Features of wild-type human SOD1 limit interactions with misfolded aggregates of mouse G86R Sod1

Molecular Neurodegeneration

Volumn 8, Issue 1, 2013, Pages

  Qualls, David A ^a   Prudencio, Mercedes ^a,b   Roberts, Brittany Lt ^a   Crosby, Keith ^a   Brown, Hilda ^a   Borchelt, David R ^a  

^a UNIVERSITY OF FLORIDA COLLEGE OF MEDICINE   (United States)

^b MAYO GRADUATE SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

COPPER ZINC SUPEROXIDE DISMUTASE; GREEN FLUORESCENT PROTEIN; RED FLUORESCENT PROTEIN; SAPONIN;

ANIMAL CELL; ARTICLE; CELL CULTURE; CELL INCLUSION; CHO CELL; CONTROLLED STUDY; FLUORESCENCE; GENETIC TRANSFECTION; HUMAN; HUMAN CELL; LUCIFERASE ASSAY; MOUSE; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN AGGREGATION; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; TRANSIENT TRANSFECTION; WILD TYPE;

MUS;

AMYOTROPHIC LATERAL SCLEROSIS; ANIMALS; DISEASE MODELS, ANIMAL; HUMANS; MICE; PROTEIN FOLDING; SUPEROXIDE DISMUTASE; TRANSFECTION;

EID: 84890287837     PISSN: None     EISSN: 17501326     Source Type: Journal    
DOI: 10.1186/1750-1326-8-46     Document Type: Article

References (32)

1. Superoxide dismutases. Fridovich I, Adv Enzymol Relat Areas Mol Biol 1974 41 35 97 4371571
2. Atomic structures of wild- type and thermostable mutant recombinant human Cu, Zn superoxide dismutase. Parge HE, Hallewell RA, Tainer JA, Proc Natl Acad Sci USA 1992 89 6109 6113 10.1073/pnas.89.13.6109 1463506
3. Unusual trigonal-planar copper configuration revealed in the atomic structure of yeast copper-zinc superoxide dismutase. Ogihara NL, Parge HE, Hart PJ, Weiss MS, Goto JJ, Crane BR, Tsang J, Slater K, Roe JA, Valentine JS, et al. Biochemistry 1996 35 2316 2321 10.1021/bi951930b 8652572 (Pubitemid 26071664)
4. Unraveling the mechanisms involved in motor neuron degeneration in ALS. Bruijn LI, Miller TM, Cleveland DW, Annu Rev Neurosci 2004 27 723 749 10.1146/annurev.neuro.27.070203.144244 15217349 (Pubitemid 39050419)
5. Variation in aggregation propensities among ALS-associated variants of SOD1: correlation to human disease. Prudencio M, Hart PJ, Borchelt DR, Andersen PM, Hum Mol Genet 2009 18 3217 3226 10.1093/hmg/ddp260 19483195
6. Motor neuron degeneration in mice that express a human Cu, Zn superoxide dismutase mutation. Gurney ME, Pu H, Chiu AY, Dal Canto MC, Polchow CY, Alexander DD, Caliendo J, Hentati A, Kwon YW, Deng H-X, et al. Science 1994 264 1772 1775 10.1126/science.8209258 8209258 (Pubitemid 24227760)
7. Conversion to the amyotrophic lateral sclerosis phenotype is associated with intermolecular linked insoluble aggregates of SOD1 in mitochondria. Deng HX, Shi Y, Furukawa Y, Zhai H, Fu R, Liu E, Gorrie GH, Khan MS, Hung WY, Bigio EH, et al. Proc Natl Acad Sci U S A 2006 103 7142 7147 10.1073/pnas.0602046103 16636275
8. Molecular dissection of ALS-associated toxicity of SOD1 in transgenic mice using an exon-fusion approach. Deng HX, Jiang H, Fu R, Zhai H, Shi Y, Liu E, Hirano M, Dal Canto MC, Siddique T, Hum Mol Genet 2008 17 2310 2319 10.1093/hmg/ddn131 18424447
9. Neuron-specific expression of mutant superoxide dismutase is sufficient to induce amyotrophic lateral sclerosis in transgenic mice. Jaarsma D, Teuling E, Haasdijk ED, De Zeeuw CI, Hoogenraad CC, J Neurosci 2008 28 2075 2088 10.1523/JNEUROSCI.5258-07.2008 18305242 (Pubitemid 351317636)
10. Wild-type SOD1 overexpression accelerates disease onset of a G85R SOD1 mouse. Wang L, Deng HX, Grisotti G, Zhai H, Siddique T, Roos RP, Hum Mol Genet 2009 18 1642 1651 10.1093/hmg/ddp085 19233858
11. An examination of wild-type SOD1 in modulating the toxicity and aggregation of ALS-associated mutant SOD1. Prudencio M, Durazo A, Whitelegge JP, Borchelt DR, Hum Mol Genet 2010 19 4774 4789 10.1093/hmg/ddq408 20871097
12. Aggregation and motor neuron toxicity of an ALS-linked SOD1 mutant independent from wild-type SOD1. Bruijn LI, Houseweart MK, Kato S, Anderson KL, Anderson SD, Ohama E, Reaume AG, Scott RW, Cleveland DW, Science 1998 281 1851 1854 9743498 (Pubitemid 28450505)
13. Wild-type human SOD1 overexpression does not accelerate motor neuron disease in mice expressing murine Sod1 G86R. Audet JN, Gowing G, Julien JP, Neurobiol Dis 2010 40 245 250 10.1016/j.nbd.2010.05.031 20573565
14. 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, Proc Natl Acad Sci USA 1995 92 689 693 10.1073/pnas.92.3.689 7846037
15. Superoxide dismutase 1 encoding mutations linked to ALS adopts a spectrum of misfolded states. Prudencio M, Borchelt DR, Mol Neurodegener 2011 6 77 10.1186/1750-1326-6-77 22094223
16. pEF-BOS, a powerful mammalian expression vector. Mizushima S, Nagata S, Nucleic Acids Res 1990 18 5322 10.1093/nar/18.17.5322 1698283 (Pubitemid 20270119)
17. Copper-binding-site-null SOD1 causes ALS in transgenic mice: aggregates of non-native SOD1 delineate a common feature. Wang J, Slunt H, Gonzales V, Fromholt D, Coonfield M, Copeland NG, Jenkins NA, Borchelt DR, Hum Mol Genet 2003 12 2753 2764 10.1093/hmg/ddg312 12966034 (Pubitemid 37407112)
18. Role of mutant SOD1 disulfide oxidation and aggregation in the pathogenesis of familial ALS. Karch CM, Prudencio M, Winkler DD, Hart PJ, Borchelt DR, Proc Natl Acad Sci U S A 2009 106 7774 7779 10.1073/pnas.0902505106 19416874
19. Modulation of mutant superoxide dismutase 1 aggregation by co-expression of wild-type enzyme. Prudencio M, Durazo A, Whitelegge JP, Borchelt DR, J Neurochem 2009 108 1009 1018 10.1111/j.1471-4159.2008.05839.x 19077113
20. A limited role for disulfide cross-linking in the aggregation of mutant SOD1 linked to familial amyotrophic lateral sclerosis. Karch CM, Borchelt DR, J Biol Chem 2008 283 13528 13537 10.1074/jbc.M800564200 18316367
21. Modification of superoxide dismutase 1 (SOD1) properties by a GFP tag - implications for research into amyotrophic lateral sclerosis (ALS). Stevens JC, Chia R, Hendriks WT, Bros-Facer V, Van MJ, Martin JE, Jackson GS, Greensmith L, Schiavo G, Fisher EM, PLoS ONE 2010 5 9541 10.1371/journal.pone.0009541 20221404
22. The biological action of saponins in animal systems: a review. Francis G, Kerem Z, Makkar HP, Becker K, Br J Nutr 2002 88 587 605 10.1079/BJN2002725 12493081 (Pubitemid 36082888)
23. An analysis of interactions between fluorescently-tagged mutant and wild-type SOD1 in intracellular inclusions. Qualls DA, Crosby K, Brown H, Borchelt DR, PLoS One in press
24. An immunological epitope selective for pathological monomer-misfolded SOD1 in ALS. Rakhit R, Robertson J, Vande VC, Horne P, Ruth DM, Griffin J, Cleveland DW, Cashman NR, Chakrabartty A, Nat Med 2007 13 754 759 10.1038/nm1559 17486090 (Pubitemid 46889748)
25. A spectroscopic characterization of a monomeric analog of copper, zinc superoxide dismutase. Bertini I, Piccioli M, Viezzoli MS, Chiu CY, Mullenbach GT, Eur Biophys J 1994 23 167 176 10.1007/BF01007608 7956977 (Pubitemid 24275234)
26. Solution structure of reduced monomeric Q133M2 copper, zinc superoxide dismutase (SOD). Why is SOD a dimeric enzyme? Banci L, Benedetto M, Bertini I, Del Conte R, Piccioli M, Viezzoli MS, Biochemistry 1998 37 11780 11791 10.1021/bi9803473 9718300 (Pubitemid 28400049)
27. Split Gaussia luciferase-based bioluminescence template for tracing protein dynamics in living cells. Kim SB, Sato M, Tao H, Anal Chem 2009 81 67 74 10.1021/ac801658y 19061336
28. Monomeric Cu, Zn-superoxide dismutase is a common misfolding intermediate in the oxidation models of sporadic and familial amyotrophic lateral sclerosis. Rakhit R, Crow JP, Lepock JR, Kondejewski LH, Cashman NR, Chakrabartty A, J Biol Chem 2004 279 15499 15504 10.1074/jbc.M313295200 14734542 (Pubitemid 38618950)
29. FALS mutations in Cu, Zn superoxide dismutase destabilize the dimer and increase dimer dissociation propensity: a large-scale thermodynamic analysis. Khare SD, Caplow M, Dokholyan NV, Amyloid 2006 13 226 235 10.1080/ 13506120600960486 17107883 (Pubitemid 44764462)
30. Metal-free ALS variants of dimeric human Cu, Zn-superoxide dismutase have enhanced populations of monomeric species. Svensson AK, Bilsel O, Kayatekin C, Adefusika JA, Zitzewitz JA, Matthews CR, PLoS ONE 2010 5 10064 10.1371/journal.pone.0010064 20404910
31. Strategies for stabilizing superoxide dismutase (SOD1), the protein destabilized in the most common form of familial amyotrophic lateral sclerosis. Auclair JR, Boggio KJ, Petsko GA, Ringe D, Agar JN, Proc Natl Acad Sci U S A 2010 107 21394 21399 10.1073/pnas.1015463107 21098299
32. An intersubunit disulfide bond prevents in vitro aggregation of a superoxide dismutase-1 mutant linked to familial amytrophic lateral sclerosis. Ray SS, Nowak RJ, Strokovich K, Brown RH Jr, Walz T, Lansbury PT Jr, Biochemistry 2004 43 4899 4905 10.1021/bi030246r 15109247 (Pubitemid 38544443)