Mechanisms of Neuroprotection by Protein Disulphide Isomerase in Amyotrophic Lateral SclerosisReport as inadecuate




Mechanisms of Neuroprotection by Protein Disulphide Isomerase in Amyotrophic Lateral Sclerosis - Download this document for free, or read online. Document in PDF available to download.

Neurology Research InternationalVolume 2011 2011, Article ID 317340, 7 pages

Review Article

Department of Biochemistry, La Trobe Institute for Molecular Science, La Trobe University, Bundoora, VIC 3086, Australia

Howard Florey Institute, Florey Neuroscience Institutes and Centre for Neuroscience, The University of Melbourne, Parkville, VIC 3010, Australia

Received 15 November 2010; Accepted 20 February 2011

Academic Editor: Changiz Geula

Copyright © 2011 Adam K. Walker and Julie D. Atkin. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

Amyotrophic lateral sclerosis ALS is a devastating neurodegenerative disease characterised by the progressive loss of motor neurons, leading to paralysis and death within several years of onset. Although protein misfolding is a key feature of ALS, the upstream triggers of disease remain elusive. Recently, endoplasmic reticulum ER stress was identified as an early and central feature in ALS disease models as well as in human patient tissues, indicating that ER stress could be an important process in disease pathogenesis. One important chaperone induced by ER stress is protein disulphide isomerase PDI, which is both upregulated and posttranslationally inhibited by S-nitrosylation in ALS. In this paper, we present evidence from studies of genetics, model organisms, and patient tissues which indicate an active role for PDI and ER stress in ALS disease processes.





Author: Adam K. Walker and Julie D. Atkin

Source: https://www.hindawi.com/



DOWNLOAD PDF




Related documents