Ischemic Conditioning Prevents Na,K-ATPase Dissociation from the Cytoskeletal Cellular Fraction after Repeat Renal Ischemia in Rats

Aufricht, Christoph

doi:10.1203/01.pdr.0000015128.65800.28

Cited by 12 publications

(21 citation statements)

References 13 publications

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“…Although enhancement of Na + -pump activity in IPC hearts had been previously described [8,9,13,26,34], the mechanism remained unknown. Lundmark et al attributed the enhancement to a better preservation of ATP during ischemia in IPC.…”

Section: Na + /K + -Atpase Activity In Ipc Heartsmentioning

confidence: 98%

“…Recently, we demonstrated that Na + /K + -ATPase activity is impaired during early reperfusion after prolonged ischemia and that this effect may be explained by calpainmediated degradation of the anchorage that fixes Na + /K + -ATPase to the membrane cytoskeleton (ankyrin) and the membrane cytoskeleton itself (fodrin) [12]. Previously, Aufricht et al described that IPC prevents dissociation of Na + /K + -ATPase from its cytoskeletal anchorage in rat renal cortex after ischemia [13], and we have demonstrated in isolated rat hearts that IPC attenuates calpain-mediated degradation of structural proteins including fodrin and ankyrin in a PKA-dependent manner and that the administration of calpain inhibitors mimicked in part the protective effects of IPC against cell death [3].…”

Section: Introductionmentioning

confidence: 95%

See 1 more Smart Citation

Ischemic preconditioning prevents calpain-mediated impairment of Na+/K+-ATPase activity during early reperfusion☆

Inserte

Garcı́a-Dorado

Hernando

et al. 2006

Cardiovascular Research

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Section: Na + /K + -Atpase Activity In Ipc Heartsmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 95%

Ischemic preconditioning prevents calpain-mediated impairment of Na+/K+-ATPase activity during early reperfusion☆

Inserte

Garcı́a-Dorado

Hernando

et al. 2006

Cardiovascular Research

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“…Kidneys were decapsulated in chilled isotonic solution and the cortex was dissected out. Cortical tissues were homogenized in chilled extraction buffer [13] containing 60 mM piperazine-N,N′-bis(2-ethanesulfonic acid) (PIPES), 1 mM ethylene glycol-bis(β-aminoethyl ether)-N,N,N′,N′-tetraacetic acid (EGTA), 1 mM EDTA, 100 mM NaCl, pH 6.9 with 0.1% Triton X-100, 0.5 mM phenylmethyl sulfonyl fluoride, and 0.1 mM dithiothreitol in a motor-driven Teflon-glass Potter homogenizer. The homogenates were centrifuged at 680 g for 10 min at 4°to remove large cellular fragments and nuclei.…”

Section: Histopathological Studiesmentioning

confidence: 99%

“…Triton X-100 extractability fractionates the cellular pool of Na + /K + ATPase into an insoluble pellet (cytoskeleton-associated) and a soluble supernatant [11]. Detachment of Na + /K + ATPase from its cytoskeletal anchorage to the basolateral membrane has been used as a marker of cellular integrity [11][12][13].…”

Section: Introductionmentioning

confidence: 99%

Heat shock protein 70 induction and its urinary excretion in a model of acetaminophen nephrotoxicity

et al. 2010

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Acetaminophen (APAP) is an analgesic-antipyretic drug widely used in children. In the present study, we used an in vivo model of APAP-induced nephrotoxicity in male Wistar rats. We analyzed whether toxic doses of APAP could induce heat shock protein 70 (HSP70) in the kidney and whether HSP70 could be detected in urine. Renal function and histological evaluation of the kidneys were performed at different times after APAP administration (1,000 mg/kg body weight i.p.). Cellular injury was assessed by Triton X-100 solubilization of Na(+)/K(+) ATPase. Renal and hepatic glutathione levels were also measured. Urinary N-acetyl-beta-D glucosaminidase (NAG) excretion increased 4 h after intoxication. At this time, urea and creatinine were at control levels and a slight degree of histological alteration was detected. Kidney microscopic evaluation, Na(+)/K(+) ATPase solubility, creatinine, and urea levels and NAG excretion did not differ from those of controls 48 h after APAP administration. HSP70 was detected in urine obtained from 4 to 24 h after APAP administration. HSP70 abundance in renal cortex was increased at early time points and 48 h after APAP administration. Urinary HSP70 excretion would be a marker of its renal induction combined with the loss of tubule integrity. NAG would be a suitable early biomarker of APAP-induced nephrotoxicity.

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“…This increased resistance to repeat cellular injury is called cytoprotection; the treatment resulting in this cytoprotection is termed conditioning [48]. Based on this approach it was shown that in vivo pretreatment with renal ischemia (ischemic conditioning) not only induces HSP but also prevents cytoskeletal disruption in rat renal cortex after repeat ischemia [49,50]. This stabilization was abolished by blocking antibodies against HSP ex vivo.…”

Section: Hsp In Renal Ischemiamentioning

confidence: 99%

Heat-shock protein 70: molecular supertool?

Aufricht

2005

Pediatr Nephrol

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The cellular stress response decreases cellular injury, either via primary induction of cytoresistance or by secondary enhancement of cellular repair mechanisms. The most frequently studied and best understood effectors of the cellular stress response are the heat shock proteins (HSP). HSP are among the oldest tools in the cellular protein machinery, demonstrating extremely high conservation of the genetic code since bacteria. Molecular chaperons, with the HSP-70 being the prototype, cooperate in transport and folding of proteins, preventing aggregation, and even resolubilizing injured proteins. Increasing evidence supports a role for HSP during the recovery from renal ischemia, in particular in cellular salvage from apoptotic cell death and cytoskeletal restoration. Recent studies also report the potential for biomolecular profiling of newborns for the risk of acute renal failure. In peritoneal dialysis novel data suggest the use of HSP expression for biocompatibility testing. More importantly, HSP are prime therapeutic candidates for clinical situations associated with predictable insults, such as organ procurement in transplant medicine and repetitive exposure to hyperosmolar and acidotic peritoneal dialysis fluids. The next challenge will be to define the regulatory pathways of the cellular stress response in these models to introduce novel therapeutic interventions, such as new pharmaceutics enhancing the HSP expression.

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Ischemic Conditioning Prevents Na,K-ATPase Dissociation from the Cytoskeletal Cellular Fraction after Repeat Renal Ischemia in Rats

Cited by 12 publications

References 13 publications

Ischemic preconditioning prevents calpain-mediated impairment of Na+/K+-ATPase activity during early reperfusion☆

Ischemic preconditioning prevents calpain-mediated impairment of Na+/K+-ATPase activity during early reperfusion☆

Heat shock protein 70 induction and its urinary excretion in a model of acetaminophen nephrotoxicity

Heat-shock protein 70: molecular supertool?

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