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Endoplasmic reticulum stress in liver diseases
Amir Ajoolabady1, Neil Kaplowitz2,3, Cynthia Lebeaupin4
1Shanghai Institute of Cardiovascular Diseases , Department of Cardiology , Zhongshan Hospital , Fudan University , Shanghai , China.
Hepatology (Baltimore, Md.)
|May 7, 2022
Summary
Endoplasmic reticulum (ER) stress, triggered by misfolded proteins, impacts liver health. The unfolded protein response (UPR) can be adaptive or maladaptive, influencing liver disease treatment strategies.
Area of Science:
- Cellular Biology
- Molecular Biology
- Hepatology
Background:
- The endoplasmic reticulum (ER) is crucial for protein folding, with dysfunction leading to ER stress.
- ER stress, including that induced by lipotoxicity, disrupts cellular homeostasis.
- The unfolded protein response (UPR) is a cellular mechanism to cope with ER stress, with adaptive and maladaptive outcomes.
Approach:
- This review synthesizes findings from cellular, murine, and human models.
- It examines the role of ER stress and UPR in liver disease pathophysiology.
- Focuses on interventions targeting maladaptive UPR in nonmalignant liver diseases.
Key Points:
- ER stress is implicated in various liver pathologies like NAFLD, alcoholic liver disease, and viral hepatitis.
- The UPR's dual role (adaptive vs. maladaptive) is critical in determining disease progression.
- Lipotoxicity is identified as a cellular perturbation contributing to ER stress.
Conclusions:
- ER stress and UPR are central to liver disease pathogenesis.
- Targeting maladaptive UPR offers potential therapeutic avenues for nonmalignant liver conditions.
- Further research into pharmacological and non-pharmacological interventions is warranted.
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