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; Ming-Cheh Liu

doi:10.1016/j.jsbmb.2017.08.005

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

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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, …

The Journal of steroid biochemistry and molecular biology, Vol.174, pp.120-127

11/2017

DOI: 10.1016/j.jsbmb.2017.08.005

PMCID: PMC5675747

PMID: 28807679

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https://www.ncbi.nlm.nih.gov/pmc/articles/5675747View

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Abstract

•Zebrafish homogenates are capable of sulfating 5α-cyprinol with a high affinity.•Zebrafish Sult2 and Sult3 members exhibit strong 5α-cyprinol-sulfating activities.•Zebrafish Sult2 members are more catalytically efficient toward cyprinol than zebrafish Sult3 members.•The catalytic property of human SULT2A1 is comparable to that of zebrafish Sult3 members, but not zebrafish Sult2 members. 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 C27-bile alcohol, 5α-cyprinol, in Cypriniform fish, whereas the enzymatic characteristics of zebrafish Sult3 members, particularly Sult3st4, correlated with those of human SULT2A1.

Zebrafish

Cytosolic sulfotransferase

5α-cyprinol

SULT

Sulfation

Details

Title: Subtitle: Identification and characterization of 5α-cyprinol-sulfating cytosolic sulfotransferases (Sults) in the zebrafish (Danio rerio)
Creators: Katsuhisa Kurogi - Department of Pharmacology, College of Pharmacy, University of Toledo Health Science Campus, Toledo, OH 43614, USA
Maki Yoshihama - Department of Pharmacology, College of Pharmacy, University of Toledo Health Science Campus, Toledo, OH 43614, USA
Austin Horton - Department of Pharmacology, College of Pharmacy, University of Toledo Health Science Campus, Toledo, OH 43614, USA
Isaac T Schiefer - Department of Pharmacology, College of Pharmacy, University of Toledo Health Science Campus, Toledo, OH 43614, USA
Matthew D Krasowski - Department of Pathology, University of Iowa Hospitals and Clinics, RCP 6233, 200 Hawkins Drive, Iowa City, IA 52242, USA
Lee R Hagey - Department of Medicine, University of California at San Diego, La Jolla, San Diego, CA 92093, USA
Frederick E Williams - Department of Pharmacology, College of Pharmacy, University of Toledo Health Science Campus, Toledo, OH 43614, USA
Yoichi Sakakibara - Biochemistry and Applied Biosciences, University of Miyazaki, Miyazaki 889-2192, Japan
Naoya Kenmochi - Frontier Research Center, University of Miyazaki, Miyazaki 889-2192, Japan
Masahito Suiko - Biochemistry and Applied Biosciences, University of Miyazaki, Miyazaki 889-2192, Japan
Ming-Cheh Liu - Department of Pharmacology, College of Pharmacy, University of Toledo Health Science Campus, Toledo, OH 43614, USA
Resource Type: Journal article
Publication Details: The Journal of steroid biochemistry and molecular biology, Vol.174, pp.120-127
DOI: 10.1016/j.jsbmb.2017.08.005
PMID: 28807679
PMCID: PMC5675747
NLM abbreviation: J Steroid Biochem Mol Biol
ISSN: 0960-0760
eISSN: 1879-1220
Publisher: Elsevier Ltd
Grant note: DOI: 10.13039/100000002, name: National Institutes of Health, award: R03HD071146; DOI: 10.13039/100000002, name: National Institutes of Health, award: K08-GM074238
Language: English
Date published: 11/2017
Academic Unit: Pathology
Record Identifier: 9984047613402771

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