Altered hsp27 Expression in Nephrotic Syndrome
نویسندگان
چکیده
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 6 233%, x 6 SEM, P , 0.01 vs. control); ( b ) glomerular hsp27 protein expression (87 6 2%, P , 0.001 vs. control); and ( c ) glomerular hsp27 phosphorylation (101 6 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. ( J. Clin. Invest. 1996. 97:2697–2704.)
منابع مشابه
Hsp27 regulates podocyte cytoskeletal changes in an in vitro model of podocyte process retraction.
Nephrotic syndrome (NS) is characterized by structural changes in the actin-rich foot processes of glomerular podocytes. We previously identified high concentrations of the small heat shock protein hsp27 within podocytes as well as increased glomerular accumulation and phosphorylation of hsp27 in puromycin aminonucleoside (PAN) -induced experimental NS. Here we analyzed murine podocytes stably ...
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