Neurodegenerative diseases involve the progressive loss of neurons, and a pathological hallmark is the presence of abnormal inclusions containing misfolded proteins. Although the precise molecular mechanisms triggering neurodegeneration remain unclear, endoplasmic reticulum (ER) stress, elevated oxidative and nitrosative stress, and protein misfolding are important features in pathogenesis. Protein disulphide isomerase (PDI) is the prototype of a family of molecular chaperones and foldases upregulated during ER stress that are increasingly implicated in neurodegenerative diseases. PDI catalyzes the rearrangement and formation of disulphide bonds, thus facilitating protein folding, and in neurodegeneration may act to ameliorate the burden of protein misfolding. However, an aberrant posttranslational modification of PDI, S-nitrosylation, inhibits its protective function in these conditions. S-nitrosylation is a redox-mediated modification that regulates protein function by covalent addition of nitric oxide- (NO-) containing groups to cysteine residues. Here, we discuss the evidence for abnormal S-nitrosylation of PDI (SNO-PDI) in neurodegeneration and how this may be linked to another aberrant modification of PDI, S-glutathionylation. Understanding the role of aberrant S-nitrosylation/S-glutathionylation of PDI in the pathogenesis of neurodegenerative diseases may provide insights into novel therapeutic interventions in the future. 1. Introduction Neurodegenerative diseases share several common pathological characteristics, including the aberrant aggregation of misfolded proteins, leading to the formation of abnormal protein inclusions [1]. These diseases are also frequently classified as protein conformational disorders in which protein aggregation occurs due to the exposure of hydrophobic regions [2]. The most common neurodegenerative diseases include Alzheimer’s disease (AD), Parkinson’s disease (PD), amyotrophic lateral sclerosis (ALS), Creutzfeldt-Jakob disease (CJD), and Huntington’s disease (HD). These diseases differ according to the specific group of neurons targeted and the type of misfolded proteins that aggregate. In AD, the accumulation of aggregated proteins occurs in cortical regions and involves both β-amyloid (βA), which forms extracellular amyloid plaques, and tau, which is hyperphosphorylated and forms intracellular neurofibrillary tangles (NFT) [3, 4]. PD involves the formation of Lewy bodies (LB) containing misfolded α-synuclein [5], and in HD aggregated Huntington protein with expanded polyglutamine repeats forms inclusions in the
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