A low-protein (LP) diet induces injury from energy depletion in renal epithelial cells. Overexpression of heat-shock proteins has been implicated in the restoration of the cytoskeletal anchorage of Na(+)/K(+)-ATPase. We tested if Hsp70 stabilizes renal Na(+)/K(+)-ATPase attachment to the cytoskeleton from the cortex and the outer stripe of the outer medulla (OSOM) in rats during recovery from a LP diet. Rats were fed with a LP diet (8% protein) for 14 days, and then the rats were recovered with a 24% protein (RP) diet. The control group received a 24% protein (NP) diet. Increased Na(+)/K(+)-ATPase dissociation was demonstrated in soluble fraction from OSOM with lower ATP content as a result of LP diet vs NP. Meanwhile, decreased Hsp70 levels in the same fraction were shown. Translocation of Hsp70 to the cytoskeletal injured fraction associated with stabilization of Na(+)/K(+)-ATPase was shown in OSOM from LP after in vitro co-incubation of the cytoskeletal fraction of LP and non-cytoskeletal fraction of RP. These effects were abolished by the addition of the anti-Hsp70 antibody. Absence of Na(+)/K(+)-ATPase detachment from its cytoskeletal anchorage was demonstrated in proximal duct segments from cortex in LP. Co-immunoprecipitation showed that the amount of Na(+)/K(+)-ATPase co-precipitating with Hsp70 increased in the OSOM as a result of the LP diet. In the cortex tissues from rats fed the LP and the RP diet, the interaction of both proteins were similar to the control groups. Our results indicate that Hsp70 has a critical role in protecting the integrity of the cytoskeletal anchorage of Na(+)/K(+)-ATPase during recovery from ATP-depleted injury resulting from LP in OSOM.

译文

:低蛋白(LP)饮食会因肾上皮细胞能量消耗而引起伤害。热休克蛋白的过表达与Na()/ K()-ATPase的细胞骨架锚定的恢复有关。我们测试了在从LP饮食中恢复过程中,Hsp70是否能稳定大鼠皮质和外延髓外条纹(OSOM)的肾Na()/ K()-ATPase与细胞骨架的附着。用低脂饮食(8%蛋白质)喂养大鼠14天,然后用24%蛋白质(RP)饮食恢复大鼠。对照组接受24%蛋白质(NP)饮食。由于LP日粮与NP日粮相比,在OSOM的可溶级分中具有较低的ATP含量,Na()/ K()-ATPase解离增加。同时,显示出相同分数的Hsp70水平降低。 Hsp70易位到与Na()/ K()-ATPase稳定相关的细胞骨架损伤部分,在LP的细胞骨架部分和RP的非细胞骨架部分体外共孵育后的OSOM中显示。通过加入抗Hsp70抗体消除了这些作用。缺乏Na()/ K()-ATPase脱离其细胞骨架锚固在LP皮质近端导管节段中。免疫共沉淀显示,LP饮食可导致OSOM中与Hsp70共沉淀的Na()/ K()-ATPase量增加。在饲喂LP和RP日粮的大鼠皮层组织中,两种蛋白质的相互作用与对照组相似。我们的结果表明,Hsp70在保护由OSOM中的LP引起的ATP耗尽损伤的恢复过程中,对保护Na()/ K()-ATPase的细胞骨架锚定的完整性具有至关重要的作用。

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