PUBLICATION
Identification and characterization of 5α-cyprinol-sulfating cytosolic sulfotransferases (Sults) in the Zebrafish (Danio rerio)
- Authors
- Kurogi, K., Yoshihama, M., Horton, A., Schiefer, I.T., Krasowski, M.D., Hagey, L.R., Williams, F.E., Sakakibara, Y., Kenmochi, N., Suiko, M., Liu, M.C.
- ID
- ZDB-PUB-170817-18
- Date
- 2017
- Source
- The Journal of steroid biochemistry and molecular biology 174: 120-127 (Journal)
- Registered Authors
- Kenmochi, Naoya
- Keywords
- 5α-cyprinol, Cytosolic sulfotransferase, SULT, sulfation, zebrafish
- MeSH Terms
-
- Animals
- Arylsulfotransferase/metabolism*
- Cholestanols/metabolism
- Cholic Acids/metabolism
- Dehydroepiandrosterone/metabolism
- Embryo, Nonmammalian
- Humans
- Zebrafish
- Zebrafish Proteins/metabolism*
- PubMed
- 28807679 Full text @ Steroid Biochem. Mol. Biol.
Citation
Kurogi, K., Yoshihama, M., Horton, A., Schiefer, I.T., Krasowski, M.D., Hagey, L.R., Williams, F.E., Sakakibara, Y., Kenmochi, N., Suiko, M., Liu, M.C. (2017) Identification and characterization of 5α-cyprinol-sulfating cytosolic sulfotransferases (Sults) in the Zebrafish (Danio rerio). The Journal of steroid biochemistry and molecular biology. 174:120-127.
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 C27-bile alcohol, 5α-cyprinol, in Cypriniform fish, whereas the enzymatic characteristics of zebrafish Sult3 members, particularly Sult3st4, correlated with those of human SULT2A1.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping