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首页> 美国卫生研究院文献>Cell Stress Chaperones >Na+/K+-ATPase stabilization by Hsp70 in the outer stripe of the outer medulla in rats during recovery from a low-protein diet
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Na+/K+-ATPase stabilization by Hsp70 in the outer stripe of the outer medulla in rats during recovery from a low-protein diet

机译：低蛋白饮食恢复过程中大鼠外延髓外条纹中Hsp70对Na + / K + -ATPase的稳定作用

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摘要

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.
机译：低蛋白（LP）饮食会因肾上皮细胞能量消耗而引起损伤。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Hsp70在恢复过程中是否能使大鼠肾脏Na + / K + -ATPase与皮质和外延髓外条纹（OSOM）的细胞骨架稳定LP饮食。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。 LP饮食与NP相比，OSOM可溶部分的Na + / K + -ATPase解离增加。同时，显示出相同分数的Hsp70水平降低。在LP的OSOM中，将Hsp70易位到与Na + / K + -ATPase稳定相关的细胞骨架损伤部分，并对其进行了体外共孵育。 LP和RP的非细胞骨架部分。通过加入抗Hsp70抗体消除了这些作用。 LP皮质近端管段显示Na + / K + -ATPase脱离细胞骨架锚定。共免疫沉淀表明，LP饮食导致OSOM中与Hsp70共同沉淀的Na + / K + -ATPase的量增加。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Na + / K + -ATPase的细胞骨架锚定的完整性过程中起着至关重要的作用，该过程在由LP引起的ATP耗竭损伤的恢复中起作用。 OSOM。

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