ID | 82750 |
Author |
Tanimura, Ayako
Department of Clinical Nutrition, Institute of Health Biosciences, the University of Tokushima Graduate School
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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
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Miyamoto, Ken-ichi
Department of Molecular Nutrition, Institute of Health Biosciences, the University of Tokushima Graduate School
Tokushima University Educator and Researcher Directory
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Taketani, Yutaka
Department of Clinical Nutrition, Institute of Health Biosciences, the University of Tokushima Graduate School
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Takeda, Eiji
Department of Clinical Nutrition, Institute of Health Biosciences, the University of Tokushima Graduate School
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|
Keywords | native PAGE
macromolecular complex
NHERF1
PDZK1
megalin
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Content Type |
Journal Article
|
Description | 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. |
Journal Title |
The journal of medical investigation : JMI
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ISSN | 13431420
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NCID | AA11166929
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Volume | 58
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Issue | 1-2
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Start Page | 140
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End Page | 147
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Sort Key | 140
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Published Date | 2011-02
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Remark | The journal of medical investigation : http://medical.med.tokushima-u.ac.jp/jmi/index.html
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EDB ID | |
FullText File | |
language |
eng
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departments |
Oral Sciences
Medical Sciences
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