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Open AccessJournal ArticleDOI

Albumin induces endoplasmic reticulum stress and apoptosis in renal proximal tubular cells

TLDR
Results indicate that renal tubular cells exposed to high protein load suffer from ER stress, and ER stress may subsequently lead to tubular damage by activation of caspase-12.
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This article is published in Kidney International.The article was published on 2006-10-02 and is currently open access. It has received 188 citations till now. The article focuses on the topics: Unfolded protein response & Endoplasmic reticulum.

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Adult Minimal-Change Disease: Clinical Characteristics, Treatment, and Outcomes

TL;DR: In this referral MCD population, response to daily and alternate-day steroids is similar, but second-line agents give greater response in patients who are steroid dependent, and remissions were more likely to be complete in steroid-dependent patients.
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Autophagy in diabetic nephropathy.

TL;DR: Findings suggest the possibility that autophagy can be a therapeutic target against diabetic nephropathy, and discuss the major nutrient-sensing signal pathways and diabetes-induced altered intracellular metabolism and cellular events.
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Proteinuria and Hyperglycemia Induce Endoplasmic Reticulum Stress

TL;DR: Observations suggest that in proteinuric diseases, tubular epithelial cells undergo ER stress, which induces an adaptive, protective UPR, which may protect the cells from ER stress but persistence of hyperglycemia and proteinuria may eventually lead to apoptosis.
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Proteostasis in endoplasmic reticulum—new mechanisms in kidney disease

TL;DR: Restoration of normal proteostasis holds promise in protecting the kidney from pathogenic stresses as well as ageing, and accumulating evidence provides a link between the UPR pathway and mitochondrial structure and function, indicating the important role of ER protestasis in the maintenance of mitochondrial homeostasis.
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Endoplasmic reticulum stress and unfolded protein response in renal pathophysiology: Janus faces.

TL;DR: Current knowledge on the relationship between ER stress and diseases is described and evidence for the link between ER Stress/UPR and renal diseases is summarized.
References
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Journal ArticleDOI

Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta.

TL;DR: It is shown that caspase-12 is localized to the ER and activated by ER stress, including disruption of ER calcium homeostasis and accumulation of excess proteins in ER, but not by membrane- or mitochondrial-targeted apoptotic signals, which may contribute to amyloid-β neurotoxicity.
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Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controls

TL;DR: What is presently known about the diversity of molecular signaling mechanisms that coordinate the complex ER stress response at the translational and transcriptional level in yeast and in higher eukaryotic cells is summarized.
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Orchestrating the unfolded protein response in health and disease

TL;DR: As the authors gain a greater understanding of the mechanisms that control UPR activation, it should be possible to discover methods to activate or inhibit the UPR as desired for therapeutic benefit.
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Coupling endoplasmic reticulum stress to the cell death program.

TL;DR: It is hoped that dissection of the molecular components and pathways that alter ER structure and function and ultimately promote cellular death will provide a framework for understanding degenerative disorders that feature misfolded proteins.
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Pathophysiology of Progressive Nephropathies

TL;DR: In patients with renal diseases characterized by proteinuria, the initial insult to the kidney is usually followed by a progressive decline in the glomerular filtration rate, which is thought to be due to changes in renal hemodynamics initiated by the loss of nephrons.
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