Evidence map›Paper›PMID 42001946›Full record

ArticleThe Journal of biological chemistry2026

Antibodies blocking PlGF or VEGF interactions with the NRP1 receptor mediate antiproliferative effects.

Samuel A Blackman, Ahlam N Qerqez, Alison G Lee, Nicole V Johnson, Justin M Owens, Grace S Lai, Emma C Aldrich, Kayla G Sprenger, Jangsoon Lee, Sophie Verrier and 3 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

13 authors.

Samuel A BlackmanMcKetta Department of Chemical Engineering, The University of Texas at Austin, Austin, Texas, USA.
Ahlam N QerqezMcKetta Department of Chemical Engineering, The University of Texas at Austin, Austin, Texas, USA.
Alison G LeeInterdisciplinary Life Sciences Graduate Program, The University of Texas at Austin, Austin, Texas, USA.
Nicole V JohnsonInterdisciplinary Life Sciences Graduate Program, The University of Texas at Austin, Austin, Texas, USA.
Justin M OwensMcKetta Department of Chemical Engineering, The University of Texas at Austin, Austin, Texas, USA.
Grace S LaiMcKetta Department of Chemical Engineering, The University of Texas at Austin, Austin, Texas, USA.
Emma C AldrichDepartment of Chemical and Biological Engineering, University of Colorado Boulder, Boulder, Colorado, USA.
Kayla G SprengerDepartment of Chemical and Biological Engineering, University of Colorado Boulder, Boulder, Colorado, USA.
Jangsoon LeeUniversity of Hawaii Comprehensive Cancer Center, University of Hawaii, Honolulu, Hawaii, USA.
Sophie VerrierAO Research Institute Davos, Davos, Switzerland.
Martin J StoddartAO Research Institute Davos, Davos, Switzerland.
Annalee W NguyenMcKetta Department of Chemical Engineering, The University of Texas at Austin, Austin, Texas, USA. Electronic address: nguyen@che.utexas.edu.
Jennifer A MaynardMcKetta Department of Chemical Engineering, The University of Texas at Austin, Austin, Texas, USA. Electronic address: maynard@che.utexas.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Antibodies blocking the function of vascular endothelial growth factor A (VEGFA) remain a promising therapeutic strategy, especially when combined with check-point inhibitors, but their efficacy is limited by tumor resistance. This can occur via multiple mechanisms, including upregulation of placental growth factor 2 (PlGF-2), an alternative ligand for VEGF receptor 1 (VEGFR1) and neuropilin receptor 1 (NRP1). The activity of both growth factors is mediated by interactions with multiple receptors and extra-cellular matrix components, which complicates efforts to understand their contributions to cancer progression. To address this, we aimed to discover new antibodies with precision blockade of PlGF-2 or VEGFA binding to NRP1 in the presence of heparin that complement existing resources to probe PlGF and VEGFA biology. Limiting angiogenesis to promote vascular normalization is one mechanism of anti-VEGF protection; here, anti-VEGFA antibodies blocking interactions with VEGFR1 and NRP1 reduced HUVEC tube formation in a physiological angiogenesis model. By contrast, antibodies binding PlGF-2 or VEGFA to block NRP1 significantly reduced proliferation and migration of Caki-I kidney carcinoma cells in vitro, indicating this receptor mediates additional effects. Interestingly, one antibody exhibited dual-reactive binding to VEGFA and PlGF-2, suggesting a novel therapeutic strategy to prevent PlGF-driven VEGF-resistance. Overall, these antibodies define new mechanisms to disrupt PlGF activity and support a role for NRP1 in cell proliferation.

Indexed as

AntibodiesNeuropilin-1Placenta Growth FactorVascular Endothelial Growth Factor ACell ProliferationHumansHuman Umbilical Vein Endothelial CellsVascular Endothelial Growth Factor Receptor-1AntibodiesNeuropilin-1NRP1 protein, humanPGF protein, humanPlacenta Growth FactorVascular Endothelial Growth Factor AVascular Endothelial Growth Factor Receptor-1VEGFA protein, humanangiogenesisantibodyheparinNRP1phage displayPlGFVEGFVEGFR1

Identifiers

PMID42001946
PMCPMC13208732

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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.