Evidence map›Paper›PMID 21691088›Full record

ArticleCellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology2011

Role of vacuolar ATPase in the trafficking of renal type IIa sodium-phosphate cotransporter.

Aamir Ahmad, Syed J Khundmiri, Francesca Pribble, Michael L Merchant, Mohammed Ameen, Jon B Klein, Moshe Levi, Eleanor D Lederer

Open access · bronzeAbstract read
In one paragraph

Article in Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.7field-weighted citation impact, top 31% of its field
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

3 citing papers in PubMed, 8 citations in OpenAlex.

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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

8 authors at 2 institutions in 1 country.

Aamir AhmadDepartment of Medicine, University of Louisville, Louisville, KY 40202, USA.
Syed J Khundmiri
Francesca Pribble
Michael L Merchant
Mohammed Ameen
Jon B Klein
Moshe Levi
Eleanor D Lederer
University of Louisville · USUniversity of Colorado Health · US

Funding

Regulation of Renal Phosphate Transport by LipidsR01DK066029 · NIDDK · UNIVERSITY OF COLORADO DENVER · PI LEVI, MOSHE · 2005 to 2013
$3.2M
NIDDK NIH HHS 1 R01 DK066029NIDDK NIH HHS R01 DK066029
6 · The paper itself

Abstract

BACKGROUND/

aimsTotal body phosphate homeostasis is regulated by expression of type IIa sodium phosphate cotransporter (NpT2a) in the apical membrane (BBM) of renal proximal tubule cells. NpT2a expression is regulated by dietary phosphate and PTH but the mechanisms for trafficking of the protein are unknown. Based on 2D gel electrophoresis and mass spectroscopy data that changes in dietary phosphate stimulated changes in BBM expression of vacuolar H(+)-ATPase, we hypothesized that vacuolar H(+)-ATPase plays a significant role in regulation of NpT2a in opossum kidney (OK) cells, a model for renal proximal tubule transport.

methodsRole of vacuolar H(+)-ATPase was studied in opossum kidney (OK) cells by examining the effect of inhibition of vacuolar H(+)-ATPase on Pi uptake and NpT2a expression.

resultsPretreatment of OK cells with bafilomycin A(1) and concanamycin A, inhibitors of vacuolar H(+)-ATPases, blocked high phosphate- and PTH-induced degradation of NpT2a, but had no effect on high phosphate or PTH induced inhibition of sodium-dependent phosphate transport. Exposure of the cells to bafilomycin A(1) significantly decreased phosphate transport and apical membrane expression of NpT2a. Treatment with brefeldin A, an inhibitor of Golgi transport, decreased phosphate transport and apical membrane expression of NpT2a while treatment of cells with both brefeldin A and bafilomycin A(1) had no additive effect.

conclusionWe conclude that vacuolar H(+)-ATPase plays a significant role in exocytosis of NpT2a into the apical membrane and in degradation of NpT2a but has no role in endocytosis.

Indexed as

AnimalsCells, CulturedElectrophoresis, Gel, Two-DimensionalKidneyMaleProtein TransportRatsRats, Sprague-DawleySodium-Phosphate Cotransporter ProteinsSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationVacuolar Proton-Translocating ATPasesSodium-Phosphate Cotransporter ProteinsVacuolar Proton-Translocating ATPases

Identifiers

PMID21691088
PMCPMC3221272
OpenAlexW2072507265

What OpenQuestion holds

Textmetadata
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Registered trials

None linked

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.