Cu/Zn superoxide dismutase can form pore-like structures

Biochemical and Biophysical Research Communications

Volumn 312, Issue 4, 2003, Pages 873-876

  Chung, Jinhyuk ^a   Yang, Hoichang ^a   De Beus, Mitchel D ^a   Ryu, Chang Y ^a   Cho, Kilwon ^b   Colón, Wilfredo ^a  

^a Rensselaer Polytechnic Institute   (United States)

^b Pohang University of Science and Technology (POSTECH)   (South Korea)

Author keywords

Aggregation; Amyloid; Amyotrophic lateral sclerosis; Channel; FALS; Neurodegeneration; Oxidative damage; Pore; SOD

Indexed keywords

COPPER; COPPER ZINC SUPEROXIDE DISMUTASE; MUTANT PROTEIN; OLIGOMER;

AMYOTROPHIC LATERAL SCLEROSIS; ARTICLE; ATOMIC FORCE MICROSCOPY; CHANNEL GATING; DEGENERATIVE DISEASE; FAMILIAL DISEASE; MOLECULAR DYNAMICS; MOTONEURON; NONHUMAN; OXIDATION; PATHOGENESIS; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ASSEMBLY; WILD TYPE;

EID: 0344495441     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2003.11.008     Document Type: Article

References (21)

1. Rosen D.R., Siddique T., Patterson D., Figlewicz D.A., Sapp P., Hentati A., Donaldson D., Goto J., More M. Mutations in Cu, Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature. 362:1993;59-62.
2. Andersen P.M., Sims K.B., Xin W.W., Kiely R., O'Neill G., Ravits J., Pioro E., Harati Y., Brower R.D., Levine J.S., Heinicke H.U., Seltzer W., Boss M., Brown R.H. Jr. Sixteen novel mutations in the Cu/Zn superoxide dismutase gene in amyotrophic lateral sclerosis: a decade of discoveries, defects and disputes. ALS and other motor neuron disorders. 4:2003;62-67.
3. Cleveland D.W., Rothstein J.D. From Charcot to Lou Gehrig: deciphering selective motor neuron death in ALS and other motor neuron disorders. Nat. Rev. Neurosci. 2:2001;806-819.
4. Kaytor M.D., Warren S.T. Aberrant protein deposition and neurological disease. J. Biol. Chem. 274:1999;37507-37510.
5. Bucciantini M., Giannoni E., Chiti F., Baroni F., Formigli L., Zurdo J., Taddei N., Ramponi G., Dobson C.M., Stefani M. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature. 416:2002;507-511.
6. Caughey B., Lansbury P.T.J. Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu. Rev. Neurosci. 26:2003;267-298.
7. Lashuel H.A., Hartley D., Petre B.M., Walz T., Lansbury P.T. Jr. Neurodegenerative disease: amyloid pores from pathogenic mutations. Nature. 418:2002;291.
8. Kagan B.L., Hirakura Y., Azimov R., Azimova R., Lin M.C. The channel hypothesis of Alzheimer's disease: current status. Peptides. 23:2002;1311-1315.
9. Crow J.P., Sampson J.B., Zhuang Y., Thompson J.A., Beckman J.S. Decreased zinc affinity of amyotrophic lateral sclerosis-associated superoxide dismutase mutants leads to enhanced catalysis of tyrosine nitration by peroxynitrite. J. Neurochem. 69:1997;1936-1944.
10. Hayward L.J., Rodriguez J.A., Kim J.W., Tiwari A., Goto J.J., Cabelli D.E., Valentine J.S., Brown R.H. Jr. Decreased metallation and activity in subsets of mutant superoxide dismutases associated with familial amyotrophic lateral sclerosis. J. Biol. Chem. 277:2002;15923-15931.
11. Sutter B., Bounds P.L., Koppenol W.H. The preparation of apo-Cu,Zn superoxide dismutase by ion-exchange chromatography on iminodiacetic acid-Sepharose. Protein Expr. Purif. 19:2000;53-56.
12. Andrus P.K., Fleck T.J., Gurney M.E., Hall E.D. Protein oxidative damage in a transgenic mouse model of familial amyotrophic lateral sclerosis. J. Neurochem. 71:1998;2041-2048.
13. Kim S.Y., Kwon O.J., Park J.W. Inactivation of catalase and superoxide dismutase by singlet oxygen derived from photoactivated dye. Biochimie. 83:2001;437-444.
14. Rakhit R., Cunningham P., Furtos-Matei A., Dahan S., Qi X.F., Crow J.P., Cashman N.R., Kondejewski L.H., Chakrabartty A. Oxidation-induced misfolding and aggregation of superoxide dismutase and its implications for amyotrophic lateral sclerosis. J. Biol. Chem. 277:2002;47551-47556.
15. 2. Free Radicals Biol. Med. 26:1999;905-918.
16. Lindberg M.J., Tibell L., Oliveberg M. Common denominator of Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis: decreased stability of the apo state. Proc. Natl. Acad. Sci. USA. 99:2002;16607-16612.
17. Okado-Matsumoto A., Fridovich I. Amyotrophic lateral sclerosis: a proposed mechanism. Proc. Natl. Acad. Sci. USA. 99:2002;9010-9014.
18. Juneja T., Pericak-Vance M.A., Laing N.G., Dave S., Siddique T. Prognosis in familial amyotrophic lateral sclerosis: progression and survival in patients with glu100gly and ala4val mutations in Cu, Zn superoxide dismutase. Neurology. 48:1997;55-57.
19. Jaarsma D., Haasdijk E.D., Grashorn J.A., Hawkins R., van Duijn W., Verspaget H.W., London J., Holstege J.C. Human Cu/Zn superoxide dismutase (SOD1) overexpression in mice causes mitochondrial vacuolization, axonal degeneration, and premature motoneuron death and accelerates motoneuron disease in mice expressing a familial amyotrophic lateral sclerosis mutant SOD1. Neurobiol. Dis. 7:2000;623-643.
20. Bendotti C., Calvaresi N., Chiveri L., Prelle A., Moggio M., Braga M., Silani V., De Biasi S. Early vacuolization and mitochondrial damage in motor neurons of FALS mice are not associated with apoptosis or with changes in cytochrome oxidase histochemical reactivity. J. Neurol. Sci. 191:2001;25-33.
21. Higgins C.M., Jung C., Xu Z. ALS-associated mutant SOD1G93A causes mitochondrial vacuolation by expansion of the intermembrane space and by involvement of SOD1 aggregation and peroxisomes. BMC Neurosci. 4:2003;16.