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Protein Misfolding and Endoplasmic Reticulum Stress in Chronic Lung DiseaseProtein Misfolding in Chronic Lung Disease

James Wei, BSc; Sadaf Rahman, BSc; Ehab A. Ayaub, BSc; Jeffrey G. Dickhout, PhD; Kjetil Ask, PhD
Author and Funding Information

From the Department of Medicine (Messrs Wei and Ayaub, Ms Rahman, and Drs Dickhout and Ask), Department of Biochemistry and Biomedical Sciences (Dr Ask), and McMaster Immunology Research Center (Mr Ayaub and Dr Ask), McMaster University; Firestone Institute for Respiratory Health (Messrs Wei and Ayaub, Ms Rahman, and Dr Ask), St. Joseph’s Healthcare; and Hamilton Centre for Kidney Research (Drs Dickhout and Ask), Hamilton, ON, Canada.

Correspondence to: Kjetil Ask, PhD, Department of Medicine, McMaster University, Firestone Institute for Respiratory Health, 50 Charlton Ave E, Room T2112, Hamilton, ON, L8N 4A6, Canada; e-mail: askkj@mcmaster.ca


Reproduction of this article is prohibited without written permission from the American College of Chest Physicians. See online for more details.


Chest. 2013;143(4):1098-1105. doi:10.1378/chest.12-2133
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The pathogenesis of chronic lung disorders is poorly understood but is often thought to arise because of repeated injuries derived from exposure to exogenous or endogenous stress factors. Protein-misfolding events have been observed in a variety of genetic and nongenetic chronic lung disorders and may contribute to both the initiation and the progression of lung disease through endoplasmic reticulum (ER) stress and activation of the unfolded protein response (UPR). Evidence indicates that exposure to common lung irritants such as cigarette smoke, environmental pollutants, and infectious viral or bacterial agents can induce ER stress and protein misfolding. Although the UPR is thought to be a molecular mechanism involved in the repair and restoration of protein homeostasis or “proteostasis,” prolonged activation of the UPR may lead to compromised cellular functions, cellular transformation, or cell death. Here, we review literature that associates protein-misfolding events with ER stress and UPR activation and discuss how this basic molecular repair mechanism may contribute to the initiation and progression of various genetic and nongenetic chronic lung diseases.

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