Evidence map›Paper›PMID 21658003›Full record

ArticleBioscience reports2012

Binding affinities of vascular endothelial growth factor (VEGF) for heparin-derived oligosaccharides.

Wenjing Zhao, Scott A McCallum, Zhongping Xiao, Fuming Zhang, Robert J Linhardt

Open access · greenAbstract read
In one paragraph

Article in Bioscience reports, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
3.0field-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

49 citing papers in PubMed, 141 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Glycosaminoglycans as Polyelectrolytes: Charge, Interactions, and Applications.Chembiochem : a European journal of chemical biology · 2025
    Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Synthesis of Sulfated Carbohydrates - Glycosaminoglycans.Handbook of experimental pharmacology · 2025
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. New anti-angiogenic compound based on chemically modified heparin.Graefe's archive for clinical and experimental ophthalmology = Albrecht von Graefes Archiv fur klinische und experimentelle Ophthalmologie · 2022
    Article
  18. Article
  19. Article
  20. RNAscope for VEGF-A Detection in Human Tumor Bioptic Specimens.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
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

5 authors at 1 institution in 1 country.

Wenjing ZhaoDepartment of Biology, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY 12180, USA.
Scott A McCallum
Zhongping Xiao
Fuming Zhang
Robert J Linhardt
Rensselaer Polytechnic Institute · US

Funding

SEQUENCING THE POLYSACCHARIDE COMPONENT OF PROTEOGLYCANSR01GM038060 · NIGMS · UNIVERSITY OF IOWA · PI LINHARDT, ROBERT J · 1988 to 2012
$2.8M
NIGMS NIH HHS GM38060NIGMS NIH HHS R01 GM038060
6 · The paper itself

Abstract

Heparin and HS (heparan sulfate) exert their wide range of biological activities by interacting with extracellular protein ligands. Among these important protein ligands are various angiogenic growth factors and cytokines. HS binding to VEGF (vascular endothelial growth factor) regulates multiple aspects of vascular development and function through its specific interaction with HS. Many studies have focused on HS-derived or HS-mimicking structures for the characterization of VEGF165 interaction with HS. Using a heparinase 1-prepared small library of heparin-derived oligosaccharides ranging from hexasaccharide to octadecasaccharide, we systematically investigated the heparin-specific structural features required for VEGF binding. We report the apparent affinities for the association between the heparin-derived oligosaccharides with both VEGF165 and VEGF55, a peptide construct encompassing exclusively the heparin-binding domain of VEGF165. An octasaccharide was the minimum size of oligosaccharide within the library to efficiently bind to both forms of VEGF and a tetradecasaccharide displayed an effective binding affinity to VEGF165 comparable to unfractionated heparin. The range of relative apparent binding affinities among VEGF and the panel of heparin-derived oligosaccharides demonstrate that the VEGF binding affinity likely depends on the specific structural features of these oligosaccharides, including their degree of sulfation, sugar-ring stereochemistry and conformation. Notably, the unique 3-O-sulfo group found within the specific antithrombin binding site of heparin is not required for VEGF165 binding. These findings afford new insight into the inherent kinetics and affinities for VEGF association with heparin and heparin-derived oligosaccharides with key residue-specific modifications and may potentially benefit the future design of oligosaccharide-based anti-angiogenesis drugs.

Indexed as

Binding SitesHeparinHeparin LyaseHumansImmobilized ProteinsKineticsOligosaccharidesPeptide LibrarySurface Plasmon ResonanceVascular Endothelial Growth Factor AHeparinHeparin LyaseImmobilized ProteinsOligosaccharidesPeptide LibraryVascular Endothelial Growth Factor AVEGFA protein, human

Identifiers

PMID21658003
PMCPMC3190640
OpenAlexW2151280162

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.