期刊
KIDNEY INTERNATIONAL
卷 84, 期 1, 页码 25-33出版社
ELSEVIER SCIENCE INC
DOI: 10.1038/ki.2012.390
关键词
apoptosis; diabetes; endoplasmic reticulum-associated degradation; glomerulonephritis; podocyte; unfolded protein response
资金
- Canadian Institutes of Health Research [MOP-53264, MOP-84213]
- Kidney Foundation of Canada
- Catherine McLaughlin Hakim Chair
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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