Abstract
Alcohol is a simple and consumable biomolecule yet its excessive consumption disturbs numerous biological pathways damaging nearly all organs of the human body. One of the essential biological processes affected by the harmful effects of alcohol is proteostasis, which regulates the balance between biogenesis and turnover of proteins within and outside the cell. A significant amount of published evidence indicates that alcohol and its metabolites directly or indirectly interfere with protein homeostasis in the endoplasmic reticulum (ER) causing an accumulation of unfolded or misfolded proteins, which triggers the unfolded protein response (UPR) leading to either restoration of homeostasis or cell death, inflammation and other pathologies under severe and chronic alcohol conditions. The UPR senses the abnormal protein accumulation and activates transcription factors that regulate nuclear transcription of genes related to ER function. Similarly, this kind of protein stress response can occur in other cellular organelles, which is an evolving field of interest. Here, I review recent advances in the alcohol-induced ER stress response as well as discuss new concepts on alcohol-induced mitochondrial, Golgi and lysosomal stress responses and injuries.
Highlights
GI/Liver Division, Research Center for Liver Disease, Department of Medicine, Keck School of Medicine of USC, University of Southern California, Los Angeles, CA 90033, USA; Academic Editor: Natalia Osna
This review aims to highlight advances in alcohol-induced endoplasmic reticulum (ER) stress response and discuss potential molecular effects of alcohol on other organelle protein stress responses
Bcl-2e associated athanogen 3 (BAG3) was suppressed in the alcoholics, indicating that the molecular switch between the ER-associated degradation (ERAD) and autophagy for protein degradation was compromised, which might contribute to alcohol-induced neurodegeneration
Summary
Proteins are essential and large biomolecules that participate in virtually every process within the cell and affect a vast array of functions of living organisms. Unwanted proteins can be removed by autophagy, an intracellular degradation system that delivers cytoplasmic constituents to the lysosome [4] These regulations and cellular mechanisms safeguard quality of proteins and maintain the proteostasis. The UPR singling in the ER attenuates protein translation, increases expression of chaperones, and increases efficiency in protein trafficking and degradation, which help alleviate the effects of ER stress and restore the ER homeostasis [5]. Chronic ethanol consumption increases the production of superoxide, H2O2, lipid peroxides, or peroxynitrite [19,20,21], which breaks the redox status of the ER and perturbs the oxidative protein folding These biological and metabolic features link alcohol consumption to interference of the proteostasis, the UPR and. This review aims to highlight advances in alcohol-induced ER stress response and discuss potential molecular effects of alcohol on other organelle protein stress responses
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