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Volumn 69, Issue 5, 1997, Pages 1936-1944

Decreased zinc affinity of amyotrophic lateral sclerosis, associated superoxide dismutase mutants leads to enhanced catalysis of tyrosine nitration by peroxynitrite

Author keywords

Amyotrophic lateral sclerosis; Motor neurons; Neurofilament L; Nitration catalysis; Nitrotyrosine; Superoxide dismutase; Zinc

Indexed keywords

COPPER ZINC SUPEROXIDE DISMUTASE; MUTANT PROTEIN; NEUROFILAMENT PROTEIN; PEROXYNITRITE; TYROSINE; ZINC;

EID: 0030833449     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1997.69051936.x     Document Type: Article
Times cited : (435)

References (53)
  • 1
    • 0028971936 scopus 로고
    • Induction of nitrotyrosine-like immunoreactivity in the lower motor neuron of amyotrophic lateral sclerosis
    • Abe K., Pan L. H., Watanabe M., Kato T., and Itoyama Y. (1995) Induction of nitrotyrosine-like immunoreactivity in the lower motor neuron of amyotrophic lateral sclerosis. Neurosci. Lett. 199, 152-154.
    • (1995) Neurosci. Lett. , vol.199 , pp. 152-154
    • Abe, K.1    Pan, L.H.2    Watanabe, M.3    Kato, T.4    Itoyama, Y.5
  • 2
    • 0029682870 scopus 로고    scopus 로고
    • Oxidative damage and tyrosine nitration from peroxynitrite
    • Beckman J. S. (1996) Oxidative damage and tyrosine nitration from peroxynitrite. Chem. Res. Toxicol. 9, 836-844.
    • (1996) Chem. Res. Toxicol. , vol.9 , pp. 836-844
    • Beckman, J.S.1
  • 3
    • 0029805172 scopus 로고    scopus 로고
    • Nitric oxide, Superoxide, and peroxynitrite - The good, the bad, and the ugly
    • Beckman J. S. and Koppenol W. H. (1996) Nitric oxide, Superoxide, and peroxynitrite - the good, the bad, and the ugly. Am. J. Physiol Cell Physiol. 40, C1424-C1437.
    • (1996) Am. J. Physiol Cell Physiol. , vol.40
    • Beckman, J.S.1    Koppenol, W.H.2
  • 7
    • 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 Jr., R.H.3    Beal, M.F.4
  • 8
    • 0029991827 scopus 로고    scopus 로고
    • Colocalization of NOS and SOD1 in neurofilament accumulation within motor neurons of amyotrophic lateral sclerosis: An immunohistochemical study
    • Chou S. M., Wang H. S., and Komai K. (1996) Colocalization of NOS and SOD1 in neurofilament accumulation within motor neurons of amyotrophic lateral sclerosis: an immunohistochemical study. J. Chem. Neuroanat. 10, 249-258.
    • (1996) J. Chem. Neuroanat. , vol.10 , pp. 249-258
    • Chou, S.M.1    Wang, H.S.2    Komai, K.3
  • 10
    • 0029004898 scopus 로고
    • Defective axonal transport in a transgenic mouse model of amyotrophic lateral sclerosis
    • Collard J. F., Cote F., and Julien J. P. (1995) Defective axonal transport in a transgenic mouse model of amyotrophic lateral sclerosis. Nature 375, 61-64.
    • (1995) Nature , vol.375 , pp. 61-64
    • Collard, J.F.1    Cote, F.2    Julien, J.P.3
  • 11
    • 0028033620 scopus 로고
    • Copydependent and correct developmental expression of the human neurofilament heavy gene in transgenic mice
    • Cote F., Collard J. F., Houle D., and Julien J. P. (1994) Copydependent and correct developmental expression of the human neurofilament heavy gene in transgenic mice. Brain Res. Mol. 1-2, 99-105.
    • (1994) Brain Res. Mol. , vol.1-2 , pp. 99-105
    • Cote, F.1    Collard, J.F.2    Houle, D.3    Julien, J.P.4
  • 12
    • 0029781820 scopus 로고    scopus 로고
    • The importance of Superoxide in nitric oxide-dependent toxicity: Evidence for peroxynitrite-mediated injury
    • Crow J. P. and Beckman J. S. (1996) The importance of Superoxide in nitric oxide-dependent toxicity: evidence for peroxynitrite-mediated injury. Adv. Exp. Med. Biol. 387, 147-161.
    • (1996) Adv. Exp. Med. Biol. , vol.387 , pp. 147-161
    • Crow, J.P.1    Beckman, J.S.2
  • 13
    • 0029794290 scopus 로고    scopus 로고
    • Detection and quantitation of nitrotyrosine residues in proteins: In vivo marker of peroxynitrite
    • Crow J. P. and Ischiropoulos H. (1996) Detection and quantitation of nitrotyrosine residues in proteins: in vivo marker of peroxynitrite. Methods Enzymol. 269, 185-194.
    • (1996) Methods Enzymol. , vol.269 , pp. 185-194
    • Crow, J.P.1    Ischiropoulos, H.2
  • 14
    • 1842289165 scopus 로고    scopus 로고
    • Superoxide dismutase catalyzes nitration of tyrosines by peroxynitrite in the rod and head domains of neurofilament-L
    • Crow J. P., Ye Z. Y., Strong M., Kirk M., Barnes S., and Beckman J. S. (1997) Superoxide dismutase catalyzes nitration of tyrosines by peroxynitrite in the rod and head domains of neurofilament-L. J. Neurochem. 69, 1945-1953.
    • (1997) J. Neurochem. , vol.69 , pp. 1945-1953
    • Crow, J.P.1    Ye, Z.Y.2    Strong, M.3    Kirk, M.4    Barnes, S.5    Beckman, J.S.6
  • 15
    • 1842323902 scopus 로고    scopus 로고
    • Peroxynitrite as a mediator of injury in brain ischemia, atherosclerosis, and amyotrophic lateral sclerosis
    • (Robertson J. T. and Nowak T. S. Jr., eds), in press. Futura Publishing Co., Armonk, New York
    • Crow J. P., Sampson J. B., and Beckman J. S. (1998) Peroxynitrite as a mediator of injury in brain ischemia, atherosclerosis, and amyotrophic lateral sclerosis, in Frontiers in Cerebrovascular Disease - Mechanisms, Diagnosis, and Treatment (Robertson J. T. and Nowak T. S. Jr., eds), in press. Futura Publishing Co., Armonk, New York.
    • (1998) Frontiers in Cerebrovascular Disease - Mechanisms, Diagnosis, and Treatment
    • Crow, J.P.1    Sampson, J.B.2    Beckman, J.S.3
  • 17
    • 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
  • 20
    • 0015935503 scopus 로고
    • On the stability of bovine Superoxide dismutase. the effects of metals
    • Forman H. J. and Fridovich I. (1973) On the stability of bovine Superoxide dismutase. The effects of metals. J. Biol. Chem. 248, 2645-2649.
    • (1973) J. Biol. Chem. , vol.248 , pp. 2645-2649
    • Forman, H.J.1    Fridovich, I.2
  • 21
    • 0015937128 scopus 로고
    • Histidine at the active site of Superoxide dismutase
    • Forman H. J., Evans H. J., Hill R. L., and Fridovich I. (1973) Histidine at the active site of Superoxide dismutase. Biochemistry 12, 823-827.
    • (1973) Biochemistry , vol.12 , pp. 823-827
    • Forman, H.J.1    Evans, H.J.2    Hill, R.L.3    Fridovich, I.4
  • 23
    • 0026042995 scopus 로고
    • Cytopathology of amyotrophic lateral sclerosis
    • Hirano A. (1991) Cytopathology of amyotrophic lateral sclerosis. Adv. Neurol 56, 91-101.
    • (1991) Adv. Neurol , vol.56 , pp. 91-101
    • Hirano, A.1
  • 24
    • 0021385195 scopus 로고
    • Selective binding behavior of zinc(II) and copper(II) ions to their native sites of apo-bovine Superoxide dismutase
    • Hirose J., Yamada M., Hayakawa C., Nagao H., Noji M., and Kidani Y. (1984) Selective binding behavior of zinc(II) and copper(II) ions to their native sites of apo-bovine Superoxide dismutase. Biochem. Int. 8, 401-408.
    • (1984) Biochem. Int. , vol.8 , pp. 401-408
    • Hirose, J.1    Yamada, M.2    Hayakawa, C.3    Nagao, H.4    Noji, M.5    Kidani, Y.6
  • 25
    • 0016816804 scopus 로고
    • The interaction of bovine erythrocyte Superoxide dismutase with hydrogen peroxide: Inactivation of the enzyme
    • Hodgson E. K. and Fridovich I. (1975) The interaction of bovine erythrocyte Superoxide dismutase with hydrogen peroxide: inactivation of the enzyme. Biochemistry 14, 5294-5299.
    • (1975) Biochemistry , vol.14 , pp. 5294-5299
    • Hodgson, E.K.1    Fridovich, I.2
  • 27
  • 28
    • 0028956596 scopus 로고
    • CNS distribution and overexpression of neurofilament light proteins (NF-L) in mice transgenic for the human NF-L: Aberrant accumulation in thalamic perikarya
    • Mathieu J. F., Ma D., Descarries L., Vallee A., Parent A., Julien J. P., and Doucet G. (1995) CNS distribution and overexpression of neurofilament light proteins (NF-L) in mice transgenic for the human NF-L: aberrant accumulation in thalamic perikarya. Exp. Neurol. 132, 134-146.
    • (1995) Exp. Neurol. , vol.132 , pp. 134-146
    • Mathieu, J.F.1    Ma, D.2    Descarries, L.3    Vallee, A.4    Parent, A.5    Julien, J.P.6    Doucet, G.7
  • 29
    • 0014691242 scopus 로고
    • Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein)
    • McCord J. M. and Fridovich I. (1969) Superoxide dismutase. An enzymic 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
  • 30
    • 0027228294 scopus 로고
    • The reaction of nitric oxide with organic peroxyl radicals
    • Padmaja S. and Huie R. E. (1993) The reaction of nitric oxide with organic peroxyl radicals. Biochem. Biophys. Res. Commun. 195, 539-544.
    • (1993) Biochem. Biophys. Res. Commun. , vol.195 , pp. 539-544
    • Padmaja, S.1    Huie, R.E.2
  • 31
    • 0020348047 scopus 로고
    • A pH-dependent Superoxide dismutase activity for zinc-free bovine erythrocuprein. Reexamination of the role of zinc in the holoprotein
    • Pantoliano M. W., Valentine J. S., Burger A. R., and Lippard S. J. (1982) A pH-dependent Superoxide dismutase activity for zinc-free bovine erythrocuprein. Reexamination of the role of zinc in the holoprotein. J. Inorg. Biochem. 17, 325-341.
    • (1982) J. Inorg. Biochem. , vol.17 , pp. 325-341
    • Pantoliano, M.W.1    Valentine, J.S.2    Burger, A.R.3    Lippard, S.J.4
  • 33
  • 35
    • 0028888945 scopus 로고
    • Transgenic mice expressing an altered murine Superoxide dismutase gene provide an animal model of amyotrophic lateral sclerosis
    • Ripps M. E., Huntley G. W., Hof P. R., Morrison J. H., and Gordon J. W. (1995) Transgenic mice expressing an altered murine Superoxide dismutase gene provide an animal model of amyotrophic lateral sclerosis. Proc. Natl. Acad. Sci. USA 92, 689-693.
    • (1995) Proc. Natl. Acad. Sci. USA , 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
  • 40
    • 0010726243 scopus 로고    scopus 로고
    • Copper/zinc Superoxide dismutase in familial amyotrophic lateral sclerosis: Tyrosine nitration catalysis as a possible mutational gain in function
    • (Salem M. A., Yasiu M., Strong M. J., Ota K., and Verity M. A., eds), CRC Press, Boca Raton Florida
    • Sampson J. S., Crow J. P., Strong M. J., and Beckman J. S. (1997) Copper/zinc Superoxide dismutase in familial amyotrophic lateral sclerosis: tyrosine nitration catalysis as a possible mutational gain in function, in Mineral and Metal Neurotoxicology (Salem M. A., Yasiu M., Strong M. J., Ota K., and Verity M. A., eds), 393-403. CRC Press, Boca Raton Florida.
    • (1997) Mineral and Metal Neurotoxicology , pp. 393-403
    • Sampson, J.S.1    Crow, J.P.2    Strong, M.J.3    Beckman, J.S.4
  • 41
    • 0026346245 scopus 로고
    • Ligand substitution and sulfhydryl reactivity of metallothionein
    • Shaw C. F., Savas M. M., and Petering D. H. (1991) Ligand substitution and sulfhydryl reactivity of metallothionein. Methods Enzymol. 205, 401-414.
    • (1991) Methods Enzymol. , vol.205 , pp. 401-414
    • Shaw, C.F.1    Savas, M.M.2    Petering, D.H.3
  • 42
    • 0028168308 scopus 로고
    • 3+ binding and conformational properties of the alanine-substituted C-terminal domain of the NF-M protein and its relevance to Alzheimer's disease
    • 3+ binding and conformational properties of the alanine-substituted C-terminal domain of the NF-M protein and its relevance to Alzheimer's disease. Biochemistry 33, 9627-9636.
    • (1994) Biochemistry , vol.33 , pp. 9627-9636
    • Shen, Z.M.1    Perczel, A.2    Hollosi, M.3    Nagypal, I.4    Fasman, G.D.5
  • 43
    • 0014194993 scopus 로고
    • Conversion of 3-nitrotyrosine to 3-aminotyrosine in peptides and proteins
    • Sokolovsky M., Riordan J. F., and Vallee B. L. (1967) Conversion of 3-nitrotyrosine to 3-aminotyrosine in peptides and proteins. Biochem. Biophys. Res. Commun. 27, 20-25.
    • (1967) Biochem. Biophys. Res. Commun. , vol.27 , pp. 20-25
    • Sokolovsky, M.1    Riordan, J.F.2    Vallee, B.L.3
  • 44
    • 0021081808 scopus 로고
    • Structure and mechanism of copper, zinc Superoxide dismutase
    • Tainer J. A., Getzoff E. D., Richardson J. S., and Richardson D. C. (1983) Structure and mechanism of copper, zinc Superoxide dismutase. Nature 306, 284-287.
    • (1983) Nature , vol.306 , pp. 284-287
    • Tainer, J.A.1    Getzoff, E.D.2    Richardson, J.S.3    Richardson, D.C.4
  • 45
    • 0029966363 scopus 로고    scopus 로고
    • Transgenic mice carrying a human mutant Superoxide dismutase transgene develop neuronal cytoskeletal pathology resembling human amyotrophic lateral sclerosis lesions
    • Tu P. H., Raju P., Robinson K. A., Gurney M. E., Trojanowski J. Q., and Lee V. M. Y. (1996) Transgenic mice carrying a human mutant Superoxide dismutase transgene develop neuronal cytoskeletal pathology resembling human amyotrophic lateral sclerosis lesions. Proc. Natl. Acad. Sci. USA 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
  • 48
    • 0026099960 scopus 로고
    • Motor neuron disease (amyotrophic lateral sclerosis)
    • Williams D. B. and Windebank A. J. (1991) Motor neuron disease (amyotrophic lateral sclerosis). Mayo Clin. Proc. 66, 54-82.
    • (1991) Mayo Clin. Proc. , vol.66 , pp. 54-82
    • Williams, D.B.1    Windebank, A.J.2
  • 49
    • 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
  • 50
    • 0027410516 scopus 로고
    • Increased expression of neurofilament subunit NF-L produces morphological alterations that resemble the pathology of human motor neuron disease
    • Xu Z., Cork L. C., Griffin J. W., and Cleveland D. W. (1993a) Increased expression of neurofilament subunit NF-L produces morphological alterations that resemble the pathology of human motor neuron disease. Cell 73, 23-33.
    • (1993) Cell , vol.73 , pp. 23-33
    • Xu, Z.1    Cork, L.C.2    Griffin, J.W.3    Cleveland, D.W.4
  • 52
    • 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
  • 53
    • 0027154585 scopus 로고
    • Polymerase chain reaction-based point mutagenesis protocol
    • Zhao L. J., Zhang Q. X., and Padmanabhan R. (1993) Polymerase chain reaction-based point mutagenesis protocol. Methods Enzymol. 217, 218-227.
    • (1993) Methods Enzymol. , vol.217 , pp. 218-227
    • Zhao, L.J.1    Zhang, Q.X.2    Padmanabhan, R.3


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