Inhibition of Human Sulfotransferases by Phthalate Monoesters.
enzyme inhibition
in silico docking
in vitro–in vivo extrapolation
phthalate esters (PAEs)
sulfotransferases (SULTs)
Journal
Frontiers in endocrinology
ISSN: 1664-2392
Titre abrégé: Front Endocrinol (Lausanne)
Pays: Switzerland
ID NLM: 101555782
Informations de publication
Date de publication:
2022
2022
Historique:
received:
02
02
2022
accepted:
14
03
2022
entrez:
9
5
2022
pubmed:
10
5
2022
medline:
11
5
2022
Statut:
epublish
Résumé
This study aimed to investigate the inhibition of human important phase II metabolic enzyme sulfotransferases (SULTs) by phthalate monoesters, which are important metabolites of phthalate esters (PAEs). Recombinant SULT-catalyzed metabolism of p-nitrophenol (PNP) was employed as the probe reactions of SULTs to investigate the inhibition of 8 kinds of phthalate monoesters towards SULT isoforms. An Multiple phthalate monoesters have been demonstrated to exert strong inhibition potential towards SULT1A1, SULT1B1, and SULT1E1, and no significant inhibition of phthalate monoesters towards SULT1A3 was found. The activity of SULT1A1 was strongly inhibited by mono-hexyl phthalate (MHP), mono-octyl phthalate (MOP), mono-benzyl phthalate (MBZP), and mono-ethylhexyl phthalate (MEHP). Monobutyl phthalate (MBP), MHP, MOP, mono-cyclohexyl phthalate (MCHP), and MEHP significantly inhibited the activity of SULT1B1. MHP, MOP, and MEHP significantly inhibited the activity of SULT1E1. MOP was chosen as the representative phthalate monoester to determine the inhibition kinetic parameters ( All these information will be beneficial for understanding the risk of phthalate monoester exposure from a new perspective.
Identifiants
pubmed: 35528018
doi: 10.3389/fendo.2022.868105
pmc: PMC9072656
doi:
Substances chimiques
Esters
0
Phthalic Acids
0
Protein Isoforms
0
phthalic acid
6O7F7IX66E
Sulfotransferases
EC 2.8.2.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
868105Informations de copyright
Copyright © 2022 Huang, Lan, Zhang, Fan, Hu, Qin, Wang, Wu, Zheng and Liu.
Déclaration de conflit d'intérêts
The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest. The handling editor [FZ] declared a shared affiliation with the author [CH] at the time of review.
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