Relationship between sodium-dependent phosphate transporter (NaPi-IIc) function and cellular vacuole formation in opossum kidney cells
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- Shiozaki Yuji
- Department of Molecular Nutrition, University of Tokushima Graduate School
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- Segawa Hiroko
- Department of Molecular Nutrition, University of Tokushima Graduate School
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- Ohnishi Saori
- Department of Molecular Nutrition, University of Tokushima Graduate School
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- Ohi Akiko
- Department of Molecular Nutrition, University of Tokushima Graduate School
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- Ito Mikiko
- Human Science and Environment, University of Hyogo Graduate School
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- Kaneko Ichiro
- Department of Molecular Nutrition, University of Tokushima Graduate School
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- Kido Shinsuke
- Laboratory of Clinical Nutrition, Department of Food Science and Nutrition, Kinki University Faculty of Agriculture
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- Tatsumi Sawako
- Department of Molecular Nutrition, University of Tokushima Graduate School
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- Miyamoto Ken-ichi
- Department of Molecular Nutrition, University of Tokushima Graduate School
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Abstract
NaPi-IIc/SLC34A3 is a sodium-dependent inorganic phosphate (Pi) transporter in the renal proximal tubules and its mutations cause hereditary hypophosphatemic rickets with hypercalciuria (HHRH). In the present study, we created a specific antibody for opossum SLC34A3, NaPi-IIc (oNaPi-IIc), and analyzed its localization and regulation in opossum kidney cells (a tissue culture model of proximal tubular cells). Immunoreactive oNaPi-IIc protein levels increased during the proliferative phase and decreased during differentiation. Moreover, stimulating cell growth upregulated oNaPi-IIc protein levels, whereas suppressing cell proliferation downregulated oNaPi-IIc protein levels. Immunocytochemistry revealed that endogenous and exogenous oNaPi-IIc proteins localized at the protrusion of the plasma membrane, which is a phosphatidylinositol 4,5-bisphosphate (PIP2) rich-membrane, and at the intracellular vacuolar membrane. Exogenous NaPi-IIc also induced cellular vacuoles and localized in the plasma membrane. The ability to form vacuoles is specific to electroneutral NaPi-IIc, and not electrogenic NaPi-IIa or NaPi-IIb. In addition, mutations of NaPi-IIc (S138F and R468W) in HHRH did not cause cellular PIP2-rich vacuoles. In conclusion, our data anticipate that NaPi-IIc may regulate PIP2 production at the plasma membrane and cellular vesicle formation. J. Med. Invest. 62: 209-218, August, 2015
Journal
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- The Journal of Medical Investigation
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The Journal of Medical Investigation 62 (3.4), 209-218, 2015
The University of Tokushima Faculty of Medicine
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Details 詳細情報について
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- CRID
- 1390001204244191232
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- NII Article ID
- 130005099143
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- NII Book ID
- AA11166929
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- ISSN
- 13496867
- 13431420
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- PubMed
- 26399350
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- Text Lang
- en
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- Data Source
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- JaLC
- Crossref
- PubMed
- CiNii Articles
- KAKEN
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- Abstract License Flag
- Disallowed