Evidence map›Paper›PMID 21239697›Full record

ArticleBlood2011

Functional study of the vitamin K cycle in mammalian cells.

Jian-Ke Tie, Da-Yun Jin, David L Straight, Darrel W Stafford

Open access · bronzeAbstract read
In one paragraph

Article in Blood, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

58 citing papers in PubMed, 90 citations in OpenAlex.

  1. γ-glutamyl carboxylase inhibition by Anisindione.Structure (London, England : 1993) · 2026
    Article
  2. Article
  3. Giant viruses encode vitamin K-based redox modules for lipid modification.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  20. Targeting multiple enzymes in vitamin K metabolism for anticoagulation.Journal of thrombosis and haemostasis : JTH · 2021
    Article
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

4 authors at 1 institution in 1 country.

Jian-Ke TieDepartment of Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC, USA.
Da-Yun Jin
David L Straight
Darrel W Stafford
University of North Carolina at Chapel Hill · US

Funding

THE ROLE OF THE VITAMIN K CYCLE IN COAGULATIONP01HL006350 · NHLBI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI STAFFORD, DARREL W · 1985 to 2013
$17.5M
Characterization of Vitamin K Epoxide ReductaseR01HL077740 · NHLBI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI STAFFORD, DARREL W, TIE, JIANKE · 2005 to 2015
$3.9M
STRUCTURE/FUNCTION OF THE GAMMA GLUTAMYL CARBOXYLASER01HL048318 · NHLBI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI STAFFORD, DARREL W · 1992 to 2011
$3.4M
NHLBI NIH HHS HL048318NHLBI NIH HHS HL06350NHLBI NIH HHS HL077740NHLBI NIH HHS P01 HL006350NHLBI NIH HHS R01 HL048318NHLBI NIH HHS R01 HL077740
6 · The paper itself

Abstract

We describe a cell-based assay for studying vitamin K-cycle enzymes. A reporter protein consisting of the gla domain of factor IX (amino acids 1-46) and residues 47-420 of protein C was stably expressed in HEK293 and AV12 cells. Both cell lines secrete carboxylated reporter when fed vitamin K or vitamin K epoxide (KO). However, neither cell line carboxylated the reporter when fed KO in the presence of warfarin. In the presence of warfarin, vitamin K rescued carboxylation in HEK293 cells but not in AV12 cells. Dicoumarol, an NAD(P)H-dependent quinone oxidoreductase 1 (NQO1) inhibitor, behaved similarly to warfarin in both cell lines. Warfarin-resistant vitamin K epoxide reductase (VKOR-Y139F) supported carboxylation in HEK293 cells when fed KO in the presence of warfarin, but it did not in AV12 cells. These results suggest the following: (1) our cell system is a good model for studying the vitamin K cycle, (2) the warfarin-resistant enzyme reducing vitamin K to hydroquinone (KH₂) is probably not NQO1, (3) there appears to be a warfarin-sensitive enzyme other than VKOR that reduces vitamin K to KH₂, and (4) the primary function of VKOR is the reduction of KO to vitamin K.

Indexed as

AnticoagulantsCell LineClinical Laboratory TechniquesHEK293 CellsHumansMixed Function OxygenasesSignal TransductionVitamin KVitamin K 1Vitamin K Epoxide ReductasesWarfarinAnticoagulantsMixed Function OxygenasesVitamin KVitamin K 1vitamin K1 oxideVitamin K Epoxide ReductasesWarfarin

Identifiers

PMID21239697
PMCPMC3062303
OpenAlexW2121152339

What OpenQuestion holds

Textmetadata
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.