The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Copper chaperone for superoxide dismutase is essential to activate mammalian Cu/Zn superoxide dismutase
Open accessAbstract
Recent studies in Saccharomyces cerevisiae suggest that the delivery of copper to Cu/Zn superoxide dismutase (SOD1) is mediated by a cytosolic protein termed the copper chaperone for superoxide dismutase (CCS). To determine the role of CCS in mammalian copper homeostasis, we generated mice with targeted disruption of CCS alleles ( CCS −/− mice). Although CCS −/− mice are viable and possess normal levels of SOD1 protein, they reveal marked reductions in SOD1 activity when compared with control littermates. Metabolic labeling with 64 Cu demonstrated that the reduction of SOD1 activity in CCS −/− mice is the direct result of impaired Cu incorporation into SOD1 and that this effect was specific because no abnormalities were observed in Cu uptake, distribution, or incorporation into other cuproenzymes. Consistent with this loss of SOD1 activity, CCS −/− mice showed increased sensitivity to paraquat and reduced female fertility, phenotypes that are characteristic of SOD1-deficient mice. These results demonstrate the essential role of any mammalian copper chaperone and have important implications for the development of novel therapeutic strategies in familial amyotrophic lateral sclerosis.
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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
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-citation
Cited by
UNRAVELING 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
Molecular biology of amyotrophic lateral sclerosis: insights from genetics
Pasinelli, P., & Brown, R. H. (2006) · Nature Reviews Neuroscience · doi:10.1038/nrn1971 · Cited by 1,107
Metallochaperones, an Intracellular Shuttle Service for Metal Ions
O'Halloran, T. V., & Culotta, V. C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.r000006200 · Cited by 806
Self-citationCopper and iron disorders of the brain
Madsen, E., & Gitlin, J. D. (2007) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.30.051606.094232 · Cited by 557
Self-citationCopper trafficking to the mitochondrion and assembly of copper metalloenzymes
Cobine, P. A., Pierrel, F., & Winge, D. R. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.03.002 · Cited by 317
Metadata
- Authors
- Wong, P. C., Waggoner, D., Subramaniam, J. R., Tessarollo, L., Bartnikas, T. B., Culotta, V. C., Price, D. L., Rothstein, J., & Gitlin, J. D.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2000-02-29
- Volume
- 97
- Issue
- 6
- Pages
- 2886-2891
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1969665448
- Cited by
- 364
- References
- 2
- FWCI
- 20.92
- Type
- journal article
- Language
- en
- Open access
- green
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- Wong, P. C., Waggoner, D., Subramaniam, J. R., Tessarollo, L., Bartnikas, T. B., Culotta, V. C., Price, D. L., Rothstein, J., & Gitlin, J. D. (2000). Copper chaperone for superoxide dismutase is essential to activate mammalian Cu/Zn superoxide dismutase. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.040461197
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