The DOI matches its Crossref record; 37 of the 37 references it cites were found in a registry or an index.
Proteasomal inhibition leads to formation of ubiquitin/α‐synuclein‐immunoreactive inclusions in PC12 cells
Abstract
Proteasomal dysfunction has been recently implicated in the pathogenesis of several neurodegenerative diseases, including Parkinson's disease and diffuse Lewy body disease. We have developed an in vitro model of proteasomal dysfunction by applying pharmacological inhibitors of the proteasome, lactacystin or ZIE[O‐t Bu]‐A‐leucinal (PSI), to dopaminergic PC12 cells. Proteasomal inhibition caused a dose‐dependent increase in death of both naive and neuronally differentiated PC12 cells, which could be prevented by caspase inhibition or CPT‐cAMP. A percentage of the surviving cells contained discrete cytoplasmic ubiquitinated inclusions, some of which also contained synuclein‐1, the rat homologue of human α‐synuclein. However the total level of synuclein‐1 was not altered by proteasomal inhibition. The ubiquitinated inclusions were present only within surviving cells, and their number was increased if cell death was prevented. We have thus replicated, in this model system, the two cardinal pathological features of Lewy body diseases, neuronal death and the formation of cytoplasmic ubiquitinated inclusions. Our findings suggest that inclusion body formation and cell death may be dissociated from one another.
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Cites
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Mutation in the α-Synuclein Gene Identified in Families with Parkinson's Disease
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Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism
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AlaSOPro mutation in the gene encoding α-synuclein in Parkinson's disease
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Chronic systemic pesticide exposure reproduces features of Parkinson's disease
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The relevance of the Lewy body to the pathogenesis of idiopathic Parkinson's disease.
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Aggresomes: A Cellular Response to Misfolded Proteins
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A Drosophila model of Parkinson's disease
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Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase
Shimura, H., Hattori, N., Kubo, S.-I., Mizuno, Y., Asakawa, S., Minoshima, S., Shimizu, N., Iwai, K., Chiba, T., Tanaka, K., et al. (2000) · Nature Genetics · doi:10.1038/77060 · Cited by 2,024 · cited 2×
“…Lewy body disease; DMSO, dimethyl sulfoxide; NGF, nerve growth factor; PAGE, polyacrylamide gel electrophoresis; PD, Parkinson's disease; PSI, ZIE[O-tBu]-A-leucinal; SDS, sodium dodecyl sulfate; UCH-L1, ubiquitin C-terminal hydrolase L1. or diminish parkin's E3-like activity (Shimura et al. 2000).”
Cited by
Impaired Degradation of Mutant α-Synuclein by Chaperone-Mediated Autophagy
Cuervo, A. M., Stefanis, L., Fredenburg, R., Lansbury, P. T., & Sulzer, D. (2004) · Science · doi:10.1126/science.1101738 · Cited by 2,024
Self-citationα-Synuclein Is Degraded by Both Autophagy and the Proteasome
Webb, J. L., Ravikumar, B., Atkins, J., Skepper, J. N., & Rubinsztein, D. C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300227200 · Cited by 1,429
Emmanouilidou, E., Melachroinou, K., Roumeliotis, T., Garbis, S. D., Ntzouni, M., Margaritis, L. H., Stefanis, L., & Vekrellis, K. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.5699-09.2010 · Cited by 1,115
“More than 98% of the cells cultured under these conditions represent postmitotic neurons (Rideout et al., 2001).”
BackgroundSelf-citationThe scientific and clinical basis for the treatment of Parkinson disease (2009)
Olanow, C. W., Stern, M. B., & Sethi, K. (2009) · Neurology · doi:10.1212/wnl.0b013e3181a1d44c · Cited by 908
Liu, Y., Fallon, L., Lashuel, H. A., Liu, Z., & Lansbury, P. T. (2002) · Cell · doi:10.1016/s0092-8674(02)01012-7 · Cited by 785
Metadata
- Authors
- Rideout, H. J., Larsen, K. E., Sulzer, D., & Stefanis, L.
- Venue
- Journal of Neurochemistry
- Publisher
- Wiley
- Published
- 2001-08-15
- Volume
- 78
- Issue
- 4
- Pages
- 899-908
- ISSN
- 0022-3042 (ISSN-L)
- 1471-4159
- OpenAlex
- W1494109356
- Cited by
- 274
- References
- 37
- FWCI
- 16.59
- Type
- journal article
- Language
- en
- Open access
- closed
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- Rideout, H. J., Larsen, K. E., Sulzer, D., & Stefanis, L. (2001). Proteasomal inhibition leads to formation of ubiquitin/α‐synuclein‐immunoreactive inclusions in PC12 cells. Journal of Neurochemistry. https://doi.org/10.1046/j.1471-4159.2001.00474.x
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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.
