Analysis of the ability of vitamin D3-metabolizing cytochromes P450 to act on vitamin D3 sulfate and 25-hydroxyvitamin D3 3-sulfate.
25-hydroxyvitamin D3
CYP11A1
CYP24A1
CYP27A1
CYP27B1
CYP2R1
Vitamin D3 sulfate
Journal
The Journal of steroid biochemistry and molecular biology
ISSN: 1879-1220
Titre abrégé: J Steroid Biochem Mol Biol
Pays: England
ID NLM: 9015483
Informations de publication
Date de publication:
03 2023
03 2023
Historique:
received:
08
09
2022
revised:
08
11
2022
accepted:
25
11
2022
pubmed:
2
12
2022
medline:
8
2
2023
entrez:
1
12
2022
Statut:
ppublish
Résumé
25-Hydroxyvitamin D3 (25(OH)D3) is present in the human circulation esterified to sulfate with some studies showing that 25(OH)D3 3-sulfate levels are almost as high as unconjugated 25(OH)D3. Vitamin D3 is also present in human serum in the sulfated form as are other metabolites. Our aim was to determine whether sulfated forms of vitamin D3 and vitamin D3 metabolites can be acted on by vitamin D-metabolizing cytochromes P450 (CYPs), one of which (CYP11A1) is known to act on cholesterol sulfate. We used purified, bacterially expressed CYPs to test if they could act on the sulfated forms of their natural substrates. Purified CYP27A1 converted vitamin D3 sulfate to 25(OH)D3 3-sulfate with a catalytic efficiency (k
Identifiants
pubmed: 36455719
pii: S0960-0760(22)00180-7
doi: 10.1016/j.jsbmb.2022.106229
pii:
doi:
Substances chimiques
vitamin D3 sulfoconjugate
10529-43-8
Calcifediol
P6YZ13C99Q
Cholesterol Side-Chain Cleavage Enzyme
EC 1.14.15.6
Sulfates
0
Cholecalciferol
1C6V77QF41
Vitamin D
1406-16-2
25-Hydroxyvitamin D3 1-alpha-Hydroxylase
EC 1.14.15.18
Vitamin D3 24-Hydroxylase
EC 1.14.15.16
Cholestanetriol 26-Monooxygenase
EC 1.14.15.15
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
106229Informations de copyright
Copyright © 2022 Elsevier Ltd. All rights reserved.
Déclaration de conflit d'intérêts
Conflict of interest The authors declare no conflict of interest.