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首页> 外文期刊>American Journal of Physiology >Regulation of the energy sensor AMP-activated protein kinase in the kidney by dietary salt intake and osmolality.
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Regulation of the energy sensor AMP-activated protein kinase in the kidney by dietary salt intake and osmolality.

机译：饮食中盐的摄入量和重量摩尔渗透压浓度对肾脏能量传感器AMP激活的蛋白激酶的调节。

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摘要

The AMP-activated protein kinase (AMPK) is a key controller of cellular energy metabolism. We studied its expression and regulation by salt handling in the kidney. Immunoprecipitation and Western blots of protein lysates from whole rat kidney using subunit-specific antibodies showed that the alpha1-catalytic subunit is expressed in the kidney, associated with the beta2- and either gamma1- or gamma2-subunits. Activated AMPK, detected by immunohistochemical staining for phospho-Thr172 AMPK (pThr172), was expressed on the apical surface of the cortical thick ascending limb of the loop of Henle, including the macula densa, and some parts of the distal convoluted tubule. Activated AMPK was also expressed on the basolateral surface of the cortical and medullary collecting ducts as well as some portions of the distal convoluted tubules. AMPK activity was increased by 25% in animals receiving a high-salt diet, and this was confirmed by Western blotting for pThr172. Low-salt diets were associated with reduced levels of the alpha-subunit of AMPK, which was highly phosphorylated on Thr172. Surprisingly, both low- and high-salt media transiently activated AMPK in the macula densa cell line MMDD1, an effect due to changes in osmolality, rather than Na+ or Cl- concentration. This study, therefore, demonstrates regulation of AMPK by both a high- and a low-salt intake in vivo and suggests a role for the kinase in the response to changes in osmolality within the kidney.
机译：AMP激活的蛋白激酶（AMPK）是细胞能量代谢的关键控制器。我们通过肾脏中的盐处理研究了它的表达和调控。使用亚基特异性抗体从整个大鼠肾脏中进行蛋白质沉淀的免疫沉淀和蛋白质印迹分析表明，α1催化亚基在肾脏中表达，与β2和gamma1或gamma2亚基相关。通过免疫组织化学染色检测到的磷酸化Thr172 AMPK（pThr172）激活的AMPK，表达在Henle the的皮层厚上升肢的顶表面，包括黄斑部和远曲小管的某些部分。激活的AMPK还表达在皮质和髓样收集管的基底外侧表面以及远端曲旋小管的某些部分。接受高盐饮食的动物中AMPK活性提高了25％，这已通过Western blotting证实了pThr172。低盐饮食与AMPK的α亚基水平降低有关，后者在Thr172上高度磷酸化。令人惊讶的是，低盐和高盐培养基均短暂激活了黄斑部牙髓细胞系MMDD1中的AMPK，这是由于重量克分子渗透压浓度而不是Na +或Cl-浓度的变化所致。因此，这项研究证明了体内高盐和低盐摄入对AMPK的调节，并暗示了该激酶在肾脏内渗透压变化响应中的作用。

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