Evidence map›Paper›PMID 24338019›Full record

ArticleThe Journal of biological chemistry2014

Intracellular and extracellular carbonic anhydrases cooperate non-enzymatically to enhance activity of monocarboxylate transporters.

Michael Klier, Fabian T Andes, Joachim W Deitmer, Holger M Becker

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed, 1 pooled it
2.4field-weighted citation impact, top 11% 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

35 citing papers in PubMed, 1 synthesis or guideline pooled it, 60 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. A study of bacteria producing carbonic anhydrase enzyme for CaCOEnvironmental science and pollution research international · 2024
    Article
  5. Review
  6. Exploring monocarboxylate transporter inhibition for cancer treatment.Exploration of targeted anti-tumor therapy · 2024
    Review
  7. Article
  8. Review
  9. Review
  10. Role of pH Regulatory Proteins and Dysregulation of pH in Prostate Cancer.Reviews of physiology, biochemistry and pharmacology · 2022
    Article
  11. Carbonic Anhydrases II and IX in Non-ampullary Duodenal Adenomas and Adenocarcinoma.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2021
    Article
  12. Proton Transport in Cancer Cells: The Role of Carbonic Anhydrases.International journal of molecular sciences · 2021
    Review
  13. Article
  14. Heteromeric Solute Carriers: Function, Structure, Pathology and Pharmacology.Advances in experimental medicine and biology · 2021
    Review
  15. Acetazolamide causes renalAmerican journal of physiology. Renal physiology · 2020
    Article
  16. Review
  17. Review
  18. Review
  19. Review
  20. 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

4 authors at 1 institution in 1 country.

Michael KlierFrom the Division of General Zoology, Department of Biology, University of Kaiserslautern D-67653 Kaiserslautern, Germany and.
Fabian T Andes
Joachim W Deitmer
Holger M Becker
University of Kaiserslautern · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proton-coupled monocarboxylate transporters (MCTs) are carriers of high-energy metabolites such as lactate, pyruvate, and ketone bodies and are expressed in most tissues. It has previously been shown that transport activity of MCT1 and MCT4 is enhanced by the cytosolic carbonic anhydrase II (CAII) independent of its catalytic activity. We have now studied the influence of the extracellular, membrane-bound CAIV on transport activity of MCT1/4, heterologously expressed in Xenopus oocytes. Coexpression of CAIV with MCT1 and MCT4 resulted in a significant increase in MCT transport activity, even in the nominal absence of CO2/HCO3(-). CAIV-mediated augmentation of MCT activity was independent of the CAIV catalytic function, since application of the CA-inhibitor ethoxyzolamide or coexpression of the catalytically inactive mutant CAIV-V165Y did not suppress CAIV-mediated augmentation of MCT transport activity. The interaction required CAIV at the extracellular surface, since injection of CAIV protein into the oocyte cytosol did not augment MCT transport function. The effects of cytosolic CAII (injected as protein) and extracellular CAIV (expressed) on MCT transport activity, were additive. Our results suggest that intra- and extracellular carbonic anhydrases can work in concert to ensure rapid shuttling of metabolites across the cell membrane.

Indexed as

AnimalsBiological TransportCarbonic Anhydrase IICarbonic Anhydrase IVCytosolExtracellular SpaceHumansHydrogen-Ion ConcentrationKetone BodiesLactic AcidMembrane ProteinsMonocarboxylate Transport Protein 1Monocarboxylic Acid TransportersMuscle ProteinsOocytesOxygen IsotopesCA4 protein, humanCarbonic Anhydrase IICarbonic Anhydrase IVKetone BodiesLactic AcidMembrane ProteinsMonocarboxylate Transport Protein 1Monocarboxylic Acid TransportersMuscle ProteinsOxygen IsotopesPyruvic AcidSLC16A4 protein, humanSymportersIon-sensitive ElectrodesLactic AcidpH RegulationProtein ComplexesProtein ExpressionProton-collecting AntennaTransport MetabolonXenopus Oocytes

Identifiers

PMID24338019
PMCPMC3908409
OpenAlexW2079490376

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.