Evidence map›Paper›PMID 32110917›Full record

ArticleMolecules (Basel, Switzerland)2020

Glycosaminoglycans as Tools to Decipher the Platelet Tumor Cell Interaction: A Focus on P-Selectin.

Svenja Schwarz, Lukas Maria Gockel, Annamaria Naggi, Uri Barash, Martina Gobec, Gerd Bendas, Martin Schlesinger

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.5field-weighted citation impact, top 9% 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

20 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
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  5. Epigenetic Targeting of Heparan Sulfate 3-ACS pharmacology & translational science · 2024
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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 3 institutions in 3 countries.

Svenja SchwarzPharmaceutical Institute, University of Bonn, An der Immenburg 4, 53121 Bonn, Germany.
Lukas Maria GockelPharmaceutical Institute, University of Bonn, An der Immenburg 4, 53121 Bonn, Germany.
Annamaria NaggiG. Ronzoni Institute for Chemical and Biochemical Research, Via G. Colombo 81, 20133 Milan, Italy.ORCID 0000-0002-1572-2271
Uri BarashCancer and Vascular Biology Research Center, Rappaport Faculty of Medicine, Technion, PO Box 9649, Haifa 31096, Israel.
Martina GobecFaculty of Pharmacy, University of Ljubljana, Aškerčeva 7, SI-1000 Ljubljana, Slovenia.
Gerd BendasPharmaceutical Institute, University of Bonn, An der Immenburg 4, 53121 Bonn, Germany.
Martin SchlesingerPharmaceutical Institute, University of Bonn, An der Immenburg 4, 53121 Bonn, Germany.
University of Bonn · DEIstituto di Ricerche Chimiche e Biochimiche G. Ronzoni · ITUniversity of Ljubljana · SI

Funding

Kirstin Diehl Stiftung , Neuwied, Germany /
6 · The paper itself

Abstract

Tumor cell-platelet interactions are regarded as an initial crucial step in hematogenous metastasis. Platelets protect tumor cells from immune surveillance in the blood, mediate vascular arrest, facilitate tumor extravasation, growth, and finally angiogenesis in the metastatic foci. Tumor cells aggregate platelets in the bloodstream by activation of the plasmatic coagulation cascade and by direct contact formation. Antimetastatic activities of unfractionated or low molecular weight heparin (UFH/LMWH) can undoubtedly be related to attenuated platelet activation, but molecular mechanisms and contribution of contact formation vs. coagulation remain to be elucidated. Using a set of non-anticoagulant heparin derivatives varying in size or degree of sulfation as compared with UFH, we provide insight into the relevance of contact formation for platelet activation. Light transmission aggregometry and ATP release assays confirmed that only those heparin derivatives with P-selectin blocking capacities were able to attenuate breast cancer cell-induced platelet activation, while pentasaccharide fondaparinux was without effects. Furthermore, a role of P-selectin in platelet activation and signaling could be confirmed by proteome profiler arrays detecting platelet kinases. In this study, we demonstrate that heparin blocks tumor cell-induced coagulation. Moreover, we identify platelet P-selectin, which obviously acts as molecular switch and controls aggregation and secretion of procoagulant platelets.

Indexed as

Blood PlateletsBreast NeoplasmsCell CommunicationCell Line, TumorCell ShapeCytoplasmic GranulesGlycosaminoglycansHeparinHumansNeoplasmsPlatelet ActivationPlatelet AggregationP-SelectinSignal TransductionGlycosaminoglycansHeparinP-Selectin2-O-desulfated heparindecasaccharide heparin fragmenthexasaccharide heparin fragmentlow molecular weight heparinplatelet aggregationplateletsplatelet secretionP-selectinRO-heparintumor metastasisunfractionated heparin

Identifiers

PMID32110917
PMCPMC7179249
OpenAlexW3008818246

What OpenQuestion holds

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LicenceCC BY
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.