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Oxid Med Cell Longev. 2017;2017:2818565. doi: 10.1155/2017/2818565. Epub 2017 Dec 31.

Protein Glutathionylation in the Pathogenesis of Neurodegenerative Diseases.

Author information

1
Soonchunhyang Institute of Medi-Bio Science, Soonchunhyang University, Cheonan 31151, Republic of Korea.
2
Department of Medical Biotechnology, Soonchunhyang University, Asan 31538, Republic of Korea.

Abstract

Protein glutathionylation is a redox-mediated posttranslational modification that regulates the function of target proteins by conjugating glutathione with a cysteine thiol group on the target proteins. Protein glutathionylation has several biological functions such as regulation of metabolic pathways, calcium homeostasis, signal transduction, remodeling of cytoskeleton, inflammation, and protein folding. However, the exact role and mechanism of glutathionylation during irreversible oxidative stress has not been completely defined. Irreversible oxidative damage is implicated in a number of neurological disorders. Here, we discuss and highlight the most recent findings and several evidences for the association of glutathionylation with neurodegenerative diseases and the role of glutathionylation of specific proteins in the pathogenesis of neurodegenerative diseases. Understanding the important role of glutathionylation in the pathogenesis of neurodegenerative diseases may provide insights into novel therapeutic interventions.

PMID:
29456785
PMCID:
PMC5804111
DOI:
10.1155/2017/2818565
[Indexed for MEDLINE]
Free PMC Article

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