Evidence map›Paper›PMID 21544310›Full record

ArticleThrombosis and haemostasis2011

Interaction of high-molecular-weight kininogen with endothelial cell binding proteins suPAR, gC1qR and cytokeratin 1 determined by surface plasmon resonance (BiaCore).

R A Pixley, R G Espinola, B Ghebrehiwet, K Joseph, A Kao, K Bdeir, D B Cines, R W Colman

Abstract read
In one paragraph

Article in Thrombosis and haemostasis, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

21 citing papers in PubMed, 44 citations in OpenAlex.

  1. Trial
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  8. Article
  9. Review
  10. Zinc chelation promotes streptokinase-induced thrombolysisInternational journal of physiology, pathophysiology and pharmacology · 2017
    Article
  11. Review
  12. Article
  13. Novel role for p56/Lck in regulation of endothelial cell survival and angiogenesis.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2016
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
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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

8 authors at 1 institution in 1 country.

R A PixleyThe Sol Sherry Thrombosis Research Center, Temple University School of Medicine, Philadelphia, PA 19140, USA.
R G Espinola
B Ghebrehiwet
K Joseph
A Kao
K Bdeir
D B Cines
R W Colman
Temple University · US

Funding

KININOGEN/UROKINASE RECEPTORS IN TUMOR ANGIOGENESISR01CA083121 · NCI · TEMPLE UNIV OF THE COMMONWEALTH · PI COLMAN, ROBERT W · 1999 to 2008
$3.0M
gC1q-R/p33: structure function and role on inflammation.R01AI060866 · NIAID · STATE UNIVERSITY NEW YORK STONY BROOK · PI GHEBREHIWET, BERHANE · 2006 to 2009
$1.2M
The role of C1q in regulation of monocyte to dendritic cell transitionR01AI084178 · NIAID · STATE UNIVERSITY NEW YORK STONY BROOK · PI GHEBREHIWET, BERHANE · 2009 to 2010
$602k
NCI NIH HHS R01 CA083121NIAID NIH HHS R01 AI060866NIAID NIH HHS R01 AI084178
6 · The paper itself

Abstract

The physiologic activation of the plasma kallikrein-kinin system requires the assembly of its constituents on a cell membrane. High- molecular-weight kininogen (HK) and cleaved HK (HKa) both interact with at least three endothelial cell binding proteins: urokinase plasminogen activator receptor (uPAR), globular C1q receptor (gC1qR,) and cytokeratin 1 (CK1). The affinity of HK and HKa for endothelial cells are KD=7-52 nM. The contribution of each protein is unknown. We examined the direct binding of HK and HKa to the soluble extracellular form of uPAR (suPAR), gC1qR and CK1 using surface plasmon resonance. Each binding protein linked to a CM-5 chip and the association, dissociation and KD (equilibrium constant) were measured. The interaction of HK and HKa with each binding protein was zinc-dependent. The affinity for HK and HKa was gC1qR>CK1>suPAR, indicating that gC1qR is dominant for binding. The affinity for HKa compared to HK was the same for gC1qR, 2.6-fold tighter for CK1 but 53-fold tighter for suPAR. Complex between binding proteins was only observed between gC1qR and CK1 indicating that a binary CK1-gC1qR complex can form independently of kininogen. Although suPAR has the weakest affinity of the three binding proteins, it is the only one that distinguished between HK and HKa. This finding indicates that uPAR may be a key membrane binding protein for differential binding and signalling between the cleaved and uncleaved forms of kininogen. The role of CK1 and gC1qR may be to initially bind HK to the membrane surface before productive cleavage to HKa.

Indexed as

Surface Plasmon ResonanceBlood CoagulationEndotheliumHumansKeratin-1KeratinsKininogen, High-Molecular-WeightMembrane GlycoproteinsProtein BindingReceptors, ComplementReceptors, Urokinase Plasminogen ActivatorSignal Transductioncomplement 1q receptorKeratin-1KeratinsKininogen, High-Molecular-WeightMembrane GlycoproteinsReceptors, ComplementReceptors, Urokinase Plasminogen Activator

Identifiers

PMID21544310
PMCPMC3149827
OpenAlexW2052053315

What OpenQuestion holds

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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.