Results 361 to 370 of about 462,885 (376)

Endoplasmic Reticulum Stress in Immunity

Annual Review of Immunology, 2015
Immune responses occur in the midst of a variety of cellular stresses that can severely perturb endoplasmic reticulum (ER) function. The unfolded protein response is a three-pronged signaling axis dedicated to preserving ER homeostasis. In this review, we highlight many important and emerging functional roles for ER stress in immunity, focusing on how ...
Laurie H. Glimcher, Sarah E. Bettigole
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Parkin and Endoplasmic Reticulum Stress

Annals of the New York Academy of Sciences, 2003
Abstract: Autosomal‐recessive juvenile parkinsonism (AR‐JP) is caused by mutations in the parkin gene. Parkin protein is characterized by a ubiquitin‐like domain at its NH2 terminus and by two RING finger motifs and one IBR (in between RING finger) motif at its COOH‐terminus (RING‐IBR‐RING). We showed that the parkin protein is an E3 ubiquitin ligase,
Ryosuke Takahashi, Yuzuru Imai, Yoshikuni Mizuno, Nobutaka Hattori   +3 more
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InterfERing with endoplasmic reticulum stress

Trends in Pharmacological Sciences, 2012
Stress to the endoplasmic reticulum (ER) is a recognized factor in Alzheimer's and Parkinson's diseases, diabetes, heart disease, liver disorders and cancer. Thus, drugs that interfere with ER stress have wide therapeutic potential. Here we review the effects of drugs on three arms of ER stress: the protein kinase RNA-activated (PKR)-like ER kinase ...
Una FitzGerald, Honorata Kraskiewicz
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Endoplasmic reticulum stress, obesity and diabetes [PDF]

Trends in Molecular Medicine, 2012
The endoplasmic reticulum (ER) stress response, also commonly known as the unfolded protein response (UPR), is an adaptive response used to align ER functional capacity with demand. It is activated in various tissues under conditions related to obesity and type 2 diabetes. Hypothalamic ER stress contributes to inflammation and leptin/insulin resistance.
Fabienne Foufelle, Licio A. Velloso, Miriam Cnop, Miriam Cnop   +3 more
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Endoplasmic Reticulum Stress and Obesity

2017
In recent years, the world has seen an alarming increase in obesity and is closely associated with insulin resistance, which is a state of low-grade inflammation, the latter characterized by elevated levels of proinflammatory cytokines in blood and tissues.
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Resveratrol treatment in patients with polycystic ovary syndrome decreased pro‐inflammatory and endoplasmic reticulum stress markers

American Journal of Reproductive Immunology, 2020
Polycystic ovary syndrome (PCOS) is associated with endoplasmic reticulum (ER) stress and pro‐inflammatory condition. The aim of the present study was to evaluate the effect of resveratrol treatment on pro‐inflammatory and ER stress markers in patients ...
Samaneh Brenjian, A. Moini, N. Yamini, L. Kashani, Maryam Faridmojtahedi, Mojdeh Bahramrezaie, Mahshad Khodarahmian, F. Amidi   +7 more
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Sensing Endoplasmic Reticulum Stress

2012
This chapter provides an overview of our present understanding of mechanisms of sensing protein folding status and endoplasmic reticulum (ER) stress in eukaryotic cells. The ER folds and matures most secretory and transmembrane proteins. Mis- or unfolded proteins are sensed by specialized ER stress sensors, such as IRE1, PERK and ATF6, which initiate ...
Martin Schröder, Vipul M. Parmar
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Endoplasmic reticulum stress in the kidney

Clinical and Experimental Nephrology, 2008
Endoplasmic reticulum (ER) stress is involved in a wide range of pathological circumstances including neurodegenerative disorders, diabetes mellitus, ischemic injury, cancers, atherosclerosis, inflammation, infection, toxicity of chemicals and metals, and psychotic diseases.
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Endoplasmic reticulum stress responses

Cellular and Molecular Life Sciences, 2007
In homeostasis, cellular processes are in a dynamic equilibrium. Perturbation of homeostasis causes stress. In this review I summarize how perturbation of three major functions of the endoplasmic reticulum (ER) in eukaryotic cells -- protein folding, lipid and sterol biosynthesis, and storing intracellular Ca(2+) -- causes ER stress and activates ...
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Endoplasmic Reticulum Stress in Disease

2016
Proper protein folding in the endoplasmic reticulum (ER) is subject to alterations in the extracellular, as well as the intracellular environment. The accumulation of misfolded proteins in the ER activates the unfolded protein response (UPR), a collection of adaptive signaling pathways that are essential to maintain protein-folding homeostasis in all ...
R. J. Kaufman, L. Popolo
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