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Research Article Free access | 10.1172/JCI118723

Altered expression of glomerular heat shock protein 27 in experimental nephrotic syndrome.

W E Smoyer, A Gupta, P Mundel, J D Ballew, and M J Welsh

Department of Pediatrics, University of Michigan, Ann Arbor 48109, USA. william.smoyer@umich.edu

Find articles by Smoyer, W. in: PubMed | Google Scholar

Department of Pediatrics, University of Michigan, Ann Arbor 48109, USA. william.smoyer@umich.edu

Find articles by Gupta, A. in: PubMed | Google Scholar

Department of Pediatrics, University of Michigan, Ann Arbor 48109, USA. william.smoyer@umich.edu

Find articles by Mundel, P. in: PubMed | Google Scholar

Department of Pediatrics, University of Michigan, Ann Arbor 48109, USA. william.smoyer@umich.edu

Find articles by Ballew, J. in: PubMed | Google Scholar

Department of Pediatrics, University of Michigan, Ann Arbor 48109, USA. william.smoyer@umich.edu

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Published June 15, 1996 - More info

Published in Volume 97, Issue 12 on June 15, 1996
J Clin Invest. 1996;97(12):2697–2704. https://doi.org/10.1172/JCI118723.
© 1996 The American Society for Clinical Investigation
Published June 15, 1996 - Version history
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Abstract

Although nephrotic syndrome is a very common kidney disease, little is known about the molecular changes occurring within glomerular capillary loops during development of disease. The characteristic histologic change is retraction (effacement) of the distal "foot" processes of glomerular epithelial cells (GEC) which surround the capillary loops. The GEC foot processes are an essential part of the kidney's filtration barrier, and their structure is regulated primarily by actin microfilaments, cytoskeletal proteins present in high concentrations in foot processes. Actin polymerization has been reported to be regulated via phosphorylation of the low molecular weight heat shock protein, hsp27. We localized hsp27 within normal rat GECs using immunofluorescence and immunoelectron microscopy. Induction of nephrotic syndrome and GEC foot process effacement using the puromycin aminonucleoside rat model resulted in significant increases in: (a) renal cortical hsp27 mRNA expression (826 +/- 233%, x +/- SEM, P < 0.01 vs. control); (b) glomerular hsp27 protein expression (87 +/- 2%, P < 0.001 vs. control); and (c) glomerular hsp27 phosphorylation (101 +/- 32%, P < 0.05 vs. control). These findings support the hypothesis that hsp27, by regulating GEC foot process actin polymerization, may be important in maintaining normal foot process structure, and regulating pathophysiologic GEC cytoskeletal changes during development of nephrotic syndrome.

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