The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Distinct cleavage patterns of normal and pathologic forms of α‐synuclein by calpain I in vitro
Abstract
Parkinson's disease (PD) is characterized by fibrillary neuronal inclusions called Lewy bodies (LBs) consisting largely of alpha‐synuclein (α‐syn), the protein mutated in some patients with familial PD. The mechanisms of α‐syn fibrillization and LB formation are unknown, but may involve aberrant degradation or turnover. We examined the ability of calpain I to cleave α‐syn in vitro. Calpain I cleaved wild‐type α‐syn predominantly after amino acid 57 and within the non‐amyloid component (NAC) region. In contrast, calpain I cleaved fibrillized α‐syn primarily in the region of amino acid 120 to generate fragments like those that increase susceptibility to dopamine toxicity and oxidative stress. Further, while calpain I cleaved wild‐type α‐syn after amino acid 57, this did not occur in mutant A53T α‐syn. This paucity of proteolysis could increase the stability of A53T α‐syn, suggesting that calpain I might protect cells from forming LBs by specific cleavages of soluble wild‐type α‐syn. However, once α‐syn has polymerized into fibrils, calpain I may contribute to toxicity of these forms of α‐syn by cleaving at aberrant sites within the C‐terminal region. Elucidating the role of calpain I in the proteolytic processing of α‐syn in normal and diseased brains may clarify mechanisms of neurodegenerative α‐synucleinopathies.
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Cites
AlaSOPro mutation in the gene encoding α-synuclein in Parkinson's disease
Krüger, R., Kuhn, W., Müller, T., Woitalla, D., Graeber, M., Kösel, S., Przuntek, H., Epplen, J. T., Schols, L., & Riess, O. (1998) · Nature Genetics · doi:10.1038/ng0298-106 · Cited by 3,836
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Proteasomal function is impaired in substantia nigra in Parkinson’s disease
McNaught, K. S. P., & Jenner, P. (2001) · Neuroscience Letters · doi:10.1016/s0304-3940(00)01701-8 · Cited by 653
Degradation of α-Synuclein by Proteasome
Bennett, M. C., Bishop, J. F., Leng, Y., Chock, P. B., Chase, T. N., & Mouradian, M. M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.48.33855 · Cited by 417
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Cited by
-Synuclein in Parkinson's Disease
Stefanis, L. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a009399 · Cited by 1,446
Cell Biology and Pathophysiology of α-Synuclein
Burré, J., Sharma, M., & Südhof, T. C. (2018) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a024091 · Cited by 579
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On the Sequential Determinants of Calpain Cleavage
Tompa, P., Buzder-Lantos, P., Tantos, A., Farkas, A., Szilágyi, A., Bánóczi, Z., Hudecz, F., & Friedrich, P. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313873200 · Cited by 317
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Metadata
- Authors
- Mishizen‐Eberz, A. J., Guttmann, R. P., Giasson, B. I., Day, G. A., Hodara, R., Ischiropoulos, H., Lee, V. M. ‐., Trojanowski, J. Q., & Lynch, D. R.
- Venue
- Journal of Neurochemistry
- Publisher
- Wiley
- Published
- 2003-07-21
- Volume
- 86
- Issue
- 4
- Pages
- 836-847
- ISSN
- 0022-3042 (ISSN-L)
- 1471-4159
- OpenAlex
- W1807475000
- Cited by
- 160
- References
- 6
- FWCI
- 7.46
- Type
- journal article
- Language
- en
- Open access
- closed
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- Mishizen‐Eberz, A. J., Guttmann, R. P., Giasson, B. I., Day, G. A., Hodara, R., Ischiropoulos, H., Lee, V. M. ‐., Trojanowski, J. Q., & Lynch, D. R. (2003). Distinct cleavage patterns of normal and pathologic forms of α‐synuclein by calpain I in vitro. Journal of Neurochemistry. https://doi.org/10.1046/j.1471-4159.2003.01878.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).
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