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Mishima, E. ; Wahida, A. ; Seibt, T. ; Conrad, M.

Diverse biological functions of vitamin K: From coagulation to ferroptosis.

Nat. Metab. 5, 924-932 (2023)
DOI PMC
Open Access Green as soon as Postprint is submitted to ZB.
Vitamin K is essential for several physiological processes, such as blood coagulation, in which it serves as a cofactor for the conversion of peptide-bound glutamate to γ-carboxyglutamate in vitamin K-dependent proteins. This process is driven by the vitamin K cycle facilitated by γ-carboxyglutamyl carboxylase, vitamin K epoxide reductase and ferroptosis suppressor protein-1, the latter of which was recently identified as the long-sought-after warfarin-resistant vitamin K reductase. In addition, vitamin K has carboxylation-independent functions. Akin to ubiquinone, vitamin K acts as an electron carrier for ATP production in some organisms and prevents ferroptosis, a type of cell death hallmarked by lipid peroxidation. In this Perspective, we provide an overview of the diverse functions of vitamin K in physiology and metabolism and, at the same time, offer a perspective on its role in ferroptosis together with ferroptosis suppressor protein-1. A comparison between vitamin K and ubiquinone, from an evolutionary perspective, may offer further insights into the manifold roles of vitamin K in biology.
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Publication type Article: Journal article
Document type Scientific Article
Corresponding Author
Keywords Gamma-glutamyl Carboxylase; Epoxide-reductase; Menaquinone-4 Vitamin-k-2; Phylloquinone Vitamin-k-1; Congenital Deficiency; Dependent Protein; Cell-death; Warfarin; Identification; Expression
ISSN (print) / ISBN 2522-5812
e-ISSN 2522-5812
Journal Nature metabolism
Quellenangaben Volume: 5, Issue: 6, Pages: 924-932 Article Number: , Supplement: ,
Publisher Springer
Publishing Place London
Non-patent literature Publications
Reviewing status Peer reviewed
Institute(s) Institute of Metabolism and Cell Death (MCD)
Grants European Research Council under the European Union - JSPS KAKENHI
ner-Fresenius-Stiftung
Else Krouml
German Federal Ministry of Education and Research (BMBF) FERROPath
Deutsche Forschungsgemeinschaft