ATP releases HSP-72 from protein aggregates after renal ischemia. Am J Physiol 1998 Feb;274(2):F268-74
Date
03/05/1998Pubmed ID
9486221DOI
10.1152/ajprenal.1998.274.2.F268Scopus ID
2-s2.0-0031990584 (requires institutional sign-in at Scopus site) 55 CitationsAbstract
The pattern of 72-kDa heat-shock protein (HSP-72) induction after renal ischemia suggests a role in restoring cell structure. HSP-72 activity in the repair and release from denatured and aggregated proteins requires ATP. Protein aggregates were purified from normal and ischemic rat renal cortex. The addition of ATP to cortical homogenates reduced HSP-72, Na(+)-K(+)-ATPase, and actin in aggregates subsequently isolated, suggesting that their interaction is ATP dependent. Altering ATP hydrolysis in the purified aggregates, however, had different effects. ATP released HSP-72 during reflow and preserved Na(+)-K(+)-ATPase association with aggregates at 2 h but had no effect in controls or at 6 h reflow and caused no change in actin. These results indicate that HSP-72 complexes with aggregated cellular proteins in an ATP-dependent manner and suggests that enhancing HSP-72 function after ischemic renal injury assists refolding and stabilization of Na(+)-K(+)-ATPase or aggregated elements of the cytoskeleton, allowing reassembly into a more organized state.
Author List
Aufricht C, Lu E, Thulin G, Kashgarian M, Siegel NJ, Van Why SKAuthor
Scott K. Van Why MD Professor in the Pediatrics department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
ActinsAdenosine Triphosphate
Animals
Cell Membrane
Cytoskeleton
HSP72 Heat-Shock Proteins
Heat-Shock Proteins
Hydrolysis
Ischemia
Kidney
Male
Proteins
Rats
Rats, Sprague-Dawley
Reperfusion
Sodium-Potassium-Exchanging ATPase
