Evidence map›Paper›PMID 10866949›Full record

ArticleBiophysical journal2000

Proton-sensitive transitions of renal type II Na(+)-coupled phosphate cotransporter kinetics.

I C Forster, J Biber, H Murer

Abstract read
In one paragraph

Article in Biophysical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

19 citing papers in PubMed.

  1. Structures of the sodium-coupled phosphate importer SLC34A2 reveal a distinct architecture and gating mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
  3. Mechanisms of phosphate transport.Nature reviews. Nephrology · 2019
    Review
  4. Review
  5. Review
  6. Review
  7. Effect of Potassium Citrate on Calcium Phosphate Stones in a Model of Hypercalciuria.Journal of the American Society of Nephrology : JASN · 2015
    Article
  8. The SLC34 family of sodium-dependent phosphate transporters.Pflugers Archiv : European journal of physiology · 2014
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Renouncing electroneutrality is not free of charge: switching on electrogenicity in a Na+-coupled phosphate cotransporter.Proceedings of the National Academy of Sciences of the United States of America · 2005
    Article
  15. Article
  16. Essential cysteine residues of the type IIa Na+/Pi cotransporter.Pflugers Archiv : European journal of physiology · 2003
    Article
  17. Article
  18. Article
  19. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

I C ForsterInstitute of Physiology, University of Zurich, Zurich, Switzerland. forster@physiol.unizh.ch
J Biber
H Murer

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In the kidney proximal tubule, acidification of the glomerular filtrate leads to an inhibition of inorganic phosphate (P(i)) reabsorption by type II Na(+)-coupled cotransporters (NaPi-II). As external pH also alters the divalent/monovalent P(i) ratio, it has been difficult to separate putative proton interactions with the cotransporter from direct titration of divalent P(i), the preferred species transported. To distinguish between these possibilities and identify pH-sensitive transitions in the cotransport cycle, the pH-dependent kinetics of two NaPi-II isoforms, expressed in Xenopus laevis oocytes, were investigated electrophysiologically. At -50 mV, both isoforms showed >70% suppression of electrogenic response for an external pH change from 8.0 to 6.2, not attributable to titration of divalent P(i). This was accompanied by a progressive removal of steady-state voltage dependence. The NaPi-II-related uncoupled slippage current was unaffected by a pH change from 7.4 to 6.2, with no shift in the reversal potential, which suggested that protons do not function as substrate. The voltage-dependence of pre-steady-state relaxations was shifted to depolarizing potentials in 100 mM and 0 mM Na(ext)(+) and two kinetic components were resolved, the slower of which was pH-dependent. The changes in kinetics are predicted by a model in which protons interact with the empty carrier and final Na(+) binding step.

Indexed as

SymportersAcidsAnimalsCarrier ProteinsCells, CulturedFlounderHydrogen-Ion ConcentrationIon TransportKineticsOocytesPatch-Clamp TechniquesPhosphatesProtein IsoformsRatsSodiumSodium-Phosphate Cotransporter ProteinsAcidsCarrier ProteinsPhosphatesProtein IsoformsSodiumSodium-Phosphate Cotransporter ProteinsSodium-Phosphate Cotransporter Proteins, Type IISymporters

Identifiers

PMID10866949
PMCPMC1300927

What OpenQuestion holds

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Read underepoch 390

Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.