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13 - Implications of Nitrosative Stress-Induced Protein Misfolding in Neurodegeneration

from Part II - Cell Death in Tissues and Organs

Published online by Cambridge University Press:  07 September 2011

Douglas R. Green
Affiliation:
St. Jude Children's Research Hospital, Memphis, Tennessee
Tomohiro Nakamura
Affiliation:
Sanford-Burnham Institute for Medical Research
Stuart A. Lipton
Affiliation:
Sanford-Burnham Medical Research Institute
John C. Reed
Affiliation:
Sanford-Burnham Medical Research Institute, La Jolla, California
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Summary

Summary

Several chronic neurodegenerative disorders manifest deposits of misfolded or aggregated proteins. Genetic mutations are the root cause for protein misfolding in rare families, but the majority of patients have sporadic forms possibly related to environmental factors. In some cases, the ubiquitin-proteasome system or molecular chaperones can prevent accumulation of aberrantly folded proteins. Recent studies suggest that generation of excessive nitric oxide (NO) and reactive oxygen species, in part due to overactivity of the N-methyl-D-aspartate (NMDA) subtype of glutamate receptor, can mediate protein misfolding in the absence of genetic mutation. S-Nitrosylation, or covalent reaction of NO with specific protein thiol groups, represents one mechanism contributing to NO-induced protein misfolding and neurotoxicity. Here, we present evidence suggesting that NO contributes to protein misfolding via S-nitrosylating protein-disulfide isomerase or the E3 ubiquitin ligase parkin. We discuss how the drugs memantine or NitroMemantine can inhibit excessive NMDA receptor activity to ameliorate NO production, protein misfolding, and neurodegeneration.

Type
Chapter
Information
Apoptosis
Physiology and Pathology
, pp. 145 - 152
Publisher: Cambridge University Press
Print publication year: 2011

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References

Ankarcrona, M., Dypbukt, J. M., Bonfoco, E., et al. (1995). Glutamate-induced neuronal death: a succession of necrosis or apoptosis depending on mitochondrial function. Neuron, 15, 961–73.
Bonfoco, E., Krainc, D., Ankarcrona, M., et al. (1995). Apoptosis and necrosis: two distinct events induced, respectively, by mild and intense insults with N-methyl-D-aspartate or nitric oxide/superoxide in cortical cell cultures. Proc Natl Acad Sci U S A, 92, 7162–6.
Chen, H. S. and Lipton, S. A. (2006). The chemical biology of clinically tolerated NMDA receptor antagonists. J Neurochem, 97, 1611–26.
Chung, K. K., Thomas, B., Li, X., et al. (2004). S-nitrosylation of parkin regulates ubiquitination and compromises parkin's protective function. Science, 304, 1328–31.
Dawson, V. L., Dawson, T. M., London, E. D., et al. (1991). Nitric oxide mediates glutamate neurotoxicity in primary cortical cultures. Proc Natl Acad Sci U S A, 88, 6368–71.
Ellgaard, L. and Ruddock, L. W. (2005). The human protein disulphide isomerase family: substrate interactions and functional properties. EMBO Rep, 6, 28–32.
Gruber, C. W., Cemazar, M., Heras, B., et al. (2006). Protein disulfide isomerase: the structure of oxidative folding. Trends Biochem Sci, 31, 455–64.
Hess, D. T., Matsumoto, A., Kim, S. O., et al. (2005). Protein S-nitrosylation: purview and parameters. Nat Rev Mol Cell Biol, 6, 150–66.
Lipton, S. A. (2006). Paradigm shift in neuroprotection by NMDA receptor blockade: memantine and beyond. Nat Rev Drug Discov, 5, 160–70.
Lipton, S. A., Choi, Y. B., Pan, Z. H., et al. (1993). A redox-based mechanism for the neuroprotective and neurodestructive effects of nitric oxide and related nitroso-compounds. Nature, 364, 626–32.
Lipton, S. A. and Rosenberg, P. A. (1994). Excitatory amino acids as a final common pathway for neurologic disorders. N Engl J Med, 330, 613–22.
Ross, C. A. and Pickart, C. M. (2004). The ubiquitin-proteasome pathway in Parkinson's disease and other neurodegenerative diseases. Trends Cell Biol, 14, 703–11.
Shimura, H., Hattori, N., Kubo, S., et al. (2000). Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase. Nat Genet, 25, 302–5.
Uehara, T., Nakamura, T., Yao, D., et al. (2006). S-nitrosylated protein-disulphide isomerase links protein misfolding to neurodegeneration. Nature, 441, 513–7.
Yao, D., Gu, Z., Nakamura, T., et al. (2004). Nitrosative stress linked to sporadic Parkinson's disease: S-nitrosylation of parkin regulates its E3 ubiquitin ligase activity. Proc Natl Acad Sci U S A, 101, 10810–4.

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