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C-peptide ameliorates high glucose-induced podocyte dysfunction through the regulation of the Notch and TGF-β signaling pathways.
- Source :
-
Peptides . Aug2021, Vol. 142, pN.PAG-N.PAG. 1p. - Publication Year :
- 2021
-
Abstract
- • Islet transplantation was superior to mere insulin therapy in diabetic nephropathy protection. • C-peptide suppressed high glucose-induced epithelial-mesenchymal transition and renal fibrosis in podocytes. • C-peptide ameliorated high-glucose induced podocyte injury via down-regulating the Notch and TGF-β signaling pathways. The podocyte is one of the main components of the glomerular filtration barrier in the kidney, and its injury may contribute to proteinuria, glomerulosclerosis and eventually kidney failure. C-peptide, a cleavage product of proinsulin, shows therapeutic potential for treating diabetic nephropathy (DN). The aim of this study was to investigate the effect of C-peptide on high glucose-induced podocyte dysfunction. In the present study, we found that the protective effects of islet transplantation were superior to simple insulin therapy for the treatment of DN in streptozotocin (STZ)-treated rats. And such superiority may due to the function of C-peptide secreted at the implanted site. Based on this background, we determined that the application of C-peptide significantly prevented high glucose-induced podocyte injury by increasing the expression of nephrin and synaptopodin. Meanwhile, C-peptide suppressed high glucose-induced epithelial-mesenchymal transition (EMT) and renal fibrosis via decreasing the expression of snail, vimentin, α-smooth muscle actin (α-SMA) and connective tissue growth factor (CTGF). Moreover, the Notch and transforming growth factor-β (TGF-β) signaling pathways were activated by high glucose, and treatment with C-peptide down-regulated the expression of the Notch signaling molecules Notch 1 and Jagged 1 and the TGF-β signaling molecule TGF-β1. These findings suggested that C-peptide might serve as a novel treatment method for DN and podocyte dysfunction. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 01969781
- Volume :
- 142
- Database :
- Academic Search Index
- Journal :
- Peptides
- Publication Type :
- Academic Journal
- Accession number :
- 151216896
- Full Text :
- https://doi.org/10.1016/j.peptides.2021.170557