Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Functionally active VEGF fusion proteins.

M V Backer1, J M Backer

  • 1Sib Tech, Incorporated, 705 North Mountain Road, Newington, Connecticut 06111, USA. mbacker@sibtech.com

Protein Expression and Purification
|September 26, 2001
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Phosphoinositide 3-kinase signaling is critical for ErbB3-driven breast cancer cell motility and metastasis.

Oncogene·2011
Same author

Regulation of class III (Vps34) PI3Ks.

Biochemical Society transactions·2007
Same author

Regulation of class IA PI3Ks.

Biochemical Society transactions·2007
Same author

Human VPS34 is required for internal vesicle formation within multivesicular endosomes.

The Journal of cell biology·2002
Same author

Targeting endothelial cells overexpressing VEGFR-2: selective toxicity of Shiga-like toxin-VEGF fusion proteins.

Bioconjugate chemistry·2001
Same author

Distinct roles of class I and class III phosphatidylinositol 3-kinases in phagosome formation and maturation.

The Journal of cell biology·2001
Same journal

Expression of a recombinant DIVA antigen for differential diagnosis of H7N9 subtype avian influenza virus infected and vaccinated chickens.

Protein expression and purification·2026
Same journal

Prokaryotic expression, purification of Tldi1 protein and preparation of its polyclonal antibody in Salmonella Typhimurium.

Protein expression and purification·2026
Same journal

Soluble expression, two-step purification and tagmentation-compatible activity assessment of hyperactive Tn5 transposase using a GB1 fusion tag strategy.

Protein expression and purification·2026
Same journal

High-level soluble production of firefly luciferase in E. coli via promoter engineering.

Protein expression and purification·2026
Same journal

Rapid generation of Drosophila Schneider 2 (S2) cell lines and FACS-based isolation of high-yield soluble or membrane proteins.

Protein expression and purification·2026
Same journal

Heterologous expression and characterization of multi-resistant manganese superoxide dismutase from Thermus aquaticus in Escherichiacoli.

Protein expression and purification·2026
See all related articles

Vascular endothelial growth factor (VEGF) fusion proteins, engineered with N-terminal extensions, activate VEGFR-2 signaling and cell responses. These modified VEGF proteins show potential for targeted delivery in angiogenesis research.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Angiogenesis, the formation of new blood vessels, is regulated by vascular endothelial growth factor (VEGF).
  • VEGF exerts its effects through specific receptors, primarily VEGFR-2, which are upregulated at sites of angiogenesis.
  • Targeted delivery of therapeutic agents to angiogenic sites is a significant challenge in medicine.

Purpose of the Study:

  • To investigate the biological activity of VEGF fusion proteins with N-terminal extensions.
  • To assess the potential of these fusion proteins for receptor-mediated targeting in angiogenesis.

Main Methods:

  • Construction, expression in E. coli, and purification of human VEGF fusion proteins (VEGF121, VEGF165, VEGF189) with a 158-amino acid N-terminal extension.

Related Experiment Videos

  • Assays to measure VEGFR-2 autophosphorylation and downstream signaling.
  • Cell contraction assays in cells overexpressing VEGFR-2.
  • Main Results:

    • VEGF fusion proteins successfully induced VEGFR-2 autophosphorylation and downstream signaling.
    • These fusion proteins also triggered cell contraction in VEGFR-2-overexpressing cells.
    • While N-terminal extensions reduced binding affinity to VEGFR-2, the fusion proteins were effective at saturating concentrations.

    Conclusions:

    • VEGF fusion proteins retain biological activity and can stimulate VEGFR-2 signaling pathways.
    • These engineered proteins demonstrate potential as vehicles for targeted delivery to endothelial cells involved in angiogenesis.