메뉴 건너뛰기




Volumn 26, Issue 3, 2000, Pages 215-226

Amyotrophic lateral sclerosis: Transgenic model and novel neuroprotective agent

Author keywords

Amyotrophic Lateral Sclerosis; Animal models; Creatine; Kinase

Indexed keywords

ADENOSINE TRIPHOSPHATE; COPPER ZINC SUPEROXIDE DISMUTASE; CREATINE;

EID: 0033919047     PISSN: 08936609     EISSN: None     Source Type: Journal    
DOI: 10.1002/1520-6769(200005/06)26:3<215::AID-NRC9>3.0.CO;2-Z     Document Type: Review
Times cited : (5)

References (39)
  • 1
    • 0028960506 scopus 로고
    • Amyotrophic lateral sclerosis: Recent insights from genetics and transgenic mice
    • Brown RH Jr. Amyotrophic lateral sclerosis: Recent insights from genetics and transgenic mice. Cell 1995;80:687-692.
    • (1995) Cell , vol.80 , pp. 687-692
    • Brown Jr., R.H.1
  • 2
    • 0020391968 scopus 로고
    • Clinical limits of Amyotrophic lateral sclerosis
    • Rowland LP editor. New York: Raven Press
    • Mulder DW. Clinical limits of Amyotrophic lateral sclerosis. In: Rowland LP editor. Human motor neuron diseases. New York: Raven Press;1982. p 15-22.
    • (1982) Human Motor Neuron Diseases , pp. 15-22
    • Mulder, D.W.1
  • 3
    • 0020392683 scopus 로고
    • Familial motor neuron disease
    • Rowland LP, editor. New York: Raven Press
    • Emery AEH and Holloway S. Familial motor neuron disease. In Rowland LP, editor. Human motor neuron diseases. New York: Raven Press;1982. p 139-147.
    • (1982) Human Motor Neuron Diseases , pp. 139-147
    • Emery, A.E.H.1    Holloway, S.2
  • 4
    • 0026002405 scopus 로고
    • Molecular genetics in amyotrophic lateral sclerosis
    • Rowland LP, editor. Amyotrophic lateral sclerosis and other motor neuron disease
    • Siddique T. Molecular genetics in amyotrophic lateral sclerosis. In Rowland LP, editor. Amyotrophic lateral sclerosis and other motor neuron disease. Adv Neurol 1991;56:227-231.
    • (1991) Adv Neurol , vol.56 , pp. 227-231
    • Siddique, T.1
  • 5
    • 0026042995 scopus 로고
    • Cytopathology of amyotrophic lateral sclerosis
    • Hirano A. Cytopathology of amyotrophic lateral sclerosis. Adv Neurol 1991;56:91-101.
    • (1991) Adv Neurol , vol.56 , pp. 91-101
    • Hirano, A.1
  • 6
    • 0027401203 scopus 로고
    • Mutations in Cu, Zn superoxide dismutase gene are associated with familial amytrophic lateral sclerosis
    • Rosen DR, Siddique T, Patterson D, et al, Mutations in Cu, Zn superoxide dismutase gene are associated with familial amytrophic lateral sclerosis. Nature 1993;362:59-62.
    • (1993) Nature , vol.362 , pp. 59-62
    • Rosen, D.R.1    Siddique, T.2    Patterson, D.3
  • 7
    • 0027426169 scopus 로고
    • Amyotrophic lateral sclerosis and strcutural defects in Cu, Zn superoxide dismutase
    • Deng HX, Hentati A, Tainer JA, et al. Amyotrophic lateral sclerosis and strcutural defects in Cu, Zn superoxide dismutase. Science 1993;261:1047-1051.
    • (1993) Science , vol.261 , pp. 1047-1051
    • Deng, H.X.1    Hentati, A.2    Tainer, J.A.3
  • 8
    • 0027359334 scopus 로고
    • Superoxide dismutase activity, oxidative damage, and mitochondrial energy metabolism in familial and sporadic amyotrophic lateral sclerosis
    • Bowling AC, Schulz JB, Brown RH Jr, Beal MF. Superoxide dismutase activity, oxidative damage, and mitochondrial energy metabolism in familial and sporadic amyotrophic lateral sclerosis. J Neurochem 1993;61:2322-2325.
    • (1993) J Neurochem , vol.61 , pp. 2322-2325
    • Bowling, A.C.1    Schulz, J.B.2    Brown Jr., R.H.3    Beal, M.F.4
  • 9
    • 15844393658 scopus 로고    scopus 로고
    • Motor neurons in Cu/Zn superoxide dismutase-deficient mice develop normally but exhibit enhanced cell death after axonal injury
    • Reaume AG, Sosa PA de, Kulkarni S. et al. Motor neurons in Cu/Zn superoxide dismutase-deficient mice develop normally but exhibit enhanced cell death after axonal injury. Nature Gent 1996;13:43-47.
    • (1996) Nature Gent , vol.13 , pp. 43-47
    • Reaume, A.G.1    De Sosa, P.A.2    Kulkarni, S.3
  • 10
    • 0029010496 scopus 로고
    • Amyotrophic lateral sclerosis associated with homozygosity for an Asp90Ala mutation in CuZn-superoxide dismutase
    • Andersen PM, Nilsson P, Ala-Hurula, et.al. Amyotrophic lateral sclerosis associated with homozygosity for an Asp90Ala mutation in CuZn-superoxide dismutase. Nat Genet 1995;10:61-66.
    • (1995) Nat Genet , vol.10 , pp. 61-66
    • Andersen, P.M.1    Nilsson, P.2    Ala-Hurula3
  • 11
    • 0027401203 scopus 로고
    • Mutations in Cu, Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis
    • Rosen et al. Mutations in Cu, Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature 1993;362: 59-62.
    • (1993) Nature , vol.362 , pp. 59-62
    • Rosen1
  • 13
    • 0028888945 scopus 로고
    • Transgenic mice expressing an altered murine superoxide dismutase gene provide an animal model of amyotrophic lateral sclerosis
    • Ripps ME, Huntley GW, Hof PR, Morrison JH, Gordon JW. Transgenic mice expressing an altered murine superoxide dismutase gene provide an animal model of amyotrophic lateral sclerosis. Proc Natl Acad Sci U.S.A. 1995;92:689-693.
    • (1995) Proc Natl Acad Sci U.S.A. , vol.92 , pp. 689-693
    • Ripps, M.E.1    Huntley, G.W.2    Hof, P.R.3    Morrison, J.H.4    Gordon, J.W.5
  • 14
    • 0029053881 scopus 로고
    • An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria
    • Wong PC, Pardo CA, Borchelt DR, Lee MK, Copeland NG, Jenkins NA, Sisodia SS, Cleveland DW, Price DL. An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria. Neuron 1995;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
  • 15
    • 0028284779 scopus 로고
    • Motor neuron degeneration in mice expressing a human Cu, Zn superoxide dismutase mutation
    • Gurey ME, Pu H, Chiu AY, et al. Motor neuron degeneration in mice expressing a human Cu, Zn superoxide dismutase mutation. Science 1994;264:1772-1775.
    • (1994) Science , vol.264 , pp. 1772-1775
    • Gurey, M.E.1    Pu, H.2    Chiu, A.Y.3
  • 16
    • 0030927253 scopus 로고    scopus 로고
    • Transgenic animal models of familial amyotrophic lateral sclerosis
    • Gurney ME. Transgenic animal models of familial amyotrophic lateral sclerosis. J Neurol 1997;244:S15-S20.
    • (1997) J Neurol , vol.244
    • Gurney, M.E.1
  • 17
    • 0030690490 scopus 로고    scopus 로고
    • The use of transgenic mouse models of amyotrophic lateral sclerosis in preclinical drug studies
    • Gurney ME. The use of transgenic mouse models of amyotrophic lateral sclerosis in preclinical drug studies. Journal of Neurological Sciences 1997;152:S67-S73.
    • (1997) Journal of Neurological Sciences , vol.152
    • Gurney, M.E.1
  • 18
    • 0030910404 scopus 로고    scopus 로고
    • Oxidative stress, mutant SOD1 and neurofilament pathology in transgenic mouse models of human motor neuron disease
    • Tu Pang-hsien, Gurney ME, Julien JP, Lee VMY and Trojanowski JQ. Oxidative stress, mutant SOD1 and neurofilament pathology in transgenic mouse models of human motor neuron disease. Laboratory Investigation 1997;76:441-456.
    • (1997) Laboratory Investigation , vol.76 , pp. 441-456
    • Pang-hsien, T.1    Gurney, M.E.2    Julien, J.P.3    Lee, V.M.Y.4    Trojanowski, J.Q.5
  • 19
    • 0016816804 scopus 로고
    • The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: Inactivation of the enzyme
    • Hodgson EK, Fridovich I. The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: inactivation of the enzyme. Biochem 1975;14:5294-5299.
    • (1975) Biochem , vol.14 , pp. 5294-5299
    • Hodgson, E.K.1    Fridovich, I.2
  • 20
    • 0025285382 scopus 로고
    • Copper, zinc superoxide dismutase catalyzes hydroxyl radical production from hydrogen peroxide
    • Yim MB, Chock PB, Stadtman ER. Copper, zinc superoxide dismutase catalyzes hydroxyl radical production from hydrogen peroxide. Proc Natl Acad Sci USA 1990;87:5006-5010.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 5006-5010
    • Yim, M.B.1    Chock, P.B.2    Stadtman, E.R.3
  • 22
    • 0029671220 scopus 로고    scopus 로고
    • Altered reactivity of superoxide dismutase in familial amyotrophic lateral sclerosis
    • Wiedau-Pazos M, Goto JJ, Rabizadeh S, et al. Altered reactivity of superoxide dismutase in familial amyotrophic lateral sclerosis. Science 1996;271:515-518.
    • (1996) Science , vol.271 , pp. 515-518
    • Wiedau-Pazos, M.1    Goto, J.J.2    Rabizadeh, S.3
  • 23
    • 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 an increase in Km for hydrogen peroxide
    • Yim MB, Kang JH, Yim HS, Kwak HS, Chock PB, Stadtman ER. A gain-of-function of an amyotrophic lateral sclerosis-associated Cu, Zn superoxide dismutase mutant: an enhancement of free radical formation due to an increase in Km for hydrogen peroxide. Proc Natl Acad Sci USA 1996;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
  • 24
    • 0031784348 scopus 로고    scopus 로고
    • Protein oxidative damage in a transgenic mouse model of familial amytrophic lateral sclerosis
    • Andrus PK, Fleck TJ, Gurney M, Hall ED. Protein oxidative damage in a transgenic mouse model of familial amytrophic lateral sclerosis. J Neurochem 1998;71:2041-2048.
    • (1998) J Neurochem , vol.71 , pp. 2041-2048
    • Andrus, P.K.1    Fleck, T.J.2    Gurney, M.3    Hall, E.D.4
  • 25
    • 0032127330 scopus 로고    scopus 로고
    • Relationship of oxygen radical-induced lipid peroxidation damage to disease onset and progression in a transgenic model of familial ALS
    • Hall ED, Andrus PK, Oostveen JA, Fleck TJ and Gurney M. Relationship of oxygen radical-induced lipid peroxidation damage to disease onset and progression in a transgenic model of familial ALS. J Neuroscience Res 1998;53:66-67.
    • (1998) J Neuroscience Res , vol.53 , pp. 66-67
    • Hall, E.D.1    Andrus, P.K.2    Oostveen, J.A.3    Fleck, T.J.4    Gurney, M.5
  • 26
    • 0027946294 scopus 로고
    • Development of central nervous system pathology in a murine transgenic model of human amyotrophic lateral sclerosis
    • Dal Canto MC and Gurney ME. Development of central nervous system pathology in a murine transgenic model of human amyotrophic lateral sclerosis. Am J Pathol 1994;145:1271-1280.
    • (1994) Am J Pathol , vol.145 , pp. 1271-1280
    • Dal Canto, M.C.1    Gurney, M.E.2
  • 27
    • 0028933344 scopus 로고
    • Neuropathological changes in two lines of mice carrying the mutant human Cu, Zn SOD, and in mice overexpressing wild type human SOD: A model of familial amyotrophic lateral sclerosis (FALS)
    • Dal Canto MC and Gurney ME. Neuropathological changes in two lines of mice carrying the mutant human Cu, Zn SOD, and in mice overexpressing wild type human SOD: A model of familial amyotrophic lateral sclerosis (FALS). Brain Res 1995;676:25-40.
    • (1995) Brain Res , vol.676 , pp. 25-40
    • Dal Canto, M.C.1    Gurney, M.E.2
  • 28
    • 0029890685 scopus 로고    scopus 로고
    • The Golgi apparatus of spinal cord motor neurons in transgenic mice expressing mutant Cu, Zn superoxide dismutase becomes fragmented in early, preclinical stages of the disease
    • Mourelatos Z, Gonatas NK, Stieber A, Gurney ME and Dal Canto MC. The Golgi apparatus of spinal cord motor neurons in transgenic mice expressing mutant Cu, Zn superoxide dismutase becomes fragmented in early, preclinical stages of the disease. Proc Natl Acad Sci USA 1996;93:5472-5477.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 5472-5477
    • Mourelatos, Z.1    Gonatas, N.K.2    Stieber, A.3    Gurney, M.E.4    Dal Canto, M.C.5
  • 29
    • 0029966363 scopus 로고    scopus 로고
    • Transgenic mice carrying a human mutant superoxide dismutase transgene develop neuronal cytoskeletal pathology resemb;ing human amyotrophic lateral sclerosis lesions
    • Tu PH, Raju P, Robinson KA, Gurney ME, Trojanowski JQ, and Lee VMY. Transgenic mice carrying a human mutant superoxide dismutase transgene develop neuronal cytoskeletal pathology resemb;ing human amyotrophic lateral sclerosis lesions. Proc Natl Acad Sci USA 1996;93:3155-3160.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 3155-3160
    • Tu, P.H.1    Raju, P.2    Robinson, K.A.3    Gurney, M.E.4    Trojanowski, J.Q.5    Lee, V.M.Y.6
  • 30
    • 0026609559 scopus 로고
    • Alternative excitotoxic hypotheses
    • Albin RL, Greenamyer JT. Alternative excitotoxic hypotheses. Neurol 1992;42:733-737.
    • (1992) Neurol , vol.42 , pp. 733-737
    • Albin, R.L.1    Greenamyer, J.T.2
  • 31
    • 0026584524 scopus 로고
    • Does impairment of energy metabolism result in excitotoxic neuronal death in neurodegenerative illnesses?
    • Beal MF. Does impairment of energy metabolism result in excitotoxic neuronal death in neurodegenerative illnesses? Ann Neurol 1992;31:119-130.
    • (1992) Ann Neurol , vol.31 , pp. 119-130
    • Beal, M.F.1
  • 32
    • 0029125857 scopus 로고
    • Aging, energy and oxidative stress in neurodegenerative diseases
    • Beal MF. Aging, energy and oxidative stress in neurodegenerative diseases. Ann Neurol 1995;38:357-359.
    • (1995) Ann Neurol , vol.38 , pp. 357-359
    • Beal, M.F.1
  • 33
    • 0031559896 scopus 로고    scopus 로고
    • Expression of a Cu, Zn superoxide dismutase typical of familial ALS induces mitochondrial alteration and increase of cytosolic Ca concentration in transfected neuroblastoma SH-SY5Y cells
    • Cari MT et al. Expression of a Cu, Zn superoxide dismutase typical of familial ALS induces mitochondrial alteration and increase of cytosolic Ca concentration in transfected neuroblastoma SH-SY5Y cells. FEBS Lett 1997;414:365-368.
    • (1997) FEBS Lett , vol.414 , pp. 365-368
    • Cari, M.T.1
  • 34
    • 0026585611 scopus 로고
    • Intracellular compartmentation, structure and function of creatine kinase isoenzymes in tissues with high and fluctuating energy demands: The phosphocratinr circuit for cellular energy homeostasis
    • Wallimann T, Wyss M, Brdiczka D, Nicolay K, Eppenberger HM. Intracellular compartmentation, structure and function of creatine kinase isoenzymes in tissues with high and fluctuating energy demands: the phosphocratinr circuit for cellular energy homeostasis. Biochem J 1992;281:21-40.
    • (1992) Biochem J , vol.281 , pp. 21-40
    • Wallimann, T.1    Wyss, M.2    Brdiczka, D.3    Nicolay, K.4    Eppenberger, H.M.5
  • 36
    • 0029572464 scopus 로고
    • Expression of brain-type creatine kinase and ubiquitous mitochondrial creatine kinase in the fetal rat brain: Evidence for a nuclear energy shuttle
    • Chen L, Roberts R, Friedman DL. Expression of brain-type creatine kinase and ubiquitous mitochondrial creatine kinase in the fetal rat brain: evidence for a nuclear energy shuttle. J Comp Neurol 1995;363:389-401.
    • (1995) J Comp Neurol , vol.363 , pp. 389-401
    • Chen, L.1    Roberts, R.2    Friedman, D.L.3
  • 37
    • 0028034636 scopus 로고
    • Invitro complex formation between the octamer of mitochondrial creatine kinase and porin
    • Brdiczka D, Kaldis P, Wallimann T. Invitro complex formation between the octamer of mitochondrial creatine kinase and porin. J Biol Chem 1994;269:27640-27644.
    • (1994) J Biol Chem , vol.269 , pp. 27640-27644
    • Brdiczka, D.1    Kaldis, P.2    Wallimann, T.3
  • 38
    • 0031559949 scopus 로고    scopus 로고
    • The role of creatine kinase inhibition in mitochondrial permeability transition
    • O'Gorman et al. The role of creatine kinase inhibition in mitochondrial permeability transition. FEBS Lett 1997;414:253-257.
    • (1997) FEBS Lett , vol.414 , pp. 253-257
    • O'Gorman1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.