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Depression is a devastating mood disorder that causes profound disability worldwide. Despite the increasing number of antidepressant medications available, the treatment options for depression are limited. Therefore, understanding the etiology and pathophysiology of depression, and exploiting potential novel agents to treat and prevent this disorder are imperative. Endoplasmic reticulum (ER) stress activates the unfolded protein response and mediates the pathogenesis of psychiatric diseases, including depression. Emerging evidence in human and animal models suggests an intriguing link between ER stress and depression. The ER serves as an important subcellular organelle for the synthesis, folding, modification, and transport of proteins, a process that is highly developed in neuronal cells. Perturbations of ER homeostasis lead to ER stress, and ER stress helps to restore the normal ER function by restoring the protein‑folding capacity of the ER. This biological defense mechanism is imperative to prevent the disease. However, excessive or persistent ER stress eventually causes cell death. If the damage occurs in the hippocampus, the amygdala and striatum and other areas of the neurons will be involved in the development of depression. In this review article, we explore how ER stress might have an important role in the pathophysiology of depression and how different drugs affect depression through ER stress.
This article was published in the following journal.
Name: Molecular medicine reports
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A system of cisternae in the CYTOPLASM of many cells. In places the endoplasmic reticulum is continuous with the plasma membrane (CELL MEMBRANE) or outer membrane of the nuclear envelope. If the outer surfaces of the endoplasmic reticulum membranes are coated with ribosomes, the endoplasmic reticulum is said to be rough-surfaced (ENDOPLASMIC RETICULUM, ROUGH); otherwise it is said to be smooth-surfaced (ENDOPLASMIC RETICULUM, SMOOTH). (King & Stansfield, A Dictionary of Genetics, 4th ed)
Various physiological or molecular disturbances that impair ENDOPLASMIC RETICULUM function. It triggers many responses, including UNFOLDED PROTEIN RESPONSE, which may lead to APOPTOSIS; and AUTOPHAGY.
A type of endoplasmic reticulum lacking associated ribosomes on the membrane surface. It exhibits a wide range of specialized metabolic functions including supplying enzymes for steroid synthesis, detoxification, and glycogen breakdown. In muscle cells, smooth endoplasmic reticulum is called SARCOPLASMIC RETICULUM.
A lectin found in ENDOPLASMIC RETICULUM membranes that binds to specific N-linked OLIGOSACCHARIDES found on newly synthesized proteins. It may play role in PROTEIN FOLDING or retention and degradation of misfolded proteins in the endoplasmic reticulum.
One of the BASIC-LEUCINE ZIPPER TRANSCRIPTION FACTORS that is synthesized as a membrane-bound protein in the ENDOPLASMIC RETICULUM. In response to endoplasmic reticulum stress it translocates to the GOLGI APPARATUS. It is activated by PROTEASES and then moves to the CELL NUCLEUS to regulate GENETIC TRANSCRIPTION of GENES involved in the unfolded protein response.
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