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Am J Physiol Renal Physiol 288: F1236-F1242, 2005. First published February 8, 2005; doi:10.1152/ajprenal.00438.2004
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HSP70 binding modulates detachment of Na-K-ATPase following energy deprivation in renal epithelial cells

Michael Riordan,1 Rajasree Sreedharan,1 Shirley Wang,2 Gunilla Thulin,1 Andrea Mann,3 Michael Stankewich,3 Scott Van Why,4 Michael Kashgarian,3 and Norman J. Siegel1

1Department of Pediatrics, 2Magnetic Resonance Research Center, 3Department of Pathology, and 4Department of Pediatrics, Medical College of Wisconsin, Milwaukee, Wisconsin

Submitted 8 December 2004 ; accepted in final form 3 February 2005

The molecular mechanisms associated with reestablishment of renal epithelial polarity after injury remain incompletely delineated. Stress proteins may act as molecular chaperones, potentially modulating injury or enhancing recovery. We tested whether overexpression of heat shock protein 70 (HSP70) would stabilize Na-K-ATPase attachment to the cytoskeleton, under conditions of ATP depletion, and whether a direct association existed between Na-K-ATPase and HSP70 in cultured renal epithelial cells. LLC-PK1 cells were transfected with a tagged HSP70 (70FLAG) or vector alone (VA). Detachment of Na-K-ATPase was detected in Triton soluble lysate after ATP depletion. 70FLAG cells demonstrated a significant (P < 0.01) decrease in detachment of Na-K-ATPase after either 2 or 4 h of ATP depletion. Interactions between HSP70 and Na-K-ATPase were determined by coimmunoprecipitation of 70FLAG and Na-K-ATPase, by direct and competitive binding assays and by immunocytochemical localization. Binding of HSP70 and Na-K-ATPase increased dramatically following injury. Interactions were: 1) reversible; 2) reciprocal to changes in the HSP70 binding protein clathrin; and 3) present only when ATP turnover was inhibited in cell lysate, an established characteristic of HSP binding. These studies indicate that 1) overexpression of HSP70 is associated with decreased detachment of Na-K-ATPase from the cytoskeleton following injury; 2) HSP70 binds to Na-K-ATPase; and 3) binding of HSP70 to Na-K-ATPase is dynamic and specific, increasing in response to injury and decreasing during recovery. Interaction between the molecular chaperone HSP70 and damaged or displaced Na-K-ATPase may represent a fundamental cellular mechanism underlying maintenance and recovery of renal tubule polarity following energy deprivation.

cytoprotection; renal cell injury; immunoprecipitation of HSP70; immunoprecipitation of Na-K-ATPase; overexpression of HSP70


Address for reprint requests and other correspondence: N. J. Siegel, Dept. of Pediatrics, Yale Univ. School of Medicine, PO Box 208064, New Haven, CT 06520-8064 (E-mail: norman.siegel{at}yale.edu)




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