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Superoxide dismutase 1 with mutations linked to familial amyotrophic lateral sclerosis possesses significant activity.
Open accessAbstract
Familial amyotrophic lateral sclerosis (FALS) has been linked to mutations in the homodimeric enzyme Cu/Zn superoxide dismutase 1 (SOD1). Assay by transient expression in primate cells of six FALS mutant enzymes revealed a continuum of enzymatic activity bounded by the enzyme carrying the mutation Gly-85-->Arg, which was inactive, and mutant enzyme G37R carrying the Gly-37-->Arg change, which retained full specific activity but displayed a 2-fold reduction in polypeptide stability. The G37R mutant displayed similar properties in transformed lymphocytes from an individual heterozygous for the G37R and wild-type SOD1 genes; heterodimeric enzymes composed of mutant and wild-type subunits were detected, but there was no measurable diminution in the stability and activity of the wild-type subunits. Thus, for mutants such as G37R, either surprisingly modest losses in activity (involving only the mutant subunit) can yield motor neuron death, or alternatively, mutant SOD1 may acquire properties that injure motor neurons by one or more mechanisms unrelated to the metabolism of oxygen radicals.
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Cites
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961
Superoxide dismutase: Improved assays and an assay applicable to acrylamide gels
Beauchamp, C., & Fridovich, I. (1971) · Analytical Biochemistry · doi:10.1016/0003-2697(71)90370-8 · Cited by 12,892
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., et al. (1993) · Nature · doi:10.1038/362059a0 · Cited by 7,062
Self-citationKozak, M. (1986) · Cell · doi:10.1016/0092-8674(86)90762-2 · Cited by 4,741
Cited by
Motor Neuron Degeneration in Mice that Express a Human Cu,Zn Superoxide Dismutase Mutation
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., et al. (1994) · Science · doi:10.1126/science.8209258 · Cited by 4,143
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., et al. (1997) · Neuron · doi:10.1016/s0896-6273(00)80272-x · Cited by 1,341
Self-citationUNRAVELING THE MECHANISMS INVOLVED IN MOTOR NEURON DEGENERATION IN ALS
Bruijn, L. I., Miller, T. M., & Cleveland, D. W. (2004) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.27.070203.144244 · Cited by 1,185
Self-citationSuperoxide dismutases and superoxide reductases
Sheng, Y., Abreu, I. A., Cabelli, D. E., Maroney, M. J., Miller, A.-F., Teixeira, M., & Valentine, J. S. (2014) · Chemical Reviews · doi:10.1021/cr4005296 · Cited by 1,081
Lebovitz, R. M., Zhang, H., Vogel, H., Cartwright, J., Dionne, L., Lu, N., Huang, S., & Matzuk, M. M. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.18.9782 · Cited by 1,023
Mitochondrial Dysfunction in Neurodegenerative Diseases
Johri, A., & Beal, M. F. (2012) · The Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.112.192138 · Cited by 806
Antisense oligonucleotide therapy for neurodegenerative disease
Smith, R. A. (2006) · Journal of Clinical Investigation · doi:10.1172/jci25424 · Cited by 506
Pramatarova, A., Laganière, J., Roussel, J., Brisebois, K., & Rouleau, G. A. (2001) · The Journal of Neuroscience · doi:10.1523/jneurosci.21-10-03369.2001 · Cited by 482
ALS Genetics: Gains, Losses, and Implications for Future Therapies
Kim, G., Gautier, O., Tassoni-Tsuchida, E., Ma, X. R., & Gitler, A. D. (2020) · Neuron · doi:10.1016/j.neuron.2020.08.022 · Cited by 370
Microglia in ALS: The Good, The Bad, and The Resting
Henkel, J. S., Beers, D. R., Zhao, W., & Appel, S. H. (2009) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-009-9171-5 · Cited by 353
Extracellular mutant SOD1 induces microglial‐mediated motoneuron injury
Zhao, W., Beers, D. R., Henkel, J. S., Zhang, W., Urushitani, M., Julien, J., & Appel, S. H. (2010) · Glia · doi:10.1002/glia.20919 · Cited by 288
Jankowsky, J. L., Slunt, H. H., Gonzales, V., Savonenko, A. V., Wen, J. C., Jenkins, N. A., Copeland, N. G., Younkin, L. H., Lester, H. A., Younkin, S. G., et al. (2005) · PLoS Medicine · doi:10.1371/journal.pmed.0020355 · Cited by 237
Self-citationInce (1998) · doi:10.1046/j.1365-2990.1998.00108.x · Cited by 224
Aggregation of Copper–Zinc Superoxide Dismutase in Familial and Sporadic ALS
Chattopadhyay, M., & Valentine, J. S. (2009) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2536 · Cited by 163
Rodent Aβ Modulates the Solubility and Distribution of Amyloid Deposits in Transgenic Mice
Jankowsky, J. L., Younkin, L. H., Gonzales, V., Fadale, D. J., Slunt, H. H., Lester, H. A., Younkin, S. G., & Borchelt, D. R. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m611050200 · Cited by 122
Self-citationApolloni, S., Amadio, S., Montilli, C., Volonte, C., & D'Ambrosi, N. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt259 · Cited by 109
CD44 expression in astrocytes and microglia is associated with ALS progression in a mouse model
Matsumoto, T., Imagama, S., Hirano, K., Ohgomori, T., Natori, T., Kobayashi, K., Muramoto, A., Ishiguro, N., & Kadomatsu, K. (2012) · Neuroscience Letters · doi:10.1016/j.neulet.2012.05.048 · Cited by 80
Mitochondria and endoplasmic reticulum crosstalk in amyotrophic lateral sclerosis
Manfredi, G., & Kawamata, H. (2016) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.08.004 · Cited by 76
Zhang, H., Andrekopoulos, C., Joseph, J., Crow, J., & Kalyanaraman, B. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.02.038 · Cited by 59
Dutta, K., Patel, P., & Julien, J.-P. (2018) · Experimental Neurology · doi:10.1016/j.expneurol.2018.08.008 · Cited by 56
Stieber, A., Gonatas, J. O., Moore, J. S., Bantly, A., Yim, H.-S., Yim, M. B., & Gonatas, N. K. (2004) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2003.12.004 · Cited by 38
A Docosahexaenoic Acid-Derived Pro-resolving Agent, Maresin 1, Protects Motor Neuron Cells Death
Ohuchi, K., Ono, Y., Joho, M., Tsuruma, K., Ogami, S., Yamane, S., Funato, M., Kaneko, H., Nakamura, S., Hara, H., et al. (2018) · Neurochemical Research · doi:10.1007/s11064-018-2556-1 · Cited by 22
Gerovska, D., Noer, J. B., Qin, Y., Ain, Q., Januzi, D., Schwab, M., Witte, O. W., Araúzo-Bravo, M. J., & Kretz, A. (2023) · Cell & Bioscience · doi:10.1186/s13578-023-01116-1 · Cited by 7
Metadata
- Authors
- Borchelt, D. R., Lee, M. K., Slunt, H. S., Guarnieri, M., Xu, Z. S., Wong, P. C., Brown, R. H., Price, D. L., Sisodia, S. S., & Cleveland, D. W.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1994-08-16
- Volume
- 91
- Issue
- 17
- Pages
- 8292-8296
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2032107666
- Cited by
- 621
- References
- 4
- FWCI
- 20.76
- Type
- journal article
- Language
- en
- Open access
- green
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