Ouabain-stimulated trafficking regulation of the Na/K-ATPase and NHE3 in renal proximal tubule cells

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• 作者：Yanling Yan (13)
  Steven Haller (1)
  Anna Shapiro (1)
  Nathan Malhotra (1)
  Jiang Tian (1)
  Zijian Xie (12)
  Deepak Malhotra (1)
  Joseph I. Shapiro (12)
  Jiang Liu (1) jiang.liu@utoledo.edu
• 关键词：Ouabain &#8211 ; Na/K ; ATPase signaling &#8211 ; Na/K ; ATPase &#8211 ; NHE3 &#8211 ; Redistribution
• 刊名：Molecular and Cellular Biochemistry
• 出版年：2012
• 出版时间：August 2012
• 年：2012
• 卷：367
• 期：1-2
• 页码：175-183
• 全文大小：664.8 KB
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• 作者单位：1. Department of Medicine, University of Toledo College of Medicine, Health Science Campus, 3000 Arlington Avenue, Toledo, OH 43614-2598, USA2. Department of Physiology and Pharmacology, University of Toledo College of Medicine, Toledo, OH, USA3. Institute of Biomedical Engineering, Yanshan University, Qinhuangdao, China
• ISSN：1573-4919

文摘

We have demonstrated that ouabain regulates protein trafficking of the Na/K-ATPase α1 subunit and NHE3 (Na/H exchanger, isoform 3) via ouabain-activated Na/K-ATPase signaling in porcine LLC-PK1 cells. To investigate whether this mechanism is species-specific, ouabain-induced regulation of the α1 subunit and NHE3 as well as transcellular 22Na+ transport were compared in three renal proximal tubular cell lines (human HK-2, porcine LLC-PK1, and AAC-19 originated from LLC-PK1 in which the pig α1 was replaced by ouabain-resistant rat α1). Ouabain-induced inhibition of transcellular 22Na+ transport is due to an ouabain-induced redistribution of the α1 subunit and NHE3. In LLC-PK1 cells, ouabain also inhibited the endocytic recycling of internalized NHE3, but has no significant effect on recycling of endocytosed α1 subunit. These data indicated that the ouabain-induced redistribution of the α1 subunit and NHE3 is not a species-specific phenomenon, and ouabain-activated Na/K-ATPase signaling influences NHE3 regulation.