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Redox regulation in amyotrophic lateral sclerosis. | LitMetric

Redox regulation in amyotrophic lateral sclerosis.

Oxid Med Cell Longev

Department of Biochemistry, La Trobe Institute for Molecular Science, La Trobe University, Vic 3086, Australia.

Published: August 2013

AI Article Synopsis

  • - Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disease caused by the death of motor neurons, and understanding its progression is crucial due to the absence of effective treatments.
  • - Research suggests that dysregulation in redox processes may contribute to ALS, affecting oxidative stress, protein misfolding, and mitochondrial dysfunction, among other cellular abnormalities.
  • - The chaperone protein disulphide isomerase (PDI) is highlighted as potentially significant in redox dysregulation, as it is vital for proper protein folding; any disruption in this function could negatively impact motor neuron health.

Article Abstract

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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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3596916PMC
http://dx.doi.org/10.1155/2013/408681DOI Listing

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