Evidence map›Paper›PMID 26358290›Full record

ArticleDrug metabolism and disposition: the biological fate of chemicals2015

Shared Ligands Between Organic Anion Transporters (OAT1 and OAT6) and Odorant Receptors.

Wei Wu, Kevin T Bush, Henry C Liu, Christopher Zhu, Ruben Abagyan, Sanjay K Nigam

Open access · bronzeAbstract read
In one paragraph

Article in Drug metabolism and disposition: the biological fate of chemicals, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

17 citing papers in PubMed, 22 citations in OpenAlex.

  1. A guide to uraemic toxicity.Nature reviews. Nephrology · 2026
    Review
  2. Article
  3. Drug metabolism and disposition: the biological fate of chemicals · 2021
    Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Review
  9. Review
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  12. Article
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  14. Article
  15. Kidney versus Liver Specification of SLC and ABC Drug Transporters, Tight Junction Molecules, and Biomarkers.Drug metabolism and disposition: the biological fate of chemicals · 2016
    Article
  16. Handling of Drugs, Metabolites, and Uremic Toxins by Kidney Proximal Tubule Drug Transporters.Clinical journal of the American Society of Nephrology : CJASN · 2015
    Article
  17. 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

6 authors at 1 institution in 1 country.

Wei WuDepartments of Pediatrics (K.T.B., S.K.N.), Medicine (Division of Nephrology and Hypertension)(W.W., S.K.N.), Bioengineering (H.C.L.), Biomedical Sciences (C.Z.), School of Pharmacy/Pharmaceutical Science (R.A.), and Cellular and Molecular Medicine (S.K.N.), University of California, San Diego, La Jolla, California.
Kevin T BushDepartments of Pediatrics (K.T.B., S.K.N.), Medicine (Division of Nephrology and Hypertension)(W.W., S.K.N.), Bioengineering (H.C.L.), Biomedical Sciences (C.Z.), School of Pharmacy/Pharmaceutical Science (R.A.), and Cellular and Molecular Medicine (S.K.N.), University of California, San Diego, La Jolla, California.
Henry C LiuDepartments of Pediatrics (K.T.B., S.K.N.), Medicine (Division of Nephrology and Hypertension)(W.W., S.K.N.), Bioengineering (H.C.L.), Biomedical Sciences (C.Z.), School of Pharmacy/Pharmaceutical Science (R.A.), and Cellular and Molecular Medicine (S.K.N.), University of California, San Diego, La Jolla, California.
Christopher ZhuDepartments of Pediatrics (K.T.B., S.K.N.), Medicine (Division of Nephrology and Hypertension)(W.W., S.K.N.), Bioengineering (H.C.L.), Biomedical Sciences (C.Z.), School of Pharmacy/Pharmaceutical Science (R.A.), and Cellular and Molecular Medicine (S.K.N.), University of California, San Diego, La Jolla, California.
Ruben AbagyanDepartments of Pediatrics (K.T.B., S.K.N.), Medicine (Division of Nephrology and Hypertension)(W.W., S.K.N.), Bioengineering (H.C.L.), Biomedical Sciences (C.Z.), School of Pharmacy/Pharmaceutical Science (R.A.), and Cellular and Molecular Medicine (S.K.N.), University of California, San Diego, La Jolla, California.
Sanjay K NigamDepartments of Pediatrics (K.T.B., S.K.N.), Medicine (Division of Nephrology and Hypertension)(W.W., S.K.N.), Bioengineering (H.C.L.), Biomedical Sciences (C.Z.), School of Pharmacy/Pharmaceutical Science (R.A.), and Cellular and Molecular Medicine (S.K.N.), University of California, San Diego, La Jolla, California snigam@ucsd.edu.
University of California, San Diego · US

Funding

Macromolecular DockingR01GM071872 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI ABAGYAN, RUBEN · 2004 to 2017
$4.2M
TRAINING & OUTREACH COREU54HD071600 · NICHD · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI SAKOULAS, GEORGE · 2011 to 2015
$3.6M
Substrate Specificity of the Choroid Plexus and Kidney Transporter Oat1R01GM098449 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI NIGAM, SANJAY K · 2012 to 2015
$2.1M
Structure Function Analysis of the Multi-specific Drug Transporter OCT1R01GM104098 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI NIGAM, SANJAY K · 2013 to 2016
$1.6M
NICHD NIH HHS U54 HD071600NIGMS NIH HHS GM098449NIGMS NIH HHS GM104098NIGMS NIH HHS R01 GM071872NIGMS NIH HHS R01 GM098449NIGMS NIH HHS R01 GM104098
6 · The paper itself

Abstract

The multispecific organic anion drug transporters OAT6 (SLC22A20) and OAT1 (SLC22A6) are expressed in nasal epithelial cells and both can bind odorants. Sequence analysis of OAT6 revealed an evolutionarily conserved 79-amino acid (AA) fragment present not only in OAT6 but also in other SLC22 transporters, such as the organic anion transporter (OAT), organic carnitine transporter (OCTN), and organic cation transporter (OCT) subfamilies. A similar fragment is also conserved in some odorant receptors (ORs) in both humans and rodents. This fragment is located in regions believed to be important for ligand/substrate preference and recognition in both classes of proteins, raising the possibility that it may be part of a potential common ligand/substrate recognition site in certain ORs and SLC22 transporters. In silico screening of an odorant database containing known OR ligands with a pharmacophore hypothesis (generated from a set of odorants known to bind OAT6 and/or OAT1), followed by in vitro uptake assays in transfected cells, identified OR ligands capable of inhibiting OAT6- and/or OAT1-mediated transport, albeit with different affinities. The conservation of the AA fragments between these two different classes of proteins, together with their coexpression in olfactory as well as other tissues, suggests the possibility that ORs and SLC22 transporters function in concert, and raises the question as to whether these transporters function in remote sensing and signaling and/or as transceptors.

Indexed as

Amino Acid SequenceAnimalsCaprylatesCHO CellsCricetinaeCricetulusDose-Response Relationship, DrugHumansLigandsMiceMolecular Sequence DataOrganic Anion TransportersOrganic Anion Transport Protein 1RatsReceptors, OdorantCaprylatesLigandsmethyl octanoateOAT6 protein, mouseOrganic Anion TransportersOrganic Anion Transport Protein 1Receptors, OdorantSlc22a6 protein, mouse

Identifiers

PMID26358290
PMCPMC4658493
OpenAlexW2255166567

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.