Sodium-dependent phosphate transport by apical membrane vesicles from a cultured renal epithelial cell line (LLC-PK 1 )
Biochimica et Biophysica Acta (BBA) - Biomembranes, ISSN: 0005-2736, Vol: 769, Issue: 2, Page: 471-478
1984
- 39Citations
- 1Captures
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Metrics Details
- Citations39
- Citation Indexes39
- CrossRef39
- 32
- Captures1
- Readers1
Article Description
Apical membrane vesicles were prepared from confluent monolayers of LLC-PK 1 cells grown upon microcarrier beads. The final membrane preparation, obtained by a modified divalent cation precipitation technique, was enriched in alkaline phosphatase, leucine aminopeptidase and trehalase (8-fold compared to the initial homogenate). Analysis of phosphate uptake into the vesicles identified a specific sodium-dependent pathway. Lithium and other cations were unable to replace sodium. At 100 mmol/l sodium and pH 7.4, an apparent Km for phosphate of 99 ± 19 μmol/l and an apparent Ki for arsenate of 1.9 mmol/l were found. Analysis of the sodium activation of phosphate uptake gave an apparent Km for sodium of 32 ± 12 mmol/l and suggested the involvement of two sodium ions in the transport mechanism. Sodium modified the apparent Km of the transport system for phosphate. The rate of sodium-dependent phosphate uptake was higher at pH 6.4 than at pH 7.4. At both pH values, an inside negative membrane potential (potassium gradient plus valinomycin) had no stimulatory effect on the rate of the sodium-dependent component of phosphate uptake. It is concluded that the apical membrane of LLC-PK 1 cells contains a sodium-phosphate cotransport system with a stoichiometry of 2 sodium ions: 1 phosphate anion.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/0005273684903328; http://dx.doi.org/10.1016/0005-2736(84)90332-8; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0021352505&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/6696895; https://linkinghub.elsevier.com/retrieve/pii/0005273684903328; http://dx.doi.org/10.1016/0005-2736%2884%2990332-8; https://dx.doi.org/10.1016/0005-2736%2884%2990332-8
Elsevier BV
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