Endoplasmic reticulum stress in liver diseases.

Autor:	Ajoolabady A; Shanghai Institute of Cardiovascular Diseases , Department of Cardiology , Zhongshan Hospital , Fudan University , Shanghai , China., Kaplowitz N; Division of Gastrointestinal and Liver Disease , Department of Medicine , Keck School of Medicine , University of Southern California , Los Angeles , California , USA.; USC Research Center for Liver Disease , Keck School of Medicine , University of Southern California , Los Angeles , California , USA., Lebeaupin C; Degenerative Diseases Program , Sanford Burnham Prebys Medical Discovery Institute , La Jolla , California , USA., Kroemer G; Centre de Recherche des Cordeliers , Equipe labellisée par la Ligue contre le cancer , Université de Paris , Sorbonne Université , Inserm U1138 , Institut Universitaire de France , Paris , France.; Metabolomics and Cell Biology Platforms , Institut Gustave Roussy , Villejuif , France.; Pôle de Biologie , Hôpital Européen Georges Pompidou , AP-HP , Paris , France., Kaufman RJ; Degenerative Diseases Program , Sanford Burnham Prebys Medical Discovery Institute , La Jolla , California , USA., Malhi H; Division of Gastroenterology and Hepatology , Mayo Clinic , Rochester , Minnesota , USA., Ren J; Shanghai Institute of Cardiovascular Diseases , Department of Cardiology , Zhongshan Hospital , Fudan University , Shanghai , China.; Department of Laboratory Medicine and Pathology , University of Washington , Seattle , Washington , USA.
Jazyk:	angličtina
Zdroj:	Hepatology (Baltimore, Md.) [Hepatology] 2023 Feb 01; Vol. 77 (2), pp. 619-639. Date of Electronic Publication: 2022 May 24.
DOI:	10.1002/hep.32562
Abstrakt:	The endoplasmic reticulum (ER) is an intracellular organelle that fosters the correct folding of linear polypeptides and proteins, a process tightly governed by the ER-resident enzymes and chaperones. Failure to shape the proper 3-dimensional architecture of proteins culminates in the accumulation of misfolded or unfolded proteins within the ER, disturbs ER homeostasis, and leads to canonically defined ER stress. Recent studies have elucidated that cellular perturbations, such as lipotoxicity, can also lead to ER stress. In response to ER stress, the unfolded protein response (UPR) is activated to reestablish ER homeostasis ("adaptive UPR"), or, conversely, to provoke cell death when ER stress is overwhelmed and sustained ("maladaptive UPR"). It is well documented that ER stress contributes to the onset and progression of multiple hepatic pathologies including NAFLD, alcohol-associated liver disease, viral hepatitis, liver ischemia, drug toxicity, and liver cancers. Here, we review key studies dealing with the emerging role of ER stress and the UPR in the pathophysiology of liver diseases from cellular, murine, and human models. Specifically, we will summarize current available knowledge on pharmacological and non-pharmacological interventions that may be used to target maladaptive UPR for the treatment of nonmalignant liver diseases. (Copyright © 2023 American Association for the Study of Liver Diseases.)
Databáze:	MEDLINE
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