Evidence map›Paper›PMID 19540581›Full record

ArticleBiomaterials2009

The phosphorylation of vascular endothelial growth factor receptor-2 (VEGFR-2) by engineered surfaces with electrostatically or covalently immobilized VEGF.

Sean M Anderson, Tom T Chen, M Luisa Iruela-Arispe, Tatiana Segura

Open access · hybridAbstract read
In one paragraph

Article in Biomaterials, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

31 citing papers in PubMed, 91 citations in OpenAlex.

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  12. Engineering Approaches to Study Cellular Decision Making.Annual review of biomedical engineering · 2018
    Review
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  19. Rac1 GTPase silencing counteracts microgravity-induced effects on osteoblastic cells.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2014
    Article
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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

4 authors at 1 institution in 1 country.

Sean M AndersonUniversity of California, Los Angeles, Chemical and Biomolecular Engineering Department, Los Angeles, CA 90095, USA.
Tom T Chen
M Luisa Iruela-Arispe
Tatiana Segura
University of California, Los Angeles · US

Funding

Biotechnology Training in Biomedical Sciences and EngineeringT32GM067555 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI GU, ZHEN · 2005 to 2019
$2.8M
Understanding the Role of the Extracellular Matrix on Non-viral Gene TransferR21EB009516 · NIBIB · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI SEGURA, TATIANA · 2009 to 2010
$397k
NIBIB NIH HHS R21 EB009516NIGMS NIH HHS T32 GM067555
6 · The paper itself

Abstract

Growth factors are a class of signaling proteins that direct cell fate through interaction with cell-surface receptors. Although a myriad of possible cell fates stems from a growth factor binding to its receptor, the signaling cascades that result in one fate over another are still being elucidated. One possible mechanism by which nature modulates growth factor signaling is through the method of presentation of the growth factor--soluble or immobilized (matrix bound). Here we present the methodology to study signaling of soluble versus immobilized VEGF through VEGFR-2. We have designed a strategy to covalently immobilize VEGF using its heparin-binding domain to orient the molecule (bind) and a secondary functional group to mediate covalent binding (lock). This bind-and-lock approach aims to allow VEGF to assume a bioactive orientation before covalent immobilization. Surface plasmon resonance (SPR) demonstrated heparin and VEGF binding with surface densities of 60 ng/cm2 and 100 pg/cm2, respectively. ELISA experiments confirmed VEGF surface density and showed that electrostatically bound VEGF releases in cell medium and heparin solutions while covalently bound VEGF remains immobilized. Electrostatically bound VEGF and covalently bound VEGF phosphorylate VEGFR-2 in both VEGFR-2 transfected cells and VEGFR-2 endogenously producing cells. HUVECs plated on VEGF functionalized surfaces showed different morphologies between surface-bound VEGF and soluble VEGF. The surfaces synthesized in these studies allow for the study of VEGF/VEGFR-2 signaling induced by covalently bound, electrostatically bound, and soluble VEGF and may provide further insight into the design of materials for the generation of a mature and stable vasculature.

Indexed as

Static ElectricityAnimalsBlotting, WesternCell AdhesionCell LineCell MovementCell ProliferationEndothelial CellsEnzyme-Linked Immunosorbent AssayGoldHeparinHumansImmobilized ProteinsMicroscopy, FluorescenceOxidation-ReductionPhosphorylationGoldHeparinImmobilized ProteinsVascular Endothelial Growth Factor AVascular Endothelial Growth Factor Receptor-2

Identifiers

PMID19540581
PMCPMC2826152
OpenAlexW2010635120

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.