Journal
KIDNEY INTERNATIONAL
Volume 84, Issue 1, Pages 25-33Publisher
ELSEVIER SCIENCE INC
DOI: 10.1038/ki.2012.390
Keywords
apoptosis; diabetes; endoplasmic reticulum-associated degradation; glomerulonephritis; podocyte; unfolded protein response
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Funding
- Canadian Institutes of Health Research [MOP-53264, MOP-84213]
- Kidney Foundation of Canada
- Catherine McLaughlin Hakim Chair
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Protein misfolding in the endoplasmic reticulum (ER) leads to ER stress. The unfolded protein response and ER-associated degradation (ERAD) interact in a coordinated manner with the ubiquitin-proteasome system and autophagy to alleviate protein misfolding or its consequences. The intersecting actions of these processes are evident in normal podocyte physiology, and in proteinuric glomerular diseases, including experimental membranous nephropathy, focal segmental sclerosis, and diabetic nephropathy. There is some evidence for the induction of ER stress, changes in the ubiquitin-proteasome system, and presence of autophagy in human glomerulopathies. Various therapeutic approaches to the unfolded protein response, ERAD, and the ubiquitin-proteasome system have corrected experimental glomerular diseases involving protein misfolding, and could potentially be developed as therapies in humans.
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