Evidence map›Paper›PMID 32917131›Full record

ArticleBMC molecular and cell biology2020

Platelet adhesion and aggregate formation controlled by immobilised and soluble VWF.

Matthias F Schneider, Mohammad A Fallah, Christian Mess, Tobias Obser, Reinhard Schneppenheim, Alfredo Alexander-Katz, Stefan W Schneider, Volker Huck

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in BMC molecular and cell biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.6field-weighted citation impact, top 28% 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

11 citing papers in PubMed, 19 citations in OpenAlex.

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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 4 institutions in 2 countries.

Matthias F SchneiderDepartment of Physics, Medical and Biological Physics, Technical University Dortmund, Emil-Figge-Str. 50, 44227, Dortmund, Germany.
Mohammad A FallahDepartment of Chemistry, University of Konstanz, Universitätsstr. 10, 78457, Constance, Germany.
Christian MessUniversity Medical Centre Hamburg-Eppendorf, Centre for Internal Medicine, Martinistr. 52, 20246, Hamburg, Germany.
Tobias ObserDepartment of Paediatric Haematology and Oncology, University Medical Centre Hamburg-Eppendorf, Martinistr. 52, 20246, Hamburg, Germany.
Reinhard SchneppenheimDepartment of Paediatric Haematology and Oncology, University Medical Centre Hamburg-Eppendorf, Martinistr. 52, 20246, Hamburg, Germany.
Alfredo Alexander-KatzDepartment of Materials Science and Engineerin, Massachusetts Institute of Technology, 400 Technology Sq. (NE46-605), Cambridge, MA, 02139, USA.
Stefan W SchneiderUniversity Medical Centre Hamburg-Eppendorf, Centre for Internal Medicine, Martinistr. 52, 20246, Hamburg, Germany.
Volker HuckUniversity Medical Centre Hamburg-Eppendorf, Centre for Internal Medicine, Martinistr. 52, 20246, Hamburg, Germany. v.huck@uke.de.ORCID https://orcid.org/0000-0001-8988-1091
Universität Hamburg · DEMassachusetts Institute of Technology · USTU Dortmund University · DEUniversity of Konstanz · DE

Funding

Deutsche Forschungsgemeinschaft FOR1543 TP A1Deutsche Forschungsgemeinschaft FOR1543 TP A2Deutsche Forschungsgemeinschaft FOR1543 TP B1Deutsche Forschungsgemeinschaft TP A9
6 · The paper itself

Abstract

backgroundIt has been demonstrated that von Willebrand factor (VWF) mediated platelet-endothelium and platelet-platelet interactions are shear dependent. The VWF's mobility under dynamic conditions (e.g. flow) is pivotal to platelet adhesion and VWF-mediated aggregate formation in the cascade of VWF-platelet interactions in haemostasis.

resultsCombining microfluidic tools with fluorescence and reflection interference contrast microscopy (RICM), here we show, that specific deletions in the A-domains of the biopolymer VWF affect both, adhesion and aggregation properties independently. Intuitively, the deletion of the A1-domain led to a significant decrease in both adhesion and aggregate formation of platelets. Nevertheless, the deletion of the A2-domain revealed a completely different picture, with a significant increase in formation of rolling aggregates (gain of function). We predict that the A2-domain effectively 'masks' the potential between the platelet glycoprotein (GP) Ib and the VWF A1-domain. Furthermore, the deletion of the A3-domain led to no significant variation in either of the two functional characteristics.

conclusionsThese data demonstrate that the macroscopic functional properties i.e. adhesion and aggregate formation cannot simply be assigned to the properties of one particular domain, but have to be explained by cooperative phenomena. The absence or presence of molecular entities likewise affects the properties (thermodynamic phenomenology) of its neighbours, therefore altering the macromolecular function.

Indexed as

BiopolymersBlood PlateletsCell LineFluorescenceHEK293 CellsHemostasisHumansMicrofluidicsMicroscopyPlatelet AdhesivenessPlatelet AggregationPlatelet Glycoprotein GPIb-IX Complexvon Willebrand FactorBiopolymersPlatelet Glycoprotein GPIb-IX Complexvon Willebrand FactorPlatelet adhesionPrimary haemostasisShear activationVon Willebrand factor

Identifiers

PMID32917131
PMCPMC7488753
OpenAlexW3085707778

What OpenQuestion holds

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LicenceCC BY
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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.