Normal binding and reactivity of copper in mutant superoxide dismutase isolated from amyotrophic lateral sclerosis patients

Journal of Neurochemistry

Volumn 69, Issue 2, 1997, Pages 675-681

  Marklund, Stefan L ^a,b   Andersen, Peter M ^a   Forsgren, Lars ^a   Nilsson, Peter ^a   Ohlsson, Per Ingvar ^a   Wikander, Göran ^b   Öberg, Agneta ^a  

^a UMEÅ UNIVERSITY HOSPITAL   (Sweden)

^b UMEÅ UNIVERSITY   (Sweden)

Author keywords

Amyotrophic lateral sclerosis; Copper; Hydroxyl radicals; Stability; Superoxide dismutase

Indexed keywords

COPPER; COPPER ZINC SUPEROXIDE DISMUTASE; HYDROXYL RADICAL;

AMYOTROPHIC LATERAL SCLEROSIS; ARTICLE; CLINICAL ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; HUMAN; HUMAN TISSUE; METAL BINDING; MUTANT; NERVE CELL DEGENERATION; PRIORITY JOURNAL;

EID: 0030749689     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1997.69020675.x     Document Type: Article

References (36)

1. 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. (1995) Amyotrophic lateral sclerosis associated with homozygosity for an Asp90Ala mutation in CuZn-superoxide dismutase. Nat. Genet. 10, 61-66.
2. 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. (1996) Autosomal recessive adult-onset ALS associated with homozygosity for Asp90Ala CuZn-superoxide dismutase mutation. Brain 119, 1153-1172.
3. Ausubel F. M., Brent R., Kingston R. E., Moore D. D., Seidman J. G., Smith J. A., and Struhl K., eds (1993) Current Protocols in Molecular Biology, Vol. 2. John Wiley, New York.
4. Barra D., Martini F., Bannister J. V., Schinina M. E., Rotilio G., Bannister W. H., and Bossa F. (1980) The complete amino acid sequence of human Cu/Zn superoxide dismutase. FEBS Lett. 120, 53-56.
5. Beckman J. S., Larson M., Smith C. E., and Koppenol W. H. (1993) ALS, SOD and peroxynitrite. Nature 364, 584.
6. Borchelt D. R., Lee M. D., Slunt H. S., Guarnieri M., Xu Z.-S., Wong P. C., Brown R. H., Price D. L., Sisodia S. S., and Cleveland D. W. (1994) Superoxide dismutase 1 with mutations linked to familial amyotrophic lateral sclerosis possesses significant activity. Proc. Natl. Acad. Sci. USA 91, 8292-8296.
7. 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. (1995) Superoxide dismutase 1 subunits with mutations linked to familial amyotrophic lateral sclerosis do not affect wild-type subunit function. J. Biol. Chem. 270, 3234-3238.
8. 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.
9. 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. (1993) Amyotrophic lateral sclerosis and structural defects in Cu,Zn superoxide dismutase. Science 261, 1047-1051.
10. Domigan N. M., Calder V. L., Broom J. K., George P. M., Donaldson I. M., and Winterbourn C. C. (1996) Superoxide dismutase (Glu100Gly) in a family with inherited motor neuron disease: detection of mutant superoxide dismutase activity and the purification of heterodimers. (Abstr.) Proceedings of the VIII Biennial Meeting International Society for Free Radical Research, Barcelona, Spain, pp. 43-44.
11. Fujii J., Myint T., Seo H. G., Kayanoki Y., Ikeda Y., and Taniguchi N. (1995) Characterization of wild-type and amyotrophic lateral sclerosis-related mutant Cu,Zn-superoxide dismutases overproduced in baculovirus-infected insect cells. J. Neurochem. 64, 1456-1461.
12. Gurney M. E., Pu H., Chiu A. Y., Dal Canto M. C., Polchow 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. (1994) Motor neuron degeneration in mice that express a human Cu,Zn superoxide dismutase mutation. Science 264, 1772-1775.
13. 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.
14. Haverkamp L. J., Appel V., and Appel S. H. (1995) Natural history of amyotrophic lateral sclerosis in a database population. Brain 118, 707-719.
15. Heikkila R. E., Cabbat F. S., and Cohen G. (1976) In vivo inhibition of superoxide dismutase in mice by diethyldithiocarbamate. J. Biol. Chem. 251, 2182-2185.
16. Hodgson E. K. and Fridovich I. (1975) The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: chemiluminescence and peroxidation. Biochemistry 14, 5299-5303.
17. Marklund S. L. (1976) A spectrophotometric study of the spontaneous disproportionation of the superoxide anion radical, and a sensitive direct assay for superoxide dismutase. J. Biol. Chem. 251, 7504-7507.
18. Marklund S. E. (1985) Direct assay of superoxide dismutase with potassium superoxide, in Handbook of Methods for Oxygen Radical Research (Greenwald R. A., ed), pp. 249-255. CRC Press, Boca Raton, Florida.
19. McCord J. M. and Fridovich I. (1969) Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J. Biol. Chem. 244, 6049-6055.
20. Ogasawara M., Matsubara Y., Narisawa K., Aoki M., Nakamura S., Itoyama Y., and Abe K. (1993) Mild ALS in Japan associated with novel SOD mutation. Nat. Genet. 5, 323-324.
21. 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. (1995) Identification of new mutations in the CuZn superoxide dismutase gene of patients with familial amyotrophic lateral sclerosis. Am. J. Hum. Genet. 56, 592-596.
22. Rabizadeh S., Gralla E. B., Borchelt D. R., Gwinn R., Valentine J. S., Sisodia S. S., Wong P., Lee M., Hahn H., and Bredesen D. E. (1995) Mutations associated with amyotrophic lateral sclerosis convert superoxide dismutase from an antiapopiotic gene to a proapoptotic gene. Studies in yeast and neural cells. Proc. Natl. Acad. Sci. USA 92, 3024-3028.
23. Radunovic A. and Leigh P. N. (1996) Cu/Zn superoxide dismutase gene mutations in ALS. Correlation between genotype and clinical features. J. Neurol. Neurosurg. Psychiatry 61, 565-572.
24. Reaume A. G., Elliott J. L., Hoffman E. K., Kowall N. W., Ferrante R. J., Siwek D. F., Wilcox H. M., Flood D. G., Beal M. F., Brown R. H., Scott R. W., and Snider W. D. (1996) Motor neurons in CuZn superoxide dismutase-deficient mice develop normally but exhibit enhanced cell death after axonal injury. Nat. Genet. 13, 43-47.
25. 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.
26. Robberecht W., Sapp P., Viaene M. K., Rosen D., McKenna-Yasek D., Haines J., Horvitz R., Theys P., and Brown R. Jr. (1994) CuZn superoxide dismutase activity in familial and sporadic amyotrophic lateral sclerosis. J. Neurochem. 62, 384-387.
27. Robberecht W., Aguirre T., Van Dėn Bosch L., Tilkin P., Cassiman R. N., and Matthijs G. (1996) D90A heterozygosity in the SOD1 gene is associated with familial and apparently sporadic amyotrophic lateral sclerosis. Neurology 47, 1336-1339.
28. 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., McKenna-Yasek 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 R. H. Jr. (1993) Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature 362, 59-62.
29. 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.
30. Tainer J. A., Getzoff E. D., Beem K. M., Richardson J. S., and Richardson D. L. (1982) Determination and analysis of the 2 Å structure of copper, zinc superoxide dismutase. J. Mol. Biol. 160, 181-217.
31. Tsuda T., Munthasser S., Fraser P. E., Percy M. E., Rainero I., Vaula G., Pinessi L., Bergamini L., Vignocchi G., McLachlan D. R. C., Tatton W. G., and St. George-Hyslop P. (1994) Analysis of the functional effects of a mutation in SOD1 associated with familial amyotrophic lateral sclerosis. Neuron 13, 727-736.
32. Wiedau-Pazos M., Goto J. J., Rabizadeh S., Gralla E. B., Roe J. A., Lee M. K., Valentine J. S., and Bredesen D. E. (1996) Altered reactivity of superoxide dismutase in familial amyotrophic lateral sclerosis. Science 271, 515-518.
33. 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 causes motor neuron disease characterised by vacuolar degeneration of mitochondria. Neuron 14, 1105-1116.
34. Yim M. B., Chock P. B., and Stadtman E. R. (1990) Copper, zinc superoxide dismutase catalyzes hydroxyl radical production from hydrogen peroxide. Proc. Natl. Acad. Sci. USA 87, 5006-5010.
35. Yim M. B., Chock P. B., and Stadtman E. R. (1993) Enzyme function of copper, zinc superoxide dismutase as a free radical generator. J. Biol. Chem. 268, 4099-4105.
36. m for hydrogen peroxide. Proc. Natl. Acad. Sci. USA 93, 5709-5714.