Carboxylative efficacy of trans and cis MK7 and comparison with other vitamin K isomers.
GGCX
carboxylation
cis/trans isomers
phylloquinone
vitamin MK7
Journal
BioFactors (Oxford, England)
ISSN: 1872-8081
Titre abrégé: Biofactors
Pays: Netherlands
ID NLM: 8807441
Informations de publication
Date de publication:
Sep 2022
Sep 2022
Historique:
received:
21
03
2022
accepted:
20
04
2022
pubmed:
19
5
2022
medline:
19
10
2022
entrez:
18
5
2022
Statut:
ppublish
Résumé
Carboxylative enzymes are involved in many pathways and their regulation plays a crucial role in many of these pathways. In particular, γ-glutamylcarboxylase (GGCX) converts glutamate residues (Glu) into γ-carboxyglutamate (Gla) of the vitamin K-dependent proteins (VKDPs) activating them. VKDPs include at least 17 proteins involved in processes such as blood coagulation, blood vessels calcification, and bone mineralization. VKDPs are activated by the reduced form of vitamin K, naturally occurring as vitamin K1 (phylloquinone) and K2 (menaquinones, MKs). Among these, MK7 is the most efficient in terms of bioavailability and biological effect. Similarly to other trans isomers, it is produced by natural fermentation or chemically in both trans and cis. However, the efficacy of the biological effect of the different isomers and the impact on humans are unknown. Our study assessed carboxylative efficacy of trans and cis MK7 and compared it with other vitamin K isomers, evaluating both the expression of residues of carboxylated Gla-protein by western blot analysis and using a cell-free system to determine the GGCX activity by HPLC. Trans MK7H
Identifiants
pubmed: 35583412
doi: 10.1002/biof.1844
pmc: PMC9790681
doi:
Substances chimiques
Vitamin K 2
11032-49-8
Vitamin K
12001-79-5
1-Carboxyglutamic Acid
53445-96-8
Warfarin
5Q7ZVV76EI
Vitamin K 1
84-80-0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
1129-1136Subventions
Organisme : Deutsche Forschungsgemeinschaft (DFG, German Research Foundation)
Informations de copyright
© 2022 The Authors. BioFactors published by Wiley Periodicals LLC on behalf of International Union of Biochemistry and Molecular Biology.
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