Evidence map›Paper›PMID 30050002›Full record

ReviewNutrients2018

VKORC1L1, An Enzyme Mediating the Effect of Vitamin K in Liver and Extrahepatic Tissues.

Julie Lacombe, Mathieu Ferron

Open access · goldAbstract readReview
In one paragraph

Review in Nutrients, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.5field-weighted citation impact, top 19% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed, 28 citations in OpenAlex.

  1. Review
  2. Article
  3. Mechanisms of Vitamins Inhibiting Ferroptosis.Antioxidants (Basel, Switzerland) · 2024
    Review
  4. TheCurrent issues in molecular biology · 2024
    Article
  5. Article
  6. Is a Vitamin K Epoxide Reductase Complex Subunit 1 (International journal of molecular sciences · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Review
  15. Review
  16. New Insights on Vitamin K Metabolism in Senegalese sole (International journal of molecular sciences · 2020
    Article
  17. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 2 institutions in 1 country.

Julie LacombeIntegrative and Molecular Physiology research unit, Institut de Recherches Cliniques de Montréal, Montréal, QC H2W 1R7, Canada. julie.lacombe@ircm.qc.ca.
Mathieu FerronIntegrative and Molecular Physiology research unit, Institut de Recherches Cliniques de Montréal, Montréal, QC H2W 1R7, Canada. mathieu.ferron@ircm.qc.ca.
McGill University · CAMontreal Clinical Research Institute · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Vitamin K is an essential nutrient involved in the regulation of blood clotting and tissue mineralization. Vitamin K oxidoreductase (VKORC1) converts vitamin K epoxide into reduced vitamin K, which acts as the co-factor for the γ-carboxylation of several proteins, including coagulation factors produced by the liver. VKORC1 is also the pharmacological target of warfarin, a widely used anticoagulant. Vertebrates possess a VKORC1 paralog, VKORC1-like 1 (VKORC1L1), but until very recently, the importance of VKORC1L1 for protein γ-carboxylation and hemostasis in vivo was not clear. Here, we first review the current knowledge on the structure, function and expression pattern of VKORC1L1, including recent data establishing that, in the absence of VKORC1, VKORC1L1 can support vitamin K-dependent carboxylation in the liver during the pre- and perinatal periods in vivo. We then provide original data showing that the partial redundancy between VKORC1 and VKORC1L1 also exists in bone around birth. Recent studies indicate that, in vitro and in cell culture models, VKORC1L1 is less sensitive to warfarin than VKORC1. Genetic evidence is presented here, which supports the notion that VKORC1L1 is not the warfarin-resistant vitamin K quinone reductase present in the liver. In summary, although the exact physiological function of VKORC1L1 remains elusive, the latest findings clearly established that this enzyme is a vitamin K oxidoreductase, which can support γ-carboxylation in vivo.

Indexed as

Blood CoagulationAnimalsAnticoagulantsCarboxylic AcidsEvolution, MolecularGene Expression Regulation, DevelopmentalGene Expression Regulation, EnzymologicHumansLiverOxidation-ReductionProtein ConformationProtein Processing, Post-TranslationalStructure-Activity RelationshipVitamin K 1Vitamin K Epoxide ReductasesWarfarinAnticoagulantsCarboxylic AcidsVitamin K 1vitamin K1 oxideVitamin K Epoxide ReductasesVKORC1L1 protein, humanVKORC1 protein, humanWarfarincoagulationGGCXosteocalcinVitamin Kvitamin K-dependent carboxylationvitamin K oxidoreductaseVKORC1VKORC1L1warfarin

Identifiers

PMID30050002
PMCPMC6116193
OpenAlexW2883623037

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.