Evidence map›Paper›PMID 22677001›Full record

ArticleThe Biochemical journal2012

Intestinal peptidases form functional complexes with the neutral amino acid transporter B(0)AT1.

Stephen J Fairweather, Angelika Bröer, Megan L O'Mara, Stefan Bröer

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
3.4field-weighted citation impact, top 8% 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

36 citing papers in PubMed, 70 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. SLC2A9 rs16890979 reduces uric acid absorption by kidney organoids.Frontiers in cell and developmental biology · 2023
    Article
  6. The "www" ofMembranes · 2022
    Review
  7. Article
  8. Article
  9. Review
  10. Control ofFrontiers in cellular and infection microbiology · 2022
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Review
  17. Evolution, correlation, structural impact and dynamics of emerging SARS-CoV-2 variants.Computational and structural biotechnology journal · 2021
    Article
  18. Heteromeric Solute Carriers: Function, Structure, Pathology and Pharmacology.Advances in experimental medicine and biology · 2021
    Review
  19. Article
  20. BFunction (Oxford, England) · 2021
    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 2 institutions in 1 country.

Stephen J FairweatherResearch School of Biology, Australian National University, Canberra, ACT 0200, Australia.
Angelika Bröer
Megan L O'Mara
Stefan Bröer
Australian National University · AUUniversity of Queensland · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The brush-border membrane of the small intestine and kidney proximal tubule are the major sites for the absorption and re-absorption of nutrients in the body respectively. Transport of amino acids is mediated through the action of numerous secondary active transporters. In the mouse, neutral amino acids are transported by B(0)AT1 [broad neutral ((0)) amino acid transporter 1; SLC6A19 (solute carrier family 6 member 19)] in the intestine and by B(0)AT1 and B(0)AT3 (SLC6A18) in the kidney. Immunoprecipitation and Blue native electrophoresis of intestinal brush-border membrane proteins revealed that B(0)AT1 forms complexes with two peptidases, APN (aminopeptidase N/CD13) and ACE2 (angiotensin-converting enzyme 2). Physiological characterization of B(0)AT1 expressed together with these peptidases in Xenopus laevis oocytes revealed that APN increased the substrate affinity of the transporter up to 2.5-fold and also increased its surface expression (V(max)). Peptide competition experiments, in silico modelling and site-directed mutagenesis of APN suggest that the catalytic site of the peptidase is involved in the observed changes of B(0)AT1 apparent substrate affinity, possibly by increasing the local substrate concentration. These results provide evidence for the existence of B(0)AT1-containing digestive complexes in the brush-border membrane, interacting differentially with various peptidases, and responding to the dynamic needs of nutrient absorption in the intestine and kidney.

Indexed as

Amino Acid Transport Systems, NeutralAngiotensin-Converting Enzyme 2AnimalsCD13 AntigensCells, CulturedFemaleHumansIntestine, SmallKineticsMaleMiceMice, Inbred C57BLMicrovilliOocytesPeptidyl-Dipeptidase AProtein TransportACE2 protein, humanAce2 protein, mouseAmino Acid Transport Systems, NeutralAngiotensin-Converting Enzyme 2CD13 AntigensPeptidyl-Dipeptidase ASLC6A19 protein, mouse

Identifiers

PMID22677001
PMCPMC3408045
OpenAlexW2098554296

What OpenQuestion holds

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LicenceCC BY-NC
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.