Evidence map›Paper›PMID 29392568›Full record

ArticleEuropean journal of drug metabolism and pharmacokinetics2018

Effects of Human Sulfotransferase 2A1 Genetic Polymorphisms 3 on the Sulfation of Tibolone.

Ethan Miller, Munaf H Zalzala, Maryam S Abunnaja, Katsuhisa Kurogi, Yoichi Sakakibara, Masahito Suiko, Ming-Cheh Liu

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

Article in European journal of drug metabolism and pharmacokinetics, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.5field-weighted citation impact, top 33% 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

2 citing papers in PubMed, 9 citations in OpenAlex.

  1. Review
  2. 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

7 authors at 3 institutions in 3 countries.

Ethan MillerDepartment of Pharmacology, College of Pharmacy and Pharmaceutical Sciences, University of Toledo Health Science Campus, 3000 Arlington Avenue, Toledo, OH, 43614, USA.
Munaf H ZalzalaDepartment of Pharmacology, College of Pharmacy and Pharmaceutical Sciences, University of Toledo Health Science Campus, 3000 Arlington Avenue, Toledo, OH, 43614, USA.
Maryam S AbunnajaDepartment of Pharmacology, College of Pharmacy and Pharmaceutical Sciences, University of Toledo Health Science Campus, 3000 Arlington Avenue, Toledo, OH, 43614, USA.
Katsuhisa KurogiDepartment of Pharmacology, College of Pharmacy and Pharmaceutical Sciences, University of Toledo Health Science Campus, 3000 Arlington Avenue, Toledo, OH, 43614, USA.
Yoichi SakakibaraDepartment of Biochemistry and Applied Biosciences, University of Miyazaki, Miyazaki, 889-2192, Japan.
Masahito SuikoDepartment of Biochemistry and Applied Biosciences, University of Miyazaki, Miyazaki, 889-2192, Japan.
Ming-Cheh LiuDepartment of Pharmacology, College of Pharmacy and Pharmaceutical Sciences, University of Toledo Health Science Campus, 3000 Arlington Avenue, Toledo, OH, 43614, USA. ming.liu@utoledo.edu.
University of Miyazaki · JPUniversity of Toledo · USUniversity of Baghdad · IQ

Funding

Ontogeny of the Phase II cytosolic sulfotransferases and adverse drug reactionsR03HD071146 · NICHD · UNIVERSITY OF TOLEDO HEALTH SCI CAMPUS · PI LIU, MING-CHEH · 2012 to 2013
$146k
National Institutes of Health R03HD071146NICHD NIH HHS R03 HD071146
6 · The paper itself

Abstract

BACKGROUND AND

objectivesPrevious studies have demonstrated the metabolism of tibolone through sulfation, with the cytosolic sulfotransferase (SULT) SULT2A1 as the major responsible enzyme. The current study aimed to investigate how SULT2A1 genetic polymorphisms may affect the dehydroepiandrosterone (DHEA)- and tibolone-sulfating activity of SULT2A1.

methodsSite-directed mutagenesis was employed to generate cDNAs encoding ten different SULT2A1 allozymes. Recombinant SULT2A1 allozymes were expressed in BL21 E. coli cells, and purified using glutathione-sepharose affinity chromatography. An established sulfotransferase assay was used to analyze DHEA- and tibolone-sulfating activity of the purified SULT2A1 allozymes.

resultsThe nine human SULT2A1 allozymes plus the wild-type SULT2A1 were found to display differential sulfating activity toward DHEA and tibolone. Kinetic analysis revealed that different SULT2A1 allozymes exhibited differential substrate affinity and catalytic efficiency toward the two substrates tested.

conclusionThe results obtained provided useful information concerning the differential metabolism of tibolone through sulfation in individuals with different SULT2A1 genotypes.

Indexed as

Polymorphism, GeneticCells, CulturedDehydroepiandrosteroneHumansIsoenzymesKineticsMutagenesis, Site-DirectedNorpregnenesSulfotransferasesalcohol sulfotransferaseDehydroepiandrosteroneIsoenzymesNorpregnenesSulfotransferasestibolone

Identifiers

PMID29392568
PMCPMC6041190
OpenAlexW2794346312

What OpenQuestion holds

Textmetadata
LicenceTDM
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.