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Updated: Jun 28, 2026

Comparative Proteomic Analysis of Whole Kidney, Medulla, and Cortical Tubules in Diabetic Pathogenesis of Kidney Injury in Mice
Published on: May 2, 2025
Heat shock protein expression in diabetic nephropathy
Federica Barutta1, Silvia Pinach, Sara Giunti
1Dept. of Internal Medicine, Univ. of Turin, Corso AM Dogliotti 14. Turin, 10126, Italy. federica.barutta@unito.it
Diabetic nephropathy involves cellular stress. Heat shock proteins (HSPs) like HSP27 are altered, with phosphorylated HSP27 increasing in podocytes, potentially impacting kidney cell protection.
Area of Science:
- Nephrology
- Cellular Biology
- Molecular Medicine
Background:
- Diabetic nephropathy is driven by hyperglycemia and glomerular hypertension, causing cellular stress in renal cells.
- Heat shock proteins (HSPs) are crucial for cytoprotection against cellular stress.
Purpose of the Study:
- To investigate the expression and phosphorylation of HSP27, HSP60, HSP70, and HSP90 in diabetic nephropathy.
- To examine HSP modulation in vivo in diabetic rats and in vitro in renal cells under stress.
Main Methods:
- Streptozotocin-induced diabetes in rats, with analysis at 4, 12, and 24 weeks.
- In vitro studies using mesangial cells and podocytes exposed to high glucose or mechanical stretch.
- Immunohistochemistry to assess HSP expression and phosphorylation states.
Main Results:
- HSP25, HSP60, and HSP72 were overexpressed in the outer medulla of diabetic rats, but not in glomeruli.
- High glucose or mechanical stretch did not alter HSP expression in mesangial cells or podocytes.
- Phosphorylated HSP27 was elevated in glomerular podocytes of diabetic animals; stretch induced HSP27 phosphorylation via a P38-dependent pathway in vitro.
Conclusions:
- Diabetes differentially affects HSP27, HSP60, and HSP70 expression and phosphorylation in renal glomeruli and medulla.
- These modulations in HSPs may influence the cytoprotective capacity of renal cells in diabetic nephropathy.
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