Evidence map›Paper›PMID 15218065›Full record

ArticleThe Journal of physiology2004

Molecular mechanism of kNBC1-carbonic anhydrase II interaction in proximal tubule cells.

Alexander Pushkin, Natalia Abuladze, Eitan Gross, Debra Newman, Sergei Tatishchev, Ivan Lee, Olga Fedotoff, Galyna Bondar, Rustam Azimov, Matt Ngyuen and 1 more

Open access · greenAbstract readComparative Study
In one paragraph

Article in The Journal of physiology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

39 citing papers in PubMed, 85 citations in OpenAlex.

  1. Review
  2. Article
  3. Activation of the Ae4 (Slc4a9) cation-driven ClAmerican journal of physiology. Gastrointestinal and liver physiology · 2021
    Article
  4. Article
  5. Acetazolamide causes renalAmerican journal of physiology. Renal physiology · 2020
    Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Cation-coupled bicarbonate transporters.Comprehensive Physiology · 2014
    Review
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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

11 authors at 2 institutions in 1 country.

Alexander PushkinDivision of Nephrology, David Geffen School of Medicine at UCLA, Los Angeles, CA 90095, USA. apushkin@mednet.ucla.edu
Natalia Abuladze
Eitan Gross
Debra Newman
Sergei Tatishchev
Ivan Lee
Olga Fedotoff
Galyna Bondar
Rustam Azimov
Matt Ngyuen
Ira Kurtz
University of California, Los Angeles · USCase Western Reserve University · US

Funding

BIOLOGY OF SODIUM BICARBONATE TRANSPORTR01DK058563 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI KURTZ, IRA · 2001 to 2011
$3.1M
Modulation of Electrogenic Sodium Bicarbonate TransportR01DK063125 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI KURTZ, IRA · 2003 to 2007
$1.8M
NEPHROLOGY SCIENTIST TRAINING GRANTT32DK007789 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI KURTZ, IRA · 2000 to 2017
$1.5M
NIDDK NIH HHS DK07789NIDDK NIH HHS DK58563NIDDK NIH HHS DK63125NIDDK NIH HHS R01 DK058563NIDDK NIH HHS R01 DK063125NIDDK NIH HHS T32 DK007789
6 · The paper itself

Abstract

We have recently shown that carbonic anhydrase II (CAII) binds in vitro to the C-terminus of the electrogenic sodium bicarbonate cotransporter kNBC1 (kNBC1-ct). In the present study we determined the molecular mechanisms for the interaction between the two proteins and whether kNBC1 and CAII form a transport metabolon in vivo wherein bicarbonate is transferred from CAII directly to the cotransporter. Various residues in the C-terminus of kNBC1 were mutated and the effect of these mutations on both the magnitude of CAII binding and the function of kNBC1 expressed in mPCT cells was determined. Two clusters of acidic amino acids, L(958)DDV and D(986)NDD in the wild-type kNBC1-ct involved in CAII binding were identified. In both acidic clusters, the first aspartate residue played a more important role in CAII binding than others. A significant correlation between the magnitude of CAII binding and kNBC1-mediated flux was shown. The results indicated that CAII activity enhances flux through the cotransporter when the enzyme is bound to kNBC1. These data are the first direct evidence that a complex of an electrogenic sodium bicarbonate cotransporter with CAII functions as a transport metabolon.

Indexed as

Amino Acid SequenceAnimalsCarbonic Anhydrase IICells, CulturedHumansKidney Tubules, ProximalMiceMolecular Sequence DataProtein BindingSodium-Bicarbonate SymportersCarbonic Anhydrase IISLC4A4 protein, humanSlc4a4 protein, mouseSodium-Bicarbonate Symporters

Identifiers

PMID15218065
PMCPMC1665076
OpenAlexW2160953172

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.