Morphological aspects of superoxide dismutase-1 mutation in amyotrophic lateral sclerosis and its transgenic mouse model

Acta Histochemica et Cytochemica

Volumn 32, Issue 1, 1999, Pages 17-30

  Shibata, Noriyuki ^a   Kobayashi, Makio ^a   Hirano, Asao ^b   Asayama, Kohtaro ^c   Horiuchi, Seiko ^d   Dal Canto, Mauro C ^e   Gurney, Mark E ^f  

^a TOKYO WOMEN'S MEDICAL UNIVERSITY   (Japan)

^b MONTEFIORE MEDICAL CENTER   (United States)

^c UNIVERSITY OF YAMANASHI   (Japan)

^d KUMAMOTO UNIV SCHOOL OF MEDICINE   (Japan)

^e NORTHWESTERN UNIVERSITY   (United States)

^f PFIZER INC   (United States)

Author keywords

Advanced glycation endproducts; Amyotrophic lateral sclerosis; Hyaline inclusions; Immunohistochemistry; Superoxide dismutase; Transgenic mouse model

Indexed keywords

AMYOTROPHIC LATERAL SCLEROSIS; ELECTRON MICROSCOPY; IMMUNOANALYSIS; MODEL; MOUSE; SUPEROXIDE DISMUTASE; TRANSGENIC ANIMAL;

EID: 0032985178     PISSN: 00445991     EISSN: None     Source Type: Journal    
DOI: 10.1267/ahc.32.17     Document Type: Conference Paper

References (117)

1. Abe, K., Aoki, M., Ikeda, M., Watanabe, M., Hirai, S. and Itoyama, Y.: Clinical characteristics of familial amyotrophic lateral sclerosis with Cu/Zn superoxide dismutase gene mutations. J. Neurol. Sci. 136; 108-116, 1996.
2. ε-carboxymethyllysine as a degradation product of fructoselysine in glycated protein. J. Biol. Chem. 261; 4889-4894, 1986.
3. Andersen, P. M., Nilsson, P., Ala-Hurula, V., Keränen, M. -L., Tarvainen, I., Haltia, T., Nilsson, L., Binzer, M., Forsgren, L. and Marklund, S. L.: Amyotrophic lateral sclerosis associated with homozygosity for an Asp90Ala mutation in CuZn-superoxide dismutase. Nat. Genet. 10; 61-65, 1995.
4. Andersen, P. M., Forsgren, L., Binzer, M., Nilsson, P., Ala-Hurula, V., Keränen, M. -L., Bergmark, L., Saarinen, A., Haltia, T., Tarvainen, I., Kinnunen, E., Udd, B. and Marklund, S. L.: Autosomal recessive adult-onset amyotrophic lateral sclerosis associated with homozygosity for Asp90Ala CuZn-superoxide dismutase mutation: a clinical and genealogical study of 36 patients. Brain 120; 1723-1737, 1997.
5. Aoki, M., Ogasawara, M., Matsubara, Y., Narisawa, K., Nakamura, S., Itoyama, Y. and Abe, K.: Familial amyotrophic lateral sclerosis (ALS) in Japan associated with H46R mutation in Cu/Zn superoxide dismutase gene: a possible new subtype of familial ALS. J. Neurol. Sci. 126; 77-83, 1994.
6. Aoki, M., Abe, K., Houi, K., Ogasawara, M., Matsubara, Y., Kobayashi, T., Mochio, S., Narisawa, K. and Itoyama, Y.: Variance of age at onset in a Japanese family with amyotrophic lateral sclerosis associated with a novel Cu/Zn superoxide dismutase mutation. Ann. Neurol. 37; 676-679, 1995.
7. Arai, K., Maguchi, S., Fujii, S., Ishibashi, H., Oikawa, K. and Taniguchi, N.: Glycation and inactivation of human Cu-Zn-superoxide dismutase. J. Biol. Chem. 262; 16969-16972, 1987.
8. Asayama, K., Janco, R. L. and Burr, I. M.: Selective induction of manganous superoxide dismutase in human monocytes. Am. J. Physiol. 249; C393-C397, 1985.
9. Beal, M. F., Ferrante, R. J., Browne S. E., Matthews, R. T., Kowall, N. W. and Brown Jr, R. H.: Increased 3-nitrotyrosine in both sporadic and familial amyotrophic lateral sclerosis. Ann. Neurol. 42; 646-654, 1997.
10. Beckman, J. S., Carson, M., Smith, C. D. and Koppenol, W. H.: ALS, SOD and peroxynitrite. Nature 364; 584, 1993.
11. Bereznai, B., Winkler, A., Borasio, G. D. and Gasser, T.: A novel SOD1 mutation in an Austrian family with amyotrophic lateral sclerosis. Neuromusc. Disord. 7; 113-116, 1997.
12. Borchelt, D. R., Wong, P. C., Sisodia, S. S. and Price, D. L.: Transgenic mouse models of Alzheimer's disease and amyotrophic lateral sclerosis. Brain Pathol. 8; 735-757, 1998.
13. Borchelt, D. R., Lee, M. K., Slunt, H. S., Guarnieri, M., Xu, Z. -S., Wong, P. C., Brown Jr, R. H., Price, D. L., Sisodia, S. S. and Cleveland, D. W.: Superoxide dismutase 1 with mutations linked to familial amyotrophic lateral sclerosis possesses significant activity. Proc. Natl. Acad. Sci. USA 91; 8292-8296, 1994.
14. Borchelt, D. R., Guarnieri, M., Wong, P. C., Lee, M. K., Slunt, H. S., Xu, Z. -S., Sisodia, S. S., Price, D. L. and Cleveland, D. W.: Superoxide dismutase 1 subunits with mutations linked to familial amyotrophic lateral sclerosis do not affect wild-type subunits function. J. Biol. Chem. 270; 3234-3238, 1995.
15. Brännström, T., Nilsson, K. E. P. and Marklund, S.: Transgenic mice with the D90A SOD1 mutation and motor neuron disease: a clinical, morphological, and biochemical study (Abstract). Brain Pathol. 7; 1073, 1997.
16. Bruijn, L. I., Beal, M. F., Becher, M. W., Schulz, J. B., Wong, P.C., Price, D. L. and Cleveland, D. W.: Elevated free nitrotyrosine levels, but not protein-bound nitrotyrosine or hydroxyl radicals, throughtout 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.
17. Bruijn, L. I., Houseweart, M. K., Kato, S., Anderson, K. L., Anderson, S. D., Ohama, E., Reasume, A. G., Scott, R. W. and Cleveland, D. W.: Aggregation and motor neuron toxicity of an ALS-linked SOD1 mutant independent from wild-type SOD1. Science 281; 1851-1854, 1998.
18. Bruijn, L. I., Becher, M. W., Lee, M. K., Anderson, K. L., Jenkins, N. A., Copeland, N. G., Sisodia, S. S., Rothstein, J. D., Borchelt, D. R., Price, D. L. and Cleveland, D. W.: ALS-linked SOD1 mutant G85R mediates damage to astrocytes and promotes rapidly progressive disease with SOD1-containing inclusions. Neuron 18; 327-338, 1997.
19. Calder, V. L., Domigan, N. M., George, P. R., Donaldson, I. M. and Winterbourn, C. C.: Superoxide dismutase (glu100 →gly) in a family with inherited motor neuron disease: detection of mutant superoxide dismutase activity and the presence of heterodimers. Neurosci. Lett. 189; 143-146, 1995.
20. Carri, M. T., Battistoni, A., Polizio, F., Desideri, A. and Rotilio, G.: Impaired copper binding by the H46R mutant of human Cu,Zn superoxide dismutase, involved in amyotrophic lateral sclerosis. FEBS Lett. 356; 314-316, 1994.
21. 2+ concentration in transfected neuroblastoma SH-SY5Y cells. FEBS Lett. 414; 365-368, 1997.
22. Castellani, R., Smith, M. A., Richey, P. L. and Perry, G.: Glycoxidation and oxidative stress in Parkinson disease and diffuse Lewy body disease. Brain Res. 737; 195-200, 1996.
23. Cudkowicz, M. E., McKenna-Yasek, D., Sapp, P. E., Chin, W., Geller, B., Hayden, D. L., Schoenfeld, D. A., Hosler, B. A., Horvitz, H. R. and Brown, R. H.: Epidemiology of mutations in superoxide dismutase in amyotrophic lateral sclerosis. Ann. Neurol. 41; 210-221, 1997.
24. Dal Canto, M. C. and Gurney, M. E.: 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.
25. Dal Canto, M. C. and Gurney, M. E.: A low expressor line of transgenic mice carrying a mutant human Cu,Zn superoxide dismutase (SOD1) gene develops pathological changes that most closely resemble those in human amyotrophic lateral sclerosis. Acta Neuropathol. 93; 537-550, 1997.
26. De Belleroche, J.: Functional and structural correlates of the SOD-1 mutation in UK families with amyotrophic lateral sclerosis (Abstract). The 6th International Symposium on ALS/MND, Dublin, 1995.
27. Deng, H. -X., Tainer, J. A., Mitsumoto, H., Ohnishi, A., He, X., Hung, W.-Y., Zhao, Y., Juneja, T., Hentati, A. and Siddique, T.: Two novel SOD1 mutations in patients with familial amyotrophic lateral sclerosis. Hum. Mol. Genet. 4; 1113-1116, 1995.
28. Deng, H. -X., Hentati, A., Tainer, J. A., Iqbal, Z., Cayabyab, A., Hung, W. -Y., Getzoff, E. D., Hu, P., Herzfeldt, B., Roos, R. P., Warner, C., Deng, G., Soriano, E., Smyth, C., Parge, H. E., Ahmed, A., Roses, A. D., Hallewell, R. A., Pericak-Vance, M. A. and Siddique, T.: Amyotrophic lateral sclerosis and structural defects in Cu,Zn superoxid dismutase. Science 261; 1047-1051, 1993.
29. Durham, H. D., Roy, J., Dong, L. and Figlewicz, D. A.: Aggregation of mutant Cu/Zn superoxide dismutase proteins in a culture model of ALS. J. Neuropathol. Exp. Neurol. 56; 523-530, 1997.
30. Elshafey, A., Lanyon, W. G. and Connor, J. M.: Identification of a new missense point mutation in exon 4 of the Cu/Zn superoxide dismutase (SOD-1) gene in a family with amyotrophic lateral sclerosis. Hum. Mol. Genet. 3; 363-364, 1994.
31. Enayat, Z. E., Orrell, R. W., Claus, A., Ludolph, A., Bachus, R., Brockmüller, J., Ray-Chaudhuri, K., Radunovic, A., Shaw, C., Wilkinson, J., King, A., Swash, M., Leigh, P. N., De Belleroche, J. and Powell, J.: Two novel mutations in the gene for copper zinc superoxide dismutase in UK families with amyotrophic lateral sclerosis. Hum. Mol. Genet. 4; 1239-1240, 1995.
32. Esteban, J., Rosen, D. R., Bowling, A. C., Sapp, P., McKenna-Yasek, D., O'Regan, J. P., Beal, M. F., Horvitz, H. R. and Brown Jr, R. H.: Identification of two novel mutations and a new polymorphism in the gene for Cu/Zn superoxide dismutase in patients with amyotrophic lateral sclreosis. Hum. Mol. Genet. 3; 997-998, 1994.
33. Fridovich, I.: Superoxide dismutases. Adv. Enzymol. Relat. Areas. Mol. Biol. 58; 61-97, 1986.
34. ε-(carboxymethyl)lysine, is a product of both lipid peroxidation and glycoxidation reactions. J. Biol. Chem. 271; 9982-9986, 1996.
35. Gonatas, N. K., Stieber, A., Mourelatos, Z., Chen, Y., Gonatas, J. O., Appel, S. H., Hays, A. P., Hickey, W. F. and Hauw, J. -J.: Fragmentation of the Golgi apparatus of motor neurons in amyotrophic lateral sclerosis. Am. J. Pathol. 140; 731-737, 1992.
36. Gurney, M. E., Cutting, F. B., Zhai, P., Doble, A., Taylor, C. P., Andrus, P. K. and Hall, E. D.: Benefit of vitamin E, riluzole, and gabapentine in a transgenic model of familial amyotrophic lateral sclerosis. Ann. Neurol. 39; 147-157, 1996.
37. Gurney, M. E., Pu, H., Chiu, A. Y., Dal Canto, M. C., Pochow, C. Y., Alexander, D. D., Caliendo, J., Hentati, A., Kwon, Y. W., Deng, H. -X., Chen, W., Zhai, P., Sufit, R. L. and Siddique, T.: Motor neuron degeneration in mice that express a human Cu,Zn superoxide dismutase mutation. Science 264; 1772-1775, 1994.
38. Hayase, F., Nagaraj, R. H., Miyata, S., Njoroge, F. G. and Monnier, V. M.: Aging of proteins: immunological detection of a glucose-derived pyrrole formed during Maillard reaction in vivo. J. Biol. Chem. 263; 3758-3764, 1989.
39. Hirano, A., Kurland, L. T. and Sayre, G. P.: Familial amyotrophic lateral sclerosis: a subgroup characterized by posterior and spinocerebellar tract involvement and hyaline inclusions in the anterior horn cells. Arch. Neurol. 16; 232-243, 1967.
40. Hirano, A., Nakano, I., Kurland, L. T., Mulder, D. W., Holley, P. W. and Saccomanno, G.: Fine structural study of neurofibrillary changes in a family with amyotrophic lateral sclerosis. J. Neuropathol. Exp. Neurol. 43; 471-480, 1984.
41. 7→Glu) deduced from lymphocytes mRNA sequences from Japanese patients with familial amyotrophic lateral sclerosis. Biochem. Biophys. Res. Commun. 204; 572-577, 1994.
42. Hosler, B. A., Nicholson, G. A., Sapp, P. C., Chin, W., Orrell, R. W., De Belleroche, J. S., Esteban, J., Hayward, L. J., MacKenna-Yasek, D., Yeung, L., Cherryson, A. K., Dench, J. E., Wilton, S. D., Laing, N. G., Horvitz, H. R. and Brown Jr, R. H.: Three novel mutations and two variants in the gene for Cu/Zn superoxide dismutase in familial amyotrophic lateral sclerosis. Neuromusc. Disord. 6; 361-366, 1996.
43. ε-(Carboxymethyl) lysine protein adduct is a major immunological epitope in proteins modified with advanced glycation end products of the Maillard reaction. Biochemistry 35; 8075-8083, 1996.
44. Ikeda, M., Abe, K., Aoki, M, Sahara, M., Watanabe, M., Shoji, M., St. George-Hyslop, P. H., Hirai, S. and Itoyama, Y.: Variable clinical symptoms in familial amyotrophic lateral sclerosis with a novel point mutation in the Cu/Zn superoxide dismutase gene. Neurology 45; 2038-2042, 1995.
45. Ikeda, M., Abe, K., Aoki, M, Ogasawara, M., Kameya, T., Watanabe, M., Shoji, M., Hirai, S. and Itoyama, Y.: A novel point mutation in the Cu/Zn superoxide dismutase gene in a patinet with familial amyotrophic lateral sclerosis. Hum. Mol. Genet. 4; 491-492, 1995.
46. Ince, P. G., Shaw, P. J., Slade, J. Y., Jones, C. and Hudgson, P.: Familial amyotrophic lateral sclerosis with a mutation in exon 4 of the Cu/Zn superoxide dismutase gene: pathological and immunohistochemical changes. Acta Neuropathol. 92; 395-403, 1996.
47. Jaarsma, D., Guchelaar, H.-J., Haasdijk, E., Vianney de Jong, J. M. B. and Holstege, J. C.: The antioxidant N-acetyl-cysteine does not delay disease onset and death in a transgenic mouse model of amyotrophic lateral sclerosis. Ann. Neurol. 44; 293, 1998.
48. Jones, C. T., Swingler, R. J. and Brock, J. H.: Identification of a novel SOD1 mutation in an apparently sporadic amyotrophic lateral sclerosis patient and the detection of Ile113Thr in three others. Hum. Mol. Genet. 3; 649-650, 1994.
49. Jones, C. T., Shaw, P. J., Chari, G. and Brock, D. J. H.: Identification of a novel exon 4 SOD1 mutation in a sporadic amyotrophic lateral sclerosis patient. Mol. Cell. Probes. 8; 329-330, 1994.
50. Juneja, T., Pericak-Vance, M. A., Laing, N. G., Dave, S. and Siddique, T.: Prognosis in familial amyotrophic lateral sclerosis: progression and survival in patients with glu100gly and ala4val mutations in Cu,Zn superoxide dismutase. Neurology 48; 55-57, 1997.
51. Kato, S., Hayashi, H., Nakashima, K., Nanba, E., Kato, M., Hirano, A., Nakano, I., Asayama, K. and Ohama, E.: Pathological characterization of astrocytic hyaline inclusions in familial amyotrophic lateral sclerosis. Am. J. Pathol. 151; 611-620, 1997.
52. 106→Val (CTC→GTC) mutation of superoxide dismutase-1 gene in patient with familial amyotrophic lateral sclerosis in Japan. Lancet 343: 1501, 1994.
53. Kawamata, J., Shimohama, S., Hasegawa, H., Imura, T., Kimura, J. and Ueda, K.: Deletion and point mutation in superoxide dismutase-1 gene in amyotrophic lateral sclerosis. In: Progress and Perspectives in Basic Research and Clinical Application, (eds.) I. Nakano & A. Hirano, International Congress Series 1104, Elsevier, pp. 276-280, 1996.
54. Kawamata, J., Shimohama, S., Takano, S., Harada, K., Ueda, K. and Kimura, J.: Novel G16S (GGC-AGC) mutation in the SOD1 gene in a patient with apparently sporadic youngonset amyotrophic lateral sclerosis. Hum. Mut. 9; 356-358, 1997.
55. Kikugawa, K., Nakano, R., Inuzuka, T., Kokubo, Y., Narita, Y., Kuzuhara, S., Yoshida, S. and Tsuji, S.: A missense mutation in the SOD1 gene in patients with amyotrophic lateral sclerosis from Ku Peninsula and its vicinity, Japan. Neurogenetics 1; 113-115, 1997.
56. Kokubo, Y., Kuzuhara, S., Narita, Y., Kikugawa, K., Nakano, R., Inuzuka, T., Tsuji, S., Watanabe, M., Miyazaki, T., Murayama, S. and Ihara, Y.: An autopsy case of familial amyotrophic lateral sclerosis with SOD1 I113T mutation and argyrophilic inclusions (Abstract). Neuropathology 18 (Suppl.); 278, 1998.
57. Korstrzewa, M., Burck-Lehmann, U. and Müller, U.: Autosomal dominant amyotrophic lateral sclreosis: a novel mutation in the Cu/Zn superoxide dismutase-1 gene. Hum. Mol. Genet. 3; 2261-2262, 1994.
58. Kurahashi, K., Takagi, Y. and Maeda, T.: Familial ALS associated with Asn86-Ser (exon 4) mutation in SOD1: on diversity of intra-familial clinical manifestations (Abstract). The 5th International Symposium on ALS/MND, Amsterdam, 1994.
59. Ledesma, M. D., Bonay, P. and Avila, J.: r protein from Alzheimer's disease patients is glycated at its tubulin-binding domain. J. Neurochem. 65; 1658-1664, 1995.
60. Levanon, D., Lieman-Hurwitz, J., Dafni, N., Wigderson, M., Sherman, L. Bernstein, Y., Laver-Rudich, Z., Dancigar, E., Stein, O. and Groner, Y.: Architecture and anatomy of the chromosomal locus in human chromosome 21 encoding the Cu/Zn superoxide dismutase. EMBO J. 4; 77-84, 1985.
61. Lin, C. -L. G., Bristol, L. A., Jin, L., Dykes-Hoberg, M., Crawford, T., Clawson, L. and Rothstein, J. D.: Aberrant RNA processing in a neurodegenerative disease: the cause for absent EAAT2, a glutamate transporter, in amyotrophic lateral sclerosis. Neuron 20; 589-602, 1998.
62. Morita, M., Aoki, M., Abe, K., Hasegawa, T., Sakura, R., Onodera, Y., Ichikawa, N., Nishizawa, M. and Itoyama, Y.: A novel two-base mutation in the Cu/Zn superoxide dismutase gene associated with familial amyotrophic lateral sclerosis. Neurosci. Lett. 205; 79-82, 1996.
63. Morrison, B. M., Janssen, W. G., Gordon, J. W. and Morrison, J. H.: Time course of neuropathology in the spinal cord of G86R superoxide dismutase transgenic mice. J. Comp. Neurol. 391; 64-77, 1998.
64. Moulard, B., Camu, W. and Brice, A.: A previously undescribed mutation in the SOD1 gene in a French family with atypical ALS (Abstract). The 6th International Symposium on ALS/MND, Dublin, 1995.
65. Mourelatos, Z., Gonatas, N. K., Stieber, A., Gurney, M. E. and Dal Canto, M. C.: 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. 93; 5472-5477, 1996.
66. Murayama, S., Namba, E., Nishiyama, K., Kitamura, Y., Morita, T., Nakashima, K., Ishida, T., Mizutani, T. and Kanazawa, I.: Molecular pathological studies of familial amyotrophic lateral sclerosis. Neuropathology 17 (Suppl.); 219, 1997.
67. ε-(carboxymethyl)lysine formation from Amadori product. Biochem. Biophys. Res. Commun. 234; 167-172, 1997.
68. Nakamura, K., Hasegawa, T., Fukunaga, Y. and Ienaga, K.: Crosslines A and B as candidates for the fluorophores in age-and diabetes-related cross-linked proteins, and their diacetates produced by Maillard reaction of α-N-acetyl-L-lysine with D-glucose. J. Chem. Soc. Chem. Commun. 14; 992-994, 1992.
69. Nakano, R., Sato, S., Inuzuka, T., Sakimura, K., Mishina, M., Takahashi, H., Ikuta, F., Honma, Y., Fujii, J., Taniguchi, N. and Tsuji, S.: A novel mutation in Cu/Zn superoxide dismutase gene in Japanese familial amyotrophic lateral sclerosis. Biochem. Biophys. Res. Commun. 200; 695-703, 1994.
70. Nakashima, K., Watanabe, Y., Kuno, N., Nanba, E. and Takahashi, K.: Abnormality of Cu/Zn superoxide dismutase (SOD1) activity in Japanese familial amyotrophic lateral scleosis with two base pair deletion in the SOD1 gene. Neurology 45; 1019-1020, 1995.
71. Nishida, C. R., Gralla, E. B. and Valentine, J. S.: Characterization of three yeast copper-zinc superoxide dismutase mutants analogous to those coded for in familial amyotrophic lateral sclerosis Proc. Natl. Acad. Sci. USA 91; 9906-9910, 1994.
72. Ogasawara, M., Matsubara, Y., Narisawa, K., Aoki, M., Nakamura, S., Itoyama, Y. and Abe, K.: Mild ALS in Japan associated with novel SOD mutation. Nat. Genet 5; 323-324, 1993.
73. Ookawara, T., Kawamura, N., Kitagawa, Y. and Taniguchi, N.: Site-specific and random fragmentation of Cu,Zn-superoxide dismutase by glycation reaction. J. Biol. Chem. 267; 18505-18510, 1992.
74. Orrell, R., De Belleroche, J., Marklund, S., Bowe, F. and Hallewell, R.: A novel SOD mutant and ALS. Nature 374; 504-505, 1995.
75. Orrell, R. W., Habgood, J., Rudge, P., Lane, R. J. M. and De Belleroche, J. S.: Difficulties in distinguishing sporadic from familial amyotrophic lateral sclreosis. Ann. Neurol. 39; 810-812, 1996.
76. Orrell, R. W., King, A. W., Hilton, D. A., Campbell, M. J., Lane, R. J. M. and De Belleroche, J. S.: Familial amyotrophic lateral sclerosis with a point mutation of SOD-1: intrafamilial heterogeneity of disease duration associated with neurofibrillary tangles. J. Neurol. Neurosurg. Psychiat. 59; 266-270, 1995.
77. Orrell, R. W., Habgood, J. J., Gardiner, I., King, A. W., Bowe, F. A., Hallewell, R. A., Marklund, S. L., Greenwood, J., Lane, R. J. M. and De Belleroche, J.: Clinical and functional investigation of 10 misserise 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.
78. Phillips, J. P., Tainer, J. A., Getzoff, E. D., Boulianne, G. L., Kirby, K. and Hilliker, A. J.: Sub unit-destabilizing mutations in Drosophila copper/zinc superoxide dismutase: neuropathology and a model of dimer dysequilibrium. Proc. Natl. Acad. Sci. USA 92; 8574-8578, 1995.
79. Pramatarova, A., Goto, J., Nanba, E., Nakashima, K., Takahashi, K., Takagi, A., Kanazawa, I., Figlewicz, D. A. and Rouleau, G. A.: A two basepair deletion in the SOD1 gene causes familial amyotrophic lateral sclerosis. Hum. Mol. Genet. 3; 2061-2062, 1994.
80. Pramatarova, A., Figlewicz, D. A., Krizus, A., Han, F. Y., Ceballos-Picot, I., Nicole, A., Dib, M., Meininger, V., Brown, R. H. and Rouleau, G. A.: Identification of new mutations in the Cu/Zn superoxide dismutase gene of patients with familial amyotrophic lateral sclerosis. Am. J. Hum. Genet. 56; 592-596, 1995.
81. Rabizadeh, S., Gralla, E. B., Borchelt, D. R., Gwinn, R., Valentine, J. S., Sisodia, S., Wong, P., Lee, M., Hahn, H. and Bredesen, D. E.: Mutations associated with amyotrophic lateral sclerosis convert superoxide dismutase from an antiapoptotic gene to a proapoptotic gene: studies in yeast and neural cells. Proc. Natl. Acad. Sci. USA 92; 3024-3028, 1995.
82. Rainero, I., Pinessi, L., Tsuda, T., Vignocchi, M. G., Vaula, G., Calvi, L., Cerrato, P., Rossi, B., Bergamini, L., McLachlan, D. R. C. and St. George-Hyslop, P. H.: SOD1 missense mutation in an Italian family with ALS. Neurology 44; 347-349, 1994.
83. Reaume, A. G., Elliott, J. L., Hoffman, E. K., Kowall, N. W., Ferrante, R. J., Siwek, D. F., Wicox, H. M., Flood, D. G., Beal, M. F., Brown Jr, R. H., Scott, R. W. and Snider, W. D.: Motor neurons in Cu/Zn superoxide dismutase-deficient mice develop normally but exhibit enhanced cell death after axonal injury. Nat. Genet. 13; 43-47, 1996.
84. Rechsteiner, M.: Ubiquitin-mediated pathways for intracellular proteolysis. Annu. Rev. Cell. Biol. 3; 1-30, 1987.
85. Ripps, M. E., Huntley, G. W., Hof, P. R., Morrison, J. H. and Gordon, J. W.: 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.
86. Robberecht, W., Aguirre, T., Van Den Bosch, L., Tilkin, P., Cassiman, J. J. and Matthijs, G.: D90A heterozygosity in the SOD1 gene is associated with familial and apparently sporadic amyotrophic lateral sclerosis. Neurology 47; 1336-1339, 1996.
87. Rosen, D. R., Siddique, T., Patterson, D., Figlewicz, D. A., Sapp, P., Hentati, A., Donaldson, D., Goto, J., O'Regan, J. P., Deng, H. -X., Rahmani, Z., Krizus, A., McKennaYasek, D., Cayabyab, A., Gaston, S. M., Berger, R., Tanzi, R. E., Halperin, J. J., Herzfeldt, B., Van Den Bergh, R., Hung, W. -Y., Bird, T., Deng, G., Mulder, D. W., Smyth, C., Laing, N. G., Soriano, E., Pericak-Vance, M. A., Haines, J., Rouleau, G. A., Gusella, J. S., Horvitz, H. R. and Brown Jr, R. H.: Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature 362; 59-62, 1993.
88. Rouleau, G. A., Clark, A. W., Rooke, K., Pramatarova, A., Krizus, A., Suchowersky, O., Julien, J. -P. and Figlewicz, D.: SOD1 mutation is associated with accumulation of neurofilaments in amyotrophic lateral sclerosis. Ann. Neurol. 39; 128-131, 1996.
89. Saida, K., Ooi, N., Nabeshima, K, Asada, Y., Kumamoto, K. and Matsukura, S.: An autopsy case of familial amyotrophic lateral sclerosis with Cu/Zn superoxide dismutase H46R mutation (Abstract). The 39th Annual Meeting of Japanese Neurolological Association, Kyoto, 1998.
90. Sapp, P. C., Rosen, D. R., Hosler, B. A., Esteban, J., McKenna-Yasek, D., O'Regan, J. P., Horvitz, H. R. and Brown Jr, R. H.: Identification of three novel mutations in the gene for Cu/Zn superoxide dismutase in patients with familial amyotrophic lateral sclerosis. Neuromusc. Disord. 5; 353-357, 1995.
91. Sell, D. R. and Monnier, V. M.: Structure elucidation of a senescence cross-link from human extracellular matrix. J. Biol. Chem. 264; 21597-21602, 1989.
92. Shaw, C. E., Enayat, Z. E., Chioza, B. A., Al-Chalabi, A., Radunovic, A., Powell, J. F. and Leigh, P. N.: Mutations in all five exons of SOD-1 may cause ALS. Ann. Neurol. 43; 390-394, 1998.
93. Shibata, N. and Kobayashi, M.: Familial amyotrophic lateral sclerosis and Cu/Zn superoxide dismutase mutation. Neuropathology 17; 255-262, 1997.
94. Shibata, N., Hirano, A., Kobayashi, M., Asayama, K., Umahara, T., Komori, T. and Ikemoto, A.: Immunohistochemical demonstration of Cu/Zn superoxide dismutase in the spinal cord of patients with familial amyotrophic lateral sclerosis. Acta Histochem. Cytochem. 26; 619-622, 1993.
95. Shibata, N., Hirano, A., Kobayashi, M., Siddique, T., Deng, H. -X., Hung, W. -Y., Kato, T. and Asayama, K.: 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.
96. Shibata, N., Hirano, A., Kobayashi, M., Dal Canto, M. C., Gurney, M. E., Komori, T., Umahara, T. and Asayama, K.: Presence of Cu/Zn superoxide dismutase (SOD) immunoreactivity in neuronal hyaline inclusions in spinal cords from mice carrying a transgene for Gly93Ala mutant human Cu/Zn SOD. Acta Neuropathol. 95; 136-142, 1998.
97. Shibata, N., Hirano, A., Kato, S., Nagai, R., Horiuchi, S., Komori, T., Umahara, T., Asayama, K. and Kobayashi, M.: Advanced glycation endproducts are deposited in neuronal hyalin inclusions: a study on familial amyotrophic lateral sclerosis with superoxide dismutase-1 mutation. Acta Neuropathol. 97; 240-246, 1999.
98. Siddique, T., Nijhawan, D. and Hentati, A.: Familial amyotrophic lateral sclerosis. J. Neural Transm. 49 (Suppl.); 219-233, 1997.
99. Själander, A. Beckman, G., Deng, H. -X., Iqbal, Z., Tainer, J. A. and Siddique, T.: The D90A mutation results in a polymorphism of Cu,Zn superoxide dismutase that is prevalent in nothern Sweden and Finland. Hum. Mol. Genet. 4; 1105-1108, 1995.
100. Smith, M. A., Taneda, S., Richey, P. L., Miyata, S., Yan, S. D., Stern, D., Sayre, L. M., Monnier, V. M. and Perry, G.: Advanced glycation end products are associated with Alzheimer disease pathology. Proc. Natl. Acad. Sci. USA 91; 5710-5714, 1994.
101. Sternberger, L. A. and Sternberger, N. H.: Monoclonal antibodies distinguish phosphorylated and nonphosphorylated forms of neurofilamerits in situ. Proc. Natl. Acad. Sci. USA 80; 3101-3105, 1983.
102. Tainer, J. A., Getzoff, E. D., Beem, K. M., Richardson, J. S. and Richardson, D. C.: Determination and analysis of the 2 Å structure of copper, zinc superoxide dismutase. J. Mol. Biol. 160; 181-217, 1982.
103. Takahashi, H.: Familial amyotrophic lateral sclerosis with or without mutation of the Cu/Zn superoxide dismutase gene. Brain Nerve 47; 535-541, 1995.
104. Takahashi, H., Makifuchi, T., Nakano, R., Sato, S., Inuzuka, T., Sakimura, K., Mishina, M., Honma, Y., Tsuji, S. and Ikuta, F.: Familial amyotrophic lateral sclerosis with a mutation in the Cu/Zn superoxide dismutase gene. Acta Neuropathol. 88; 185-188, 1994.
105. Takeda, A., Yasuda, T., Miyata, T., Goto, Y., Wakai, M., Watanabe, M., Yasuda, Y., Horie, K., Inagaki, T., Doyu, M., Maeda, K. and Sobue, G.: Advanced glycation end products co-localized with astrocytes and microglial cells in Alzheimer's disease brain. Acta Neuropathol. 95; 555-558, 1998.
106. Takizawa, N., Takada, K. and Ohkawa, K.: Inhibitory effect of nonenzymatic glycosylation on ubiquitination and ubiquitin-mediated degradation of lysozyme. Biochem. Biophys. Res. Commun. 192; 700-706, 1993.
107. Trotti, D., Rossi, D., Gjesdal, O., Levy, L. M., Racagni, G., Danbolt, N. C. and Volterra, A.: Peroxynitrite inhibits glutamate transporter subtypes. J. Biol. Chem. 271; 5976-5979, 1996.
108. Vitek, M. P., Bhattacharya, K., Glendening, J. M., Stopa, E., Vlassara, H., Bucala, R., Manogue, K. and Cerami, A.: Advanced glycation end products contribute to amyoloidosis in Alzheimer disease. Proc. Natl. Acad. Sci. USA 91; 4766-4770, 1994.
109. Vlassara, H., Bucala, R. and Striker, L.: Pathogenic effects of advanced glycosylation: biochemical, biologic, and clinical implications for diabetes and aging. Lab. Invest. 70; 138-151, 1994.
110. Volterra, A., Trotti, D., Tromba, C., Floridi, S. and Racagni, G.: Glutamate uptake inhibition by oxygen free radicals in rat cortical astrocytes. J. Neurosci. 14; 2924-2932, 1994.
111. Watanabe, M., Aoki, M., Abe, K., Shoji, M., Iizuka, T., Ikeda, Y., Hirai, S., Kurokawa, K., Kato, T., Sasaki, H. and Itoyama, Y.: A novel missense point mutation (S134N) of the Cu/Zn superoxide dismutase gene in a patient with familial motor neuron disease. Hum. Mut. 9; 69-71, 1997.
112. Wiedau-Pazos, M., Goto, J. J., Rabizadeh, S., Gralla, E. B., Roe, J. A., Lee, M. K., Valentine, J. S. and Bredesen, D. E.: Altered reactivity of superoxide dismutase in familial amyotrophic lateral sclerosis. Science 271; 515-518, 1996.
113. 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.: 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.
114. Yan, S. -D., Chen, X., Schmidt, A. -M., Brett, J., Godman, G., Zou, Y. -S., Scott, C. W., Caputo, C., Frappier, T., Smith, M. A., Perry, G., Yen, S. -H. and Stern, D.: Glycated tau protein in Alzheimer disease: a mechanism for induction of oxidant stress. Proc. Natl. Acad. Sci. USA 91; 7787-7791, 1994.
115. Yan, S. D., Zhu, H., Fu, J., Yan, S. F., Roher, A., Tourtellotte, W. W., Rajavashisth, T., Chen, X., Godman, G. C., Stern, D. and Schmidt, A. M.: Amyloid-β peptide - receptor for advanced glycation endproduct stimulating factor: a proinflammatory pathway in Alzheimer disease. Proc. Natl. Acad. Sci. USA 94; 5296-5301, 1997.
116. m for hydrogen peroxide. Proc. Natl. Acad. Sci. USA 93; 5709-5714, 1996.
117. Yulug, I. G., Katsanis, N., De Belleroche, J., Collinge, J. and Fisher, E. M. C.: An improved protocol for the analysis of SOD1 gene mutations, and a new mutation in exon 4. Hum. Mol. Genet. 4; 1101-1104, 1995.