The DOI matches its Crossref record; 38 of the 38 references it cites were found in a registry or an index.
Up‐Regulation of Protein Chaperones Preserves Viability of Cells Expressing Toxic Cu/Zn‐Superoxide Dismutase Mutants Associated with Amyotrophic Lateral Sclerosis
Abstract
Abstract : Mutations in the Cu/Zn‐superoxidedismutase (SOD‐1) gene underlie some familial cases of amytotrophic lateral sclerosis, a neurodegenerative disorder charactreized by loss of cortical, brainstem, and spinal motor nrurons. We present evidence that SOD‐1 mutants alter the activity of molecular chaperones that aid in proper protein folding and targeting of abnormal proteins for degradation. In a cultured cell line (NOH 3T3), resistance to mutant SOD‐1 toxicity correlated with increased overall chaperoning activity (measured by the ability of cytosolic extracts to prevent heat denaturation of catalase) as well as with up‐regulation of individual chaperones/stress proteins. In transgenic mice expressing human SOD‐1 with the G93A mutation, chaperoning activity was decreased in lumbar spinal cord but increased or unchanged in clinically unaffected tissues. Increasing the level of the stress‐inducible chaperone 70‐kDa heat shock protein by gene transfer reduced formation of mutant SOD‐containing proteinaceous aggregates in cultured primary motor neurons expressing G93A SOG‐1 and prolonged their survival. We propose that insufficiency of molecular chaperones may be directly involved in loss of motor neurons in this disease.
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Self-citationMotor Neuron Degeneration in Mice that Express a Human Cu,Zn Superoxide Dismutase Mutation
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Amyotrophic Lateral Ssclerosis and Structural Defects in Cu,Zn Superoxide Dismutase
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Evidence of Increased Oxidative Damage in Both Sporadic and Familial Amyotrophic Lateral Sclerosis
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Altered Reactivity of Superoxide Dismutase in Familial Amyotrophic Lateral Sclerosis
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Cited by
Oxidative stress in neurodegeneration: Cause or consequence?
Andersen, J. K. (2004) · Nature Medicine · doi:10.1038/nrn1434 · Cited by 1,869
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
Cellular Defenses against Unfolded Proteins
Sherman, M. Y., & Goldberg, A. L. (2001) · Neuron · doi:10.1016/s0896-6273(01)00177-5 · Cited by 991
Current hypotheses for the underlying biology of amyotrophic lateral sclerosis
Rothstein, J. D. (2009) · Annals of Neurology · doi:10.1002/ana.21543 · Cited by 703
The Endoplasmic Reticulum: Folding, Calcium Homeostasis, Signaling, and Redox Control
Görlach, A., Klappa, P., & Kietzmann, D. T. (2006) · Antioxidants & Redox Signaling · doi:10.1089/ars.2006.8.1391 · Cited by 615
Metadata
- Authors
- Bruening, W., Roy, J., Giasson, B., Figlewicz, D. A., Mushynski, W. E., & Durham, H. D.
- Venue
- Journal of Neurochemistry
- Publisher
- Wiley
- Published
- 1999-02
- Volume
- 72
- Issue
- 2
- Pages
- 693-699
- ISSN
- 0022-3042 (ISSN-L)
- 1471-4159
- OpenAlex
- W2113777884
- Cited by
- 263
- References
- 38
- FWCI
- 10.14
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Up‐Regulation of Protein Chaperones Preserves Viability of Cells Expressing Toxic Cu/Zn‐Superoxide Dismutase Mutants Associated with Amyotrophic Lateral Sclerosis. https://app.cochat.ai/papers/10.1046/j.1471-4159.1999.0720693.x
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- Bruening, W., Roy, J., Giasson, B., Figlewicz, D. A., Mushynski, W. E., & Durham, H. D. (1999). Up‐Regulation of Protein Chaperones Preserves Viability of Cells Expressing Toxic Cu/Zn‐Superoxide Dismutase Mutants Associated with Amyotrophic Lateral Sclerosis. Journal of Neurochemistry. https://doi.org/10.1046/j.1471-4159.1999.0720693.x
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
