Evidence map›Paper›PMID 28807679›Full record

ArticleThe Journal of steroid biochemistry and molecular biology2017

Identification and characterization of 5α-cyprinol-sulfating cytosolic sulfotransferases (Sults) in the zebrafish (Danio rerio).

Katsuhisa Kurogi, Maki Yoshihama, Austin Horton, Isaac T Schiefer, Matthew D Krasowski, Lee R Hagey, Frederick E Williams, Yoichi Sakakibara, Naoya Kenmochi, Masahito Suiko and 1 more

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PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of steroid biochemistry and molecular biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.4field-weighted citation impact, top 37% 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

1 citing paper in PubMed, 10 citations in OpenAlex.

  1. 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

11 authors at 4 institutions in 2 countries.

Katsuhisa KurogiDepartment of Pharmacology, College of Pharmacy, University of Toledo Health Science Campus, Toledo, OH 43614, USA; Biochemistry and Applied Biosciences, University of Miyazaki, Miyazaki 889-2192, Japan.
Maki YoshihamaDepartment of Pharmacology, College of Pharmacy, University of Toledo Health Science Campus, Toledo, OH 43614, USA; Frontier Research Center, University of Miyazaki, Miyazaki 889-2192, Japan.
Austin HortonDepartment of Pharmacology, College of Pharmacy, University of Toledo Health Science Campus, Toledo, OH 43614, USA.
Isaac T SchieferDepartment of Pharmacology, College of Pharmacy, University of Toledo Health Science Campus, Toledo, OH 43614, USA.
Matthew D KrasowskiDepartment of Pathology, University of Iowa Hospitals and Clinics, RCP 6233, 200 Hawkins Drive, Iowa City, IA 52242, USA.
Lee R HageyDepartment of Medicine, University of California at San Diego, La Jolla, San Diego, CA 92093, USA.
Frederick E WilliamsDepartment of Pharmacology, College of Pharmacy, University of Toledo Health Science Campus, Toledo, OH 43614, USA.
Yoichi SakakibaraBiochemistry and Applied Biosciences, University of Miyazaki, Miyazaki 889-2192, Japan.
Naoya KenmochiFrontier Research Center, University of Miyazaki, Miyazaki 889-2192, Japan.
Masahito SuikoBiochemistry and Applied Biosciences, University of Miyazaki, Miyazaki 889-2192, Japan.
Ming-Cheh LiuDepartment of Pharmacology, College of Pharmacy, University of Toledo Health Science Campus, Toledo, OH 43614, USA. Electronic address: ming.liu@utoledo.edu.
University of Miyazaki · JPUniversity of Toledo · USUniversity of California, San Diego · USUniversity of Iowa Hospitals and Clinics · US

Funding

Function and Evolution of the Pregnane X Receptor (PXR)K08GM074238 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI KRASOWSKI, MATTHEW D · 2006 to 2009
$509k
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
NICHD NIH HHS R03 HD071146NIGMS NIH HHS K08 GM074238
6 · The paper itself

Abstract

5α-Cyprinol 27-sulfate is the major biliary bile salt present in cypriniform fish including the zebrafish (Danio rerio). The current study was designed to identify the zebrafish cytosolic sulfotransferase (Sult) enzyme(s) capable of sulfating 5α-cyprinol and to characterize the zebrafish 5α-cyprinol-sulfating Sults in comparison with human SULT2A1. Enzymatic assays using zebrafish homogenates showed 5α-cyprinol-sulfating activity. A systematic analysis, using a panel of recombinant zebrafish Sults, revealed two Sult2 subfamily members, Sult2st2 and Sult2st3, as major 5α-cyprinol-sulfating Sults. Both enzymes showed higher activities using 5α-cyprinol as the substrate, compared to their activity with DHEA, a representative substrate for mammalian SULT2 family members, particularly SULT2A1. pH-Dependence and kinetics experiments indicated that the catalytic properties of zebrafish Sult2 family members in mediating the sulfation of 5α-cyprinol were different from those of either zebrafish Sult3st4 or human SULT2A1. Collectively, these results imply that both Sult2st2 and Sult2st3 have evolved to sulfate specifically C

Indexed as

AnimalsArylsulfotransferaseCholestanolsCholic AcidsDehydroepiandrosteroneEmbryo, NonmammalianHumansZebrafishZebrafish ProteinsanhydrocyprinolArylsulfotransferaseCholestanolsCholic AcidsDehydroepiandrosteroneZebrafish Proteins5α-cyprinolCytosolic sulfotransferaseSulfationSULTZebrafish

Identifiers

PMID28807679
PMCPMC5675747
OpenAlexW2744471330

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.