. Y. and Goldberg A. L. (1996) Involvement of molecular chaperones in intracellular protein breakdown. EXS 77, 57-78.
    • (1996) EXS , vol.77 , pp. 57-78
    • Sherman, M.Y.1    Goldberg, A.L.2
  • 39
    • 0029927679 scopus 로고    scopus 로고
    • Intense superoxide dismutase-1 immunoreactivity in intracytoplasmic hyaline inclusions of familial amyotrophic lateral sclerosis with posterior column involvement
    • Shibata N., Hirano A., Kobayashi M., Siddique T., Deng H. X., Hung W. Y., Kato T., and Asayama K. (1996) Intense superoxide dismutase-1 immunoreactivity in intracytoplasmic hyaline inclusions of familial amyotrophic lateral sclerosis with posterior column involvement. J. Neuropathol. Exp. Neurol. 55, 481-490.
    • (1996) J. Neuropathol. Exp. Neurol. , vol.55 , pp. 481-490
    • Shibata, N.1    Hirano, A.2    Kobayashi, M.3    Siddique, T.4    Deng, H.X.5    Hung, W.Y.6    Kato, T.7    Asayama, K.8
  • 40
    • 0032499788 scopus 로고    scopus 로고
    • Reexamination of the mechanism of hydroxyl radical adducts formed from the reaction between familial amyotrophic lateral sclerosis-associated Cu,Zn superoxide dismutase mutants
    • Singh R. J., Karoui H., Gunther M. R., Beckman J. S., Mason R. P., and Kalyanaraman B. (1998) Reexamination of the mechanism of hydroxyl radical adducts formed from the reaction between familial amyotrophic lateral sclerosis-associated Cu,Zn superoxide dismutase mutants. Proc. Natl. Acad. Sci. USA 95, 6675-6680.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6675-6680
    • Singh, R.J.1    Karoui, H.2    Gunther, M.R.3    Beckman, J.S.4    Mason, R.P.5    Kalyanaraman, B.6
  • 42
    • 0029053881 scopus 로고
    • An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria
    • Wong P. C., Pardo C. A., Borchelt D. R., Lee M. K., Copeland N. G., Jenkins N. A., Sisodia S. S., Cleveland D. W., and Price D. L. (1995) An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria. Neuron 14, 1105-1116.
    • (1995) Neuron , vol.14 , pp. 1105-1116
    • Wong, P.C.1    Pardo, C.A.2    Borchelt, D.R.3    Lee, M.K.4    Copeland, N.G.5    Jenkins, N.A.6    Sisodia, S.S.7    Cleveland, D.W.8    Price, D.L.9
  • 43
    • 0029939471 scopus 로고    scopus 로고
    • A gain-of-function of an amyotrophic lateral sclerosis-associated Cu,Zn-superoxide dismutase mutant: An enhancement of free radical formation due to a decrease in Km for hydrogen peroxide
    • Yim M. B., Kang J.-H., Yim H.-S., Kwak H.-S., Chock P. B., and Stadtman E. R. (1996) A gain-of-function of an amyotrophic lateral sclerosis-associated Cu,Zn-superoxide dismutase mutant: an enhancement of free radical formation due to a decrease in Km for hydrogen peroxide. Proc. Natl. Acad. Sci. USA 93, 5709-5714.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5709-5714
    • Yim, M.B.1    Kang, J.-H.2    Yim, H.-S.3    Kwak, H.-S.4    Chock, P.B.5    Stadtman, E.R.6


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