Redox Regulation in Amyotrophic Lateral Sclerosis

被引:70
作者
Parakh, Sonam [1 ]
Spencer, Damian M. [1 ]
Halloran, Mark A. [2 ]
Soo, Kai Y. [1 ]
Atkin, Julie D. [1 ,3 ]
机构
[1] La Trobe Univ, Dept Biochem, La Trobe Inst Mol Sci, Bundoora, Vic 3086, Australia
[2] La Trobe Univ, Sch Psychol Sci, Bundoora, Vic 3086, Australia
[3] Univ Melbourne, Florey Dept Neurosci, Parkville, Vic 3010, Australia
基金
英国医学研究理事会;
关键词
PROTEIN-DISULFIDE-ISOMERASE; ENDOPLASMIC-RETICULUM STRESS; FRONTOTEMPORAL LOBAR DEGENERATION; INCREASED OXIDATIVE DAMAGE; MOTOR-NEURON DEGENERATION; TRANSGENIC MOUSE MODEL; ANTERIOR HORN NEURONS; SUPEROXIDE-DISMUTASE; REACTIVE OXYGEN; CEREBROSPINAL-FLUID;
D O I
10.1155/2013/408681
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disease that results from the death of upper and lower motor neurons. Due to a lack of effective treatment, it is imperative to understand the underlying mechanisms and processes involved in disease progression. Regulations in cellular reduction/oxidation (redox) processes are being increasingly implicated in disease. Here we discuss the possible involvement of redox dysregulation in the pathophysiology of ALS, either as a cause of cellular abnormalities or a consequence. We focus on its possible role in oxidative stress, protein misfolding, glutamate excitotoxicity, lipid peroxidation and cholesterol esterification, mitochondrial dysfunction, impaired axonal transport and neurofilament aggregation, autophagic stress, and endoplasmic reticulum (ER) stress. We also speculate that an ER chaperone protein disulphide isomerase (PDI) could play a key role in this dysregulation. PDI is essential for normal protein folding by oxidation and reduction of disulphide bonds, and hence any disruption to this process may have consequences for motor neurons. Addressing the mechanism underlying redox regulation and dysregulation may therefore help to unravel the molecular mechanism involved in ALS.
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页数:12
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