Analysis of different complexes of type IIa sodium-dependent phosphate transporter in rat renal cortex using blue-native polyacrylamide gel electrophoresis

• Tanimura Ayako

  Department of Clinical Nutrition, Institute of Health Biosciences, the University of Tokushima Graduate School

• Yamada Fumiyo

  Department of Clinical Nutrition, Institute of Health Biosciences, the University of Tokushima Graduate School

• Saito Akihito

  Department of Applied Molecular Medicine, Niigata University Graduate School of Medicine and Dental Sciences

• Ito Mikiko

  Department of Food Science and Nutrition, School of Human Science and Environment, University of Hyogo

• Kimura Toru

  Department of Pharmacology, School of Medicine, Kyorin University

• Anzai Naohiko

  Department of Pharmacology, School of Medicine, Kyorin University

• Horie Daisuke

  Department of Clinical Nutrition, Institute of Health Biosciences, the University of Tokushima Graduate School

• Yamamoto Hironori

  Department of Clinical Nutrition, Institute of Health Biosciences, the University of Tokushima Graduate School

• Miyamoto Ken-ichi

  Department of Molecular Nutrition, Institute of Health Biosciences, the University of Tokushima Graduate School

• Taketani Yutaka

  Department of Clinical Nutrition, Institute of Health Biosciences, the University of Tokushima Graduate School

• Takeda Eiji

  Department of Clinical Nutrition, Institute of Health Biosciences, the University of Tokushima Graduate School

Abstract

Type IIa sodium-dependent phosphate transporter (NaPi-IIa) can be localized in the apical plasma membrane of renal proximal tubule to carry out a rate-limiting step of phosphate reabsorption. For the apical localization, NaPi-IIa is required to form a macromolecular complex with some adaptor proteins such as Na⁺/H⁺ exchanger regulatory factor 1 (NHERF-1) and ezrin. However, the detail of macromolecular complex containing NaPi-IIa in the apical membrane of the renal proximal tubular cells has not been clarified. In this study, we identified at least four different complexes (220, 480, 920, 1,100 kDa) containing NaPi-IIa by using blue-native polyacrylamide gel electrophoresis. Interestingly, LC-MS/MS analysis and immunoprecipitation analysis reveal that megalin is a component of larger complexs (920 and 1,100 kDa). In addition, NaPi-IIa can be heterogeneously co-localized with ezrin and megalin on the apical membrane of renal proximal tubuler cells by fluorescence microscopy analysis. These results suggest that NaPi-IIa can form some different complexes on the apical plasma membrane of renal proximal tubular cells. J. Med. Invest. 58: 140-147, February, 2011

Journal

• The Journal of Medical Investigation

  The Journal of Medical Investigation 58 (1,2), 140-147, 2011

  The University of Tokushima Faculty of Medicine

Keywords

• native PAGE
• macromolecular complex
• NHERF1
• PDZK1
• megalin

Details

• CRID: 1390001204242910336
• NII Article ID: 130004465236
• NII Article ID: 80021578962
• NII Book ID: AA11166929
• DOI: 10.2152/jmi.58.140
• ISSN: 13496867
• ISSN: 13431420
• Web Site: http://repo.lib.tokushima-u.ac.jp/82750
• Web Site: http://www.jstage.jst.go.jp/article/jmi/58/1,2/58_1,2_140/_pdf
• Web Site: https://search.jamas.or.jp/link/ui/2012060865
• Text Lang: en
• Data Source:
  • JaLC
  • IRDB
  • Crossref
  • CiNii Articles
  • KAKEN
• Abstract License Flag: Disallowed