Evidence map›Paper›PMID 23667501›Full record

ArticlePloS one2013

Membrane transporters for sulfated steroids in the human testis--cellular localization, expression pattern and functional analysis.

Daniela Fietz, Katharina Bakhaus, Britta Wapelhorst, Gary Grosser, Sabine Günther, Jörg Alber, Barbara Döring, Sabine Kliesch, Wolfgang Weidner, Christina E Galuska and 4 more

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

29 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. In Vitro and In Vivo Models for Drug Transport Across the Blood-Testis Barrier.Drug metabolism and disposition: the biological fate of chemicals · 2023
    Review
  6. Review
  7. Article
  8. Localization of Xenobiotic Transporters Expressed at the Human Blood-Testis Barrier.Drug metabolism and disposition: the biological fate of chemicals · 2022
    Article
  9. Drug transport across the blood-testis barrier.American journal of translational research · 2022
    Review
  10. Role of the Steroid Sulfate Uptake Transporter Soat (Frontiers in molecular biosciences · 2022
    Article
  11. Article
  12. Article
  13. Sertoli cell-only syndrome: etiology and clinical management.Journal of assisted reproduction and genetics · 2021
    Review
  14. Review
  15. Article
  16. Article
  17. Transepithelial transport across the blood-testis barrier.Reproduction (Cambridge, England) · 2018
    Review
  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

14 authors at 2 institutions in 1 country.

Daniela FietzInstitute for Veterinary Anatomy, Histology and Embryology, Justus Liebig University Giessen, Giessen, Germany. Daniela.Fietz@vetmed.uni-giessen.de
Katharina Bakhaus
Britta Wapelhorst
Gary Grosser
Sabine Günther
Jörg Alber
Barbara Döring
Sabine Kliesch
Wolfgang Weidner
Christina E Galuska
Michaela F Hartmann
Stefan A Wudy
Martin Bergmann
Joachim Geyer
University of Giessen · DEUniversity Hospital Münster · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sulfated steroid hormones are commonly considered to be biologically inactive metabolites, but may be reactivated by the steroid sulfatase into biologically active free steroids, thereby having regulatory function via nuclear androgen and estrogen receptors which are widespread in the testis. However, a prerequisite for this mode of action would be a carrier-mediated import of the hydrophilic steroid sulfate molecules into specific target cells in reproductive tissues such as the testis. In the present study we detected predominant expression of the Sodium-dependent Organic Anion Transporter (SOAT), the Organic Anion Transporting Polypeptide 6A1, and the Organic Solute Carrier Partner 1 in human testis biopsies. All of these showed significantly lower or even absent mRNA expression in severe disorders of spermatogenesis (arrest at the level of spermatocytes or spermatogonia, Sertoli cell only syndrome). Only SOAT was significantly lower expressed in biopsies showing hypospermatogenesis. By use of immunohistochemistry SOAT was localized to germ cells at various stages in human testis biopsies showing normal spermatogenesis. SOAT immunoreactivity was detected in zygotene primary spermatocytes of stage V, pachytene spermatocytes of all stages (I-V), secondary spermatocytes of stage VI, and round spermatids (step 1 and step 2) in stages I and II. Furthermore, SOAT transport function for steroid sulfates was analyzed with a novel liquid chromatography tandem mass spectrometry procedure capable of profiling steroid sulfate molecules from cell lysates. With this technique, the cellular inward-directed SOAT transport was verified for the established substrates dehydroepiandrosterone sulfate and estrone-3-sulfate. Additionally, β-estradiol-3-sulfate and androstenediol-3-sulfate were identified as novel SOAT substrates.

Indexed as

Blotting, WesternChromatography, LiquidDNA PrimersFluorescent Antibody TechniqueHEK293 CellsHumansImmunohistochemistryIn Situ HybridizationMaleMembrane Transport ProteinsOligospermiaOrganic Anion TransportersReal-Time Polymerase Chain ReactionSteroidsSulfatesTandem Mass SpectrometryDNA PrimersMembrane Transport ProteinsOrganic Anion TransportersOSCP1 protein, humanSteroidsSulfates

Identifiers

PMID23667501
PMCPMC3648580
OpenAlexW1995374847

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.