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FEBS Lett. 2012 Aug 31;586(18):2826-34. doi: 10.1016/j.febslet.2012.07.023. Epub 2012 Jul 22.

Protein disulfide isomerases in neurodegeneration: from disease mechanisms to biomedical applications.

Author information

1
Institute of Biomedical Sciences, Program of Cellular and Molecular Biology, University of Chile, Santiago, Chile.

Abstract

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.

PMID:
22828277
DOI:
10.1016/j.febslet.2012.07.023
[Indexed for MEDLINE]
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