The ability of translated cellular proteins to perform their functions requires their proper folding after synthesis. The endoplasmic reticulum (ER) is responsible for coordinating protein folding and maturation. Infections, genetic mutations, environmental factors and many other conditions can lead to challenges to the ER known as ER stress. Altering ER homeostasis results in accumulation of misfolded or unfolded proteins. To eliminate this problem, a response is initiated by the cell called the unfolded protein response (UPR), which involves multiple signaling pathways. Prolonged ER stress or a dysregulated UPR can lead to premature apoptosis and an exaggerated inflammatory response. Following these discoveries, ER stress was shown to be related to several chronic diseases, such as diabetes mellitus, neurodegenerative disorders, fatty liver disease and inflammatory bowel disease that have not yet been clearly demonstrated pathophysiologically. Here, we review the field and present up-to-date information on the relationship between biological processing, ER stress, UPR, and several chronic diseases.
- biological transport
- cell death
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Contributors ARK drafted the manuscript. ARK, GNV and QZ edited the manuscript.
Funding This study was supported by the National Institute of Diabetes and Digestive and Kidney Diseases (DK099052 and DK118959) funds to GNV and QZ; and the Department of Veterans Affairs (1l01CX001477) to QZ. ARK was supported by funds received from the Akdamar Fellowship Program, Department of Gastroenterology and Hepatology, Tulane University Health Sciences Center.
Competing interests None declared.
Patient consent for publication Not required.
Provenance and peer review Not commissioned; externally peer reviewed.
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