Evidence map›Paper›PMID 9294213›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1997

Isolation of a multispecific organic anion and cardiac glycoside transporter from rat brain.

B Noé, B Hagenbuch, B Stieger, P J Meier

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
13.8field-weighted citation impact, top 1% 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

58 citing papers in PubMed, 395 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
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  7. Article
  8. Organic Anion Transporting Polypeptides Contribute to the Disposition of Perfluoroalkyl Acids in Humans and Rats.Toxicological sciences : an official journal of the Society of Toxicology · 2017
    Article
  9. Article
  10. Article
  11. Drug transporters in the central nervous system.Clinical pharmacokinetics · 2015
    Review
  12. Article
  13. Pharmacogenetics of membrane transporters: a review of current approaches.Methods in molecular biology (Clifton, N.J.) · 2014
    Review
  14. Article
  15. Organic anion-transporting polypeptides.Current topics in membranes · 2014
    Review
  16. Article
  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.

B NoéDivision of Clinical Pharmacology and Toxicology, Department of Medicine, University Hospital Zurich, CH-8091 Zurich, Switzerland.
B Hagenbuch
B Stieger
P J Meier
University Hospital of Zurich · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A novel multispecific organic anion transporting polypeptide (oatp2) has been isolated from rat brain. The cloned cDNA contains 3,640 bp. The coding region extends over 1,983 nucleotides, thus encoding a polypeptide of 661 amino acids. Oatp2 is homologous to other members of the oatp gene family of membrane transporters with 12 predicted transmembrane domains, five potential glycosylation, and six potential protein kinase C phosphorylation sites. In functional expression studies in Xenopus laevis oocytes, oatp2 mediated uptake of the bile acids taurocholate (Km approximately 35 microM) and cholate (Km approximately 46 microM), the estrogen conjugates 17beta-estradiol-glucuronide (Km approximately 3 microM) and estrone-3-sulfate (Km approximately 11 microM), and the cardiac gylcosides ouabain (Km approximately 470 microM) and digoxin (Km approximately 0.24 microM). Although most of the tested compounds are common substrates of several oatp-related transporters, high-affinity uptake of digoxin is a unique feature of the newly cloned oatp2. On the basis of Northern blot analysis under high-stringency conditions, oatp2 is highly expressed in brain, liver, and kidney but not in heart, spleen, lung, skeletal muscle, and testes. These results provide further support for the overall significance of oatps as a new family of multispecific organic anion transporters. They indicate that oatp2 may play an especially important role in the brain accumulation and toxicity of digoxin and in the hepatobiliary and renal excretion of cardiac glycosides from the body.

Indexed as

Amino Acid SequenceAnimalsAnion Transport ProteinsBiological TransportBrainCardiac GlycosidesCarrier ProteinsCloning, MolecularDNA, ComplementaryHumansMaleMolecular Sequence DataRatsRats, Sprague-DawleyRNA, MessengerSequence Homology, Amino AcidAnion Transport ProteinsCardiac GlycosidesCarrier ProteinsDNA, ComplementaryRNA, Messenger

Identifiers

PMID9294213
PMCPMC23365
OpenAlexW2088776629

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.