The DOI matches its Crossref record; 30 of the 30 references it cites were found in a registry or an index.
Superoxide dismutase is an abundant component in cell bodies, dendrites, and axons of motor neurons and in a subset of other neurons.
Open accessAbstract
Mutation in superoxide dismutase 1 (SOD1), a Cu/Zn enzyme that removes oxygen radicals and protects against oxidative injury, has been implicated in some cases of familial amyotrophic lateral sclerosis (FALS). As a first approach to examining the mechanism(s) through which these mutations cause specific degeneration of motor neurons, we have used immunocytochemistry to identify the distribution of SOD1 in populations of cells in the peripheral and central nervous systems. In the spinal cord, intense SOD1 immunoreactivity was present in motor neurons, interneurons, and substantia gelatinosa. In motor neurons, SOD1 immunoreactivity was abundant in perikarya, dendrites, and axons; most of this activity appeared to be free in the cytoplasm, although a portion was associated with membranous vesicles, presumably peroxisomes. Since a variety of central nervous system neurons, including pyramidal cells in cerebral cortex and neurons of the CA3 and CA4 sectors of the hippocampus, showed high immunoreactivity but are unaffected in ALS, the apparent abundance of SOD1 does not predict vulnerability of neurons to mutations in SOD1. Rather, SOD1 accumulates in many neuronal populations but is particularly abundant in motor neurons. Consistent with recent studies of FALS-linked SOD1 mutations in vitro and in transgenic mice, our findings offer further support for the view that the mutations confer a gain of adverse function. In this view, high, rather than limiting, levels of SOD1 may place motor neurons selectively at risk in FALS.
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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
Raza, H., John, A., & Nemmar, A. (2013) · Cellular Physiology and Biochemistry · doi:10.1159/000350087 · Cited by 47,221
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
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
Temporal profile of neuronal damage in a model of transient forebrain ischemia
Pulsinelli, W. A., Brierley, J. B., & Plum, F. (1982) · Annals of Neurology · doi:10.1002/ana.410110509 · Cited by 2,675
Cellular defenses against damage from reactive oxygen species
Yu, B. P. (1994) · Physiological Reviews · doi:10.1152/physrev.1994.74.1.139 · Cited by 2,370
Amyotrophic Lateral Ssclerosis and Structural Defects in Cu,Zn Superoxide Dismutase
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., et al. (1993) · Science · doi:10.1126/science.8351519 · Cited by 1,477
Bowling, A. C., Schulz, J. B., Brown, R. H., & Beal, M. F. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb07478.x · Cited by 630
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. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.17.8292 · Cited by 621
Self-citationFridovich, I. (1986) · Advances in Enzymology - and Related Areas of Molecular Biology · doi:10.1002/9780470123041.ch2 · Cited by 468
Cited by
Caughey, B., & Lansbury, P. T. (2003) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.26.010302.081142 · Cited by 1,650
Wong, P. C., Pardo, C. A., Borchelt, D. R., Lee, M. K., Copeland, N. G., Jenkins, N. A., Sisodia, S. S., Cleveland, D. W., & Price, D. L. (1995) · Neuron · doi:10.1016/0896-6273(95)90259-7 · Cited by 1,445
Self-citationBruijn, 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-citationAggregation and Motor Neuron Toxicity of an ALS-Linked SOD1 Mutant Independent from Wild-Type SOD1
Bruijn, L. I., Houseweart, M. K., Kato, S., Anderson, K. L., Anderson, S. D., Ohama, E., Reaume, A. G., Scott, R. W., & Cleveland, D. W. (1998) · Science · doi:10.1126/science.281.5384.1851 · Cited by 1,228
Self-citationAltered Reactivity of Superoxide Dismutase in Familial Amyotrophic Lateral Sclerosis
Wiedau-Pazos, M., Goto, J. J., Rabizadeh, S., Gralla, E. B., Roe, J. A., Lee, M. K., Valentine, J. S., & Bredesen, D. E. (1996) · Science · doi:10.1126/science.271.5248.515 · Cited by 719
Metadata
- Authors
- Pardo, C. A., Xu, Z., Borchelt, D. R., Price, D. L., Sisodia, S. S., & Cleveland, D. W.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1995-02-14
- Volume
- 92
- Issue
- 4
- Pages
- 954-958
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2032670789
- Cited by
- 314
- References
- 30
- FWCI
- 15.08
- Type
- journal article
- Language
- en
- Open access
- green
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- CoChat. (2026). Citation check: Superoxide dismutase is an abundant component in cell bodies, dendrites, and axons of motor neurons and in a subset of other neurons. https://app.cochat.ai/papers/10.1073/pnas.92.4.954
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- Pardo, C. A., Xu, Z., Borchelt, D. R., Price, D. L., Sisodia, S. S., & Cleveland, D. W. (1995). Superoxide dismutase is an abundant component in cell bodies, dendrites, and axons of motor neurons and in a subset of other neurons. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.92.4.954
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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