Relationship between sodium-dependent phosphate transporter (NaPi-IIc) function and cellular vacuole formation in opossum kidney cells

• Shiozaki Yuji

  Department of Molecular Nutrition, University of Tokushima Graduate School

• Segawa Hiroko

  Department of Molecular Nutrition, University of Tokushima Graduate School

• Ohnishi Saori

  Department of Molecular Nutrition, University of Tokushima Graduate School

• Ohi Akiko

  Department of Molecular Nutrition, University of Tokushima Graduate School

• Ito Mikiko

  Human Science and Environment, University of Hyogo Graduate School

• Kaneko Ichiro

  Department of Molecular Nutrition, University of Tokushima Graduate School

• Kido Shinsuke

  Laboratory of Clinical Nutrition, Department of Food Science and Nutrition, Kinki University Faculty of Agriculture

• Tatsumi Sawako

  Department of Molecular Nutrition, University of Tokushima Graduate School

• Miyamoto Ken-ichi

  Department of Molecular Nutrition, University of Tokushima Graduate School

抄録

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

収録刊行物

• The Journal of Medical Investigation

  The Journal of Medical Investigation 62 (3.4), 209-218, 2015

  国立大学法人　徳島大学医学部

キーワード

• proximal tubule
• SLC34A3
• opossum kidney cells
• proliferation
• vacuole

詳細情報

• CRID: 1390001204244191232
• NII論文ID: 130005099143
• NII書誌ID: AA11166929
• DOI: 10.2152/jmi.62.209
• ISSN: 13496867
• ISSN: 13431420
• PubMed: 26399350
• Web Site: https://www.jstage.jst.go.jp/article/jmi/62/3.4/62_209/_pdf
• Web Site: https://search.jamas.or.jp/link/ui/2016247015
• 本文言語コード: en
• データソース種別:
  • JaLC
  • Crossref
  • PubMed
  • CiNii Articles
  • KAKEN
• 抄録ライセンスフラグ: 使用不可