NDLI: ER Protein Processing Under Oxidative Stress: Implications and Prevention

Content Provider	Springer Nature Link
Author	Khalil, Mahmoud F. Valenzuela, Carlos Sisniega, Daniella Skouta, Rachid Narayan, Mahesh
Copyright Year	2016
Abstract	Elevated levels of mitochondrial nitrosative stress have been associated with the pathogenesis of both Parkinson’s and Alzheimer’s diseases. The mechanism involves catalytic poisoning of the endoplasmic reticulum (ER)—resident oxidoreductase chaperone, protein disulfide isomerase (PDI), and the subsequent accumulation of ER-processed substrate proteins. Using a model system to mimic mitochondrial oxidative and nitrosative stress, we demonstrate a PDI-independent mechanism whereby reactive oxygen species (ROS) compromise regeneration rates of disulfide bond-containing ER-processed proteins. Under ROS-duress, the secretion-destined traffic adopts disulfide-exposed structures making the protein flux retrotranslocation biased. We also demonstrate that ROS-compromised protein maturation rates can be rescued by the polyphenol ellagic acid (EA). Our results are significant in that they reveal an additional mechanism which could promote neurodegenerative disorders. Furthermore, our data reveal that EA possesses therapeutic potential as a lead prophylactic agent against oxidative/nitrosative stress-related neurodegenerative diseases.
Starting Page	213
Ending Page	220
Page Count	8
File Format	PDF
ISSN	10859195
Journal	Cell Biochemistry and Biophysics
Volume Number	74
Issue Number	2
e-ISSN	15590283
Language	English
Publisher	Springer US
Publisher Date	2016-03-17
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Parkinson’s disease Ellagic acid Nitrosative stress Protein folding Radical scavengers Protein aggregation Biochemistry Pharmacology/Toxicology Biotechnology Cell Biology Biophysics and Biological Physics
Content Type	Text
Resource Type	Article
Subject	Cell Biology Medicine Biochemistry Biophysics

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