Heat shock protein expression in diabetic nephropathy

Barutta, Federica, Pinach, Silvia, Giunti, Sara, Vittone, Ferdinando, Forbes, Josephine M., Chiarle, Roberto, Arnstein, Maryann, Perin, Paolo Cavallo, Camussi, Giovanni, Cooper, Mark E. and Gruden, Gabriella (2008) Heat shock protein expression in diabetic nephropathy. American Journal of Physiology - Renal Physiology, 295 6: F1817-F1824. doi:10.1152/ajprenal.90234.2008


Author Barutta, Federica
Pinach, Silvia
Giunti, Sara
Vittone, Ferdinando
Forbes, Josephine M.
Chiarle, Roberto
Arnstein, Maryann
Perin, Paolo Cavallo
Camussi, Giovanni
Cooper, Mark E.
Gruden, Gabriella
Title Heat shock protein expression in diabetic nephropathy
Journal name American Journal of Physiology - Renal Physiology   Check publisher's open access policy
ISSN 0363-6127
1522-1466
Publication date 2008-12-01
Sub-type Article (original research)
DOI 10.1152/ajprenal.90234.2008
Open Access Status
Volume 295
Issue 6
Start page F1817
End page F1824
Total pages 8
Place of publication Bethesda, MD, United States
Publisher American Physiological Society
Language eng
Abstract Heat shock protein (HSP) HSP27, HSP60, HSP70, and HSP90 are induced by cellular stresses and play a key role in cytoprotection. Both hyperglycemia and glomerular hypertension are crucial determinants in the pathogenesis of diabetic nephropathy and impose cellular stresses on renal target cells. We studied both the expression and the phosphorylation state of HSP27, HSP60, HSP70, and HSP90 in vivo in rats made diabetic with streptozotocin and in vitro in mesangial cells and podocytes exposed to either high glucose or mechanical stretch. Diabetic and control animals were studied 4, 12, and 24 wk after the onset of diabetes. Immunohistochemical analysis revealed an overexpression of HSP25, HSP60, and HSP72 in the diabetic outer medulla, whereas no differences were seen in the glomeruli. Similarly, exposure neither to high glucose nor to stretch altered HSP expression in mesangial cells and podocytes. By contrast, the phosphorylated form of HSP27 was enhanced in the glomerular podocytes of diabetic animals, and in vitro exposure of podocytes to stretch induced HSP27 phosphorylation via a P38-dependent mechanism. In conclusion, diabetes and diabetes-related insults differentially modulate HSP27, HSP60, and HSP70 expression/phosphorylation in the glomeruli and in the medulla, and this may affect the ability of renal cells to mount an effective cytoprotective response. Copyright
Keyword Glomerular epithelial cells
Mechanical stretch
Mesangial cells
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Mater Research Institute-UQ (MRI-UQ)
School of Medicine Publications
 
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