Evidence map›Paper›PMID 33537548›Full record

ArticleResearch and practice in thrombosis and haemostasis2021

Inhibition of platelet adhesion, thrombus formation, and fibrin formation by a potent αIIbβ3 integrin inhibitor from ticks.

Danique L van den Kerkhof, Magdolna Nagy, Kanin Wichapong, Sanne L N Brouns, Johan W M Heemskerk, Tilman M Hackeng, Ingrid Dijkgraaf

Open access · goldAbstract read
In one paragraph

Article in Research and practice in thrombosis and haemostasis, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.3field-weighted citation impact, top 17% 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

10 citing papers in PubMed, 14 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

7 authors at 1 institution in 1 country.

Danique L van den KerkhofDepartment of Biochemistry Cardiovascular Research Institute Maastricht (CARIM) Maastricht University Maastricht The Netherlands.
Magdolna NagyDepartment of Biochemistry Cardiovascular Research Institute Maastricht (CARIM) Maastricht University Maastricht The Netherlands.
Kanin WichapongDepartment of Biochemistry Cardiovascular Research Institute Maastricht (CARIM) Maastricht University Maastricht The Netherlands.
Sanne L N BrounsDepartment of Biochemistry Cardiovascular Research Institute Maastricht (CARIM) Maastricht University Maastricht The Netherlands.
Johan W M HeemskerkDepartment of Biochemistry Cardiovascular Research Institute Maastricht (CARIM) Maastricht University Maastricht The Netherlands.
Tilman M HackengDepartment of Biochemistry Cardiovascular Research Institute Maastricht (CARIM) Maastricht University Maastricht The Netherlands.
Ingrid DijkgraafDepartment of Biochemistry Cardiovascular Research Institute Maastricht (CARIM) Maastricht University Maastricht The Netherlands.
Maastricht University · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundTicks puncture the skin of their hosts and secrete saliva, containing antiplatelet proteins, into the blood. Here, we studied disagregin, a potent platelet-inhibiting protein derived from the salivary glands of

objectivesWe aimed to compare the inhibitory effects of disagregin and its RGD variant (RGD-disagregin) on platelet activation and to unravel the molecular basis of disagregin-αIIbβ3 integrin interactions.

methodsDisagregin and RGD-disagregin were synthesized by tert-butyloxycarbonyl -based solid-phase peptide synthesis. Effects of both disagregins on platelet aggregation were assessed by light transmission aggregometry in human platelet-rich plasma. Whole-blood thrombus formation was investigated by perfusing blood over collagen I with and without tissue factor at a high wall-shear rate (1000 s

resultsDisagregin showed inhibition of collagen- and ADP-induced platelet aggregation with half maximal inhibitory concentration values of 64 and 99 nM, respectively. This resembled the complete antiaggregatory effect of eptifibatide. Multiparameter assessment of thrombus formation showed highly suppressed platelet adhesion and aggregate formation with both disagregins, in contrast to eptifibatide treatment, which incompletely blocked aggregation under flow. Fibrin formation under flow was delayed by both disagregin and RGD-disagregin (

conclusionsBoth αIIbβ3-blocking disagregins have a strong potential to suppress collagen-tissue factor-mediated platelet adhesion, thrombus formation, and fibrin formation. Both disagregins can be seen as potential new αIIbβ3 inhibitors.

Indexed as

blood coagulationplatelet activationplatelet aggregation inhibitorssynthetic chemistry techniquesticks

Identifiers

PMID33537548
PMCPMC7845065
OpenAlexW3117866106

What OpenQuestion holds

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LicenceCC BY-NC-ND
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Registered trials

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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.