title: Pharmacological Modulators of Endoplasmic Reticulum Stress in Metabolic Diseases.
abstract: The endoplasmic reticulum (ER) is the principal organelle responsible for correct protein folding, a step in protein synthesis that is critical for the functional conformation of proteins. ER stress is a primary feature of secretory cells and is involved in the pathogenesis of numerous human diseases, such as certain neurodegenerative and cardiometabolic disorders. The unfolded protein response (UPR) is a defense mechanism to attenuate ER stress and maintain the homeostasis of the organism. Two major degradation systems, including the proteasome and autophagy, are involved in this defense system. If ER stress overwhelms the capacity of the cell's defense mechanisms, apoptotic death may result. This review is focused on the various pharmacological modulators that can protect cells from damage induced by ER stress. The possible mechanisms for cytoprotection are also discussed.
authors: Division of Endocrinology and Metabolism, Department of Internal Medicine, College of Medicine, Korea University, Seoul 152-703, Korea. ohayo2030@hanmail.net.
authors: Tae Woo
authors: TW
authors: Jung
authors: Division of Endocrinology and Metabolism, Department of Internal Medicine, College of Medicine, Korea University, Seoul 152-703, Korea. medica7@gmail.com.
authors: Kyung Mook
authors: KM
authors: Choi
mesh_terms: D057911:Angiotensin Receptor Antagonists / Q000494:pharmacology; D000818:Animals; D059865:Endoplasmic Reticulum Stress / Q000187:drug effects*; D006801:Humans; D008659:Metabolic Diseases / Q000378:metabolism*; D011480:Protease Inhibitors / Q000494:pharmacology; D047428:Protein Kinase Inhibitors / Q000494:pharmacology; D020123:Sirolimus / Q000494:pharmacology; D056811:Unfolded Protein Response / Q000187:drug effects
chemical_list: D057911:Angiotensin Receptor Antagonists; D011480:Protease Inhibitors; D047428:Protein Kinase Inhibitors; D020123:Sirolimus
keywords: AMPK-activated protein kinase; angiotensin II type 1 receptor blockers; endoplasmic reticulum stress; glucagon-like peptide-1; peroxisome proliferator-activated receptors; unfolded protein response