Evidence map›Paper›PMID 20696943›Full record

ArticleBlood2010

von Willebrand factor self-association on platelet GpIbalpha under hydrodynamic shear: effect on shear-induced platelet activation.

Kannayakanahalli M Dayananda, Indrajeet Singh, Nandini Mondal, Sriram Neelamegham

Open access · bronzeAbstract read
In one paragraph

Article in Blood, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed, 1 pooled it
3.5field-weighted citation impact, top 7% 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

47 citing papers in PubMed, 1 synthesis or guideline pooled it, 81 citations in OpenAlex.

  1. Pooled it
  2. Laboratory Assessment and Clinical Outlook forAnnals of laboratory medicine · 2026
    Review
  3. Article
  4. Article
  5. Von Willebrand factor and hematogenous cancer metastasis under flow.Frontiers in cell and developmental biology · 2024
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
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  15. Article
  16. Article
  17. Review
  18. Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Kannayakanahalli M DayanandaChemical and Biological Engineering, State University of New York, Buffalo, NY 14260, USA.
Indrajeet Singh
Nandini Mondal
Sriram Neelamegham
University at Buffalo, State University of New York · US

Funding

VON WILLEBRAND FACTOR STRUCTURE-FUNCTION UNDE FLUID FLOWR01HL077258 · NHLBI · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI NEELAMEGHAM, SRIRAM · 2006 to 2015
$3.0M
FLUID FORCES REGULATING PROTEIN STRUCTURE AND FUNCTIONK02HL076211 · NHLBI · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI NEELAMEGHAM, SRIRAM · 2004 to 2008
$531k
NHLBI NIH HHS HL 76211NHLBI NIH HHS HL 77258NHLBI NIH HHS K02 HL076211NHLBI NIH HHS R01 HL077258
6 · The paper itself

Abstract

The function of the mechanosensitive, multimeric blood protein von Willebrand factor (VWF) is dependent on its size. We tested the hypothesis that VWF may self-associate on the platelet glycoprotein Ibα (GpIbα) receptor under hydrodynamic shear. Consistent with this proposition, whereas Alexa-488-conjugated VWF (VWF-488) bound platelets at modest levels, addition of unlabeled VWF enhanced the extent of VWF-488 binding. Recombinant VWF lacking the A1-domain was conjugated with Alexa-488 to produce ΔA1-488. Although ΔA1-488 alone did not bind platelets under shear, this protein bound GpIbα on addition of either purified plasma VWF or recombinant full-length VWF. The extent of self-association increased with applied shear stress more than ∼ 60 to 70 dyne/cm(2). ΔA1-488 bound platelets in the milieu of plasma. On application of fluid shear to whole blood, half of the activated platelets had ΔA1-488 bound, suggesting that VWF self-association may be necessary for cell activation. Shearing platelets with 6-μm beads bearing either immobilized VWF or anti-GpIbα mAb resulted in cell activation at shear stress down to 2 to 5 dyne/cm(2). Taken together, the data suggest that fluid shear in circulation can increase the effective size of VWF bound to platelet GpIbα via protein self-association. This can trigger mechanotransduction and cell activation by enhancing the drag force applied on the cell-surface receptor.

Indexed as

Antibodies, MonoclonalBlood PlateletsHemorheologyHumansHydrodynamicsIn Vitro TechniquesMechanotransduction, CellularPlatelet ActivationPlatelet Glycoprotein GPIb-IX ComplexProtein BindingProtein MultimerizationRecombinant ProteinsStress, Mechanicalvon Willebrand FactorAntibodies, MonoclonalPlatelet Glycoprotein GPIb-IX ComplexRecombinant Proteinsvon Willebrand Factor

Identifiers

PMID20696943
PMCPMC2981547
OpenAlexW2029837592

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.