Evidence map›Paper›PMID 22239091›Full record

ArticleThe Biochemical journal2012

Caveolae optimize tissue factor-Factor VIIa inhibitory activity of cell-surface-associated tissue factor pathway inhibitor.

Susan A Maroney, Paul E Ellery, Jeremy P Wood, Josephine P Ferrel, Catherine E Bonesho, Alan E Mast

Abstract read
In one paragraph

Article in The Biochemical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.8field-weighted citation impact, top 30% 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

9 citing papers in PubMed, 12 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. New insights into the biology of tissue factor pathway inhibitor.Journal of thrombosis and haemostasis : JTH · 2015
    Review
  6. Review
  7. Article
  8. Review
  9. 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

6 authors at 2 institutions in 1 country.

Susan A MaroneyBlood Research Institute, Blood Center of Wisconsin, 8727 Watertown Plank Road, Milwaukee, WI 53201, USA.
Paul E Ellery
Jeremy P Wood
Josephine P Ferrel
Catherine E Bonesho
Alan E Mast
Versiti Blood Center of Wisconsin · USMedical College of Wisconsin · US

Funding

Clincal and Translational Science AwardUL1TR000055 · NCATS · MEDICAL COLLEGE OF WISCONSIN · PI SHAKER, REZA NONE · 2012 to 2015
$11.3M
Tissue Factor Pathway Inhibitor Binding Proteins on EndoR01HL068835 · NHLBI · VERSITI WISCONSIN, INC. · PI Alan E Mast · 2002 to 2026
$9.7M
Cysteine oxidation in the heartR01HL091469 · NHLBI · UNIV OF MED/DENT OF NJ-NJ MEDICAL SCHOOL · PI Junichi Sadoshima · 2008 to 2026
$9.4M
RESEARCH TRAINING IN TRANSFUSION SCIENCET32HL007209 · NHLBI · VERSITI WISCONSIN, INC. · PI WHITE, II, GILBERT C. · 1985 to 2019
$2.9M
The Biochemistry and Physiology of Platelet TFPIK01HL096419 · NHLBI · VERSITI WISCONSIN, INC. · PI MARONEY, SUSAN ANTONE · 2009 to 2013
$626k
NCATS NIH HHS UL1 TR000055NHLBI NIH HHS HL007209NHLBI NIH HHS HL068835NHLBI NIH HHS HL091469NHLBI NIH HHS K01 HL096419NHLBI NIH HHS R01 HL068835NHLBI NIH HHS R01 HL091469NHLBI NIH HHS T32 HL007209
6 · The paper itself

Abstract

TFPI (tissue factor pathway inhibitor) is an anticoagulant protein that prevents intravascular coagulation through inhibition of fXa (Factor Xa) and the TF (tissue factor)-fVIIa (Factor VIIa) complex. Localization of TFPI within caveolae enhances its anticoagulant activity. To define further how caveolae contribute to TFPI anticoagulant activity, CHO (Chinese-hamster ovary) cells were co-transfected with TF and membrane-associated TFPI targeted to either caveolae [TFPI-GPI (TFPI-glycosylphosphatidylinositol anchor chimaera)] or to bulk plasma membrane [TFPI-TM (TFPI-transmembrane anchor chimaera)]. Stable clones had equal expression of surface TF and TFPI. TX-114 cellular lysis confirmed localization of TFPI-GPI to detergent-insoluble membrane fractions, whereas TFPI-TM localized to the aqueous phase. TFPI-GPI and TFPI-TM were equally effective direct inhibitors of fXa in amidolytic assays. However, TFPI-GPI was a significantly better inhibitor of TF-fVIIa than TFPI-TM, as measured in both amidolytic and plasma-clotting assays. Disrupting caveolae by removing membrane cholesterol from EA.hy926 cells, which make TFPIα, CHO cells transfected with TFPIβ and HUVECs (human umbilical vein endothelial cells) did not affect their fXa inhibition, but significantly decreased their inhibition of TF-fVIIa. These studies confirm and quantify the enhanced anticoagulant activity of TFPI localized within caveolae, demonstrate that caveolae enhance the inhibitory activity of both TFPI isoforms and define the effect of caveolae as specifically enhancing the anti-TF activity of TFPI.

Indexed as

Animalsbeta-CyclodextrinsBlood CoagulationBlood Coagulation TestsCaveolaeCell MembraneCHO CellsCholesterolCricetinaeFactor VIIaFactor XaFactor Xa InhibitorsGPI-Linked ProteinsHumansHuman Umbilical Vein Endothelial CellsLipoproteinsbeta-CyclodextrinsCholesterolFactor VIIaFactor XaFactor Xa InhibitorsGPI-Linked Proteinslipoprotein-associated coagulation inhibitorLipoproteinsmethyl-beta-cyclodextrinRecombinant Fusion Proteins

Identifiers

PMID22239091
PMCPMC3549619
OpenAlexW2032030304

What OpenQuestion holds

Textmetadata
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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.