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Biochem Biophys Res Commun. 2010 Feb 19;392(4):567-71. doi: 10.1016/j.bbrc.2010.01.071. Epub 2010 Jan 25.

Rescue of ER oxidoreductase function through polyphenolic phytochemical intervention: implications for subcellular traffic and neurodegenerative disorders.

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Department of Chemistry, University of Texas at El Paso, El Paso, TX 79968, USA.


Protein disulfide isomerase (PDI), the chief endoplasmic reticulum (ER) resident oxidoreductase chaperone that catalyzes maturation of disulfide-bond-containing proteins is involved in the pathogenesis of both Parkinson's (PD) and Alzheimer's (AD) diseases. S-nitrosylation of PDI cysteines due to nitrosative stress is associated with cytosolic debris accumulation and Lewy-body aggregates in PD and AD brains. We demonstrate that the polyphenolic phytochemicals curcumin and masoprocol can rescue PDI from becoming S-nitrosylated and maintain its catalytic function under conditions mimicking nitrosative stress by forming stable NOx adducts. Furthermore, both polyphenols intervene to prevent the formation of PDI-resistant polymeric misfolded protein forms that accumulate upon exposure to oxidative stress. Our study suggests that curcumin and masoprocol can serve as lead-candidate prophylactics for reactive oxygen species induced chaperone damage, protein misfolding and neurodegenerative disease; importantly, they can play a vital role in sustaining traffic along the ER's secretory pathway by preserving functional integrity of PDI.

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