Evidence map›Paper›PMID 22733256›Full record

ArticleIntegrative biology : quantitative biosciences from nano to macro2012

Differential effects of a soluble or immobilized VEGFR-binding peptide.

Justin T Koepsel, Eric H Nguyen, William L Murphy

Open access · greenAbstract read
In one paragraph

Article in Integrative biology : quantitative biosciences from nano to macro, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.7field-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

16 citing papers in PubMed, 32 citations in OpenAlex.

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  15. Patterned self-assembled monolayers: efficient, chemically defined tools for cell biology.Chembiochem : a European journal of chemical biology · 2012
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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

3 authors at 1 institution in 1 country.

Justin T KoepselDepartment of Biomedical Engineering, University of Wisconsin - Madison, 1550 Engineering Dr., Engineering Centers Building, Madison, WI 53706, USA.
Eric H Nguyen
William L Murphy
University of Wisconsin–Madison · US

Funding

BIOTECHNOLOGY TRAINING PROGRAMT32GM008349 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI FOX, BRIAN G · 1989 to 2019
$22.5M
Biomaterials for local regulation of growth factor signalingR01HL093282 · NHLBI · UNIVERSITY OF WISCONSIN-MADISON · PI MURPHY, WILLIAM L. · 2009 to 2018
$3.3M
ACQUISITION OF MASS SPECTROMETER FOR CORE FACILITYS10RR013790 · NCRR · UNIVERSITY OF WISCONSIN MADISON · PI RAINES, RONALD T · 1999 to 1999
–
NCRR NIH HHS S10 RR013790NHLBI NIH HHS R01 HL093282NHLBI NIH HHS R01HL093282NIGMS NIH HHS 5 T32GM08349NIGMS NIH HHS T32 GM008349
6 · The paper itself

Abstract

Regulating endothelial cell behavior is a key step in understanding and controlling neovascularization for both pro-angiogenic and anti-angiogenic therapeutic strategies. Here, we characterized the effects of a covalently immobilized peptide mimic of vascular endothelial growth factor, herein referred to as VEGF receptor-binding peptide (VR-BP), on human umbilical vein endothelial cell (HUVEC) behavior. Self-assembled monolayer arrays presenting varied densities of covalently immobilized VR-BP and varied densities of the fibronectin-derived cell adhesion peptide Gly-Arg-Gly-Asp-Ser-Pro (GRGDSP) were used to probe for changes in HUVEC attachment, proliferation and tubulogenesis. In a soluble form, VR-BP exhibited pro-angiogenic effects in agreement with previous studies, indicated by increases in HUVEC proliferation. However, when presented to cells in an insoluble context, covalently immobilized VR-BP inhibited several pro-angiogenic HUVEC behaviors, including attachment and proliferation, and also inhibited HUVEC response to soluble recombinant VEGF protein. Furthermore, substrates with covalently immobilized VR-BP also modulated HUVEC tubulogenesis when a matrigel overlay assay was used to provide cells with a pseudo-three dimensional environment. Taken together, these results demonstrate that the context in which ligands are presented to cell surface receptors strongly influences their effects, and that the same ligand can be an agonist or an antagonist depending on the manner of presentation to the cell.

Indexed as

AdsorptionAmino Acid SequenceCell AdhesionCell Culture TechniquesCell MembraneCell ProliferationCircular DichroismElastomersFluorescent DyesHumansHuman Umbilical Vein Endothelial CellsLigandsModels, BiologicalMolecular Sequence DataOligopeptidesPeptidesElastomersFluorescent Dyesglycyl-arginyl-glycyl-aspartyl-seryl-prolineLigandsOligopeptidesPeptidesReceptors, Vascular Endothelial Growth Factor

Identifiers

PMID22733256
PMCPMC3415255
OpenAlexW2075168250

What OpenQuestion holds

Textmetadata
LicenceTDM
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.