Journal
FEBS LETTERS
Volume 586, Issue 18, Pages 2826-2834Publisher
WILEY
DOI: 10.1016/j.febslet.2012.07.023
Keywords
Neurodegenerative disease; Protein disulfide isomerase; Protein misfolding; Endoplasmic reticulum stress; Protein quality control
Funding
- Muscular Dystrophy Association and ALS Therapy Alliance
- FONDECYT [1100176]
- postdoctoral FONDECYT fellowship [3110067]
- FONDAP Grant [15010006]
- Millennium Institute [P09-015-F]
- Ring Initiative Act [1109]
- Alzheimer Association
- North American Spine Society
- Michael J. Fox Foundation for Parkinson research
- CONICYT
- FEBA Foundation PhD fellowships
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Protein disulfide isomerases (PDIs) are a family of foldases and chaperones primarily located at the endoplasmic reticulum that catalyze the formation and isomerization of disulfide bonds thereby facilitating protein folding. PDIs also perform important physiological functions in protein quality control, cell death, and cell signaling. Protein misfolding is involved in the etiology of the most common neurodegenerative diseases, including Alzheimer, Parkinson, amyotrophic lateral sclerosis, Prion-related disorders, among others. Accumulating evidence indicate altered expression of PDIs as a prominent and common feature of these neurodegenerative conditions. Here we overview most recent advances in our understanding of the possible functional contribution of PDIs to neurodegeneration, depicting a complex and poorly understood scenario. Possible therapeutic benefits of targeting PDIs in a disease context and their use as biomarkers are discussed. (c) 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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