Related Experiment Video

Updated: Jun 23, 2026

A Simple Bioassay for the Evaluation of Vascular Endothelial Growth Factors
09:04

A Simple Bioassay for the Evaluation of Vascular Endothelial Growth Factors

Published on: March 15, 2016

Insulin-like growth factor binding protein-7 (IGFBP7) blocks vascular endothelial cell growth factor (VEGF)-induced

Kazuhiro Tamura1, Keisuke Hashimoto, Kenta Suzuki

  • 1Department of Endocrine Pharmacology, Tokyo University of Pharmacy & Life Sciences, Horinouchi 1432-1, Hachioji, Tokyo, 192-0392, Japan. hiro@ps.toyaku.ac.jp

European Journal of Pharmacology
|April 21, 2009
PubMed

Insights

Insulin-like growth factor binding protein-7 (IGFBP7) inhibits vascular endothelial growth factor (VEGF)-induced angiogenesis by suppressing VEGF signaling and expression, not by inducing apoptosis. This modulation impacts tumor vascularization.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Cancer Research

Background:

  • Insulin-like growth factor binding protein-7 (IGFBP7) and vascular endothelial growth factor (VEGF) are implicated in tumor angiogenesis.
  • VEGF is a key driver of blood vessel formation in tumors, promoting endothelial cell proliferation and migration.
  • The precise role of IGFBP7 in modulating VEGF-driven angiogenesis requires further elucidation.

Purpose of the Study:

  • To investigate the effect of IGFBP7 on VEGF-induced angiogenesis in human umbilical vein endothelial cells (HUVECs).
  • To determine the mechanisms by which IGFBP7 influences VEGF signaling pathways.
  • To assess whether IGFBP7 induces apoptosis in the context of VEGF stimulation.

Main Methods:

  • Treatment of HUVECs with IGFBP7 and VEGF.
  • Assessment of tube formation, cell proliferation, and protein phosphorylation (MEK, ERK1/2).
  • Measurement of cyclooxygenase-2 (COX-2) and VEGF mRNA expression, prostaglandin E(2) secretion, and caspase activity.

Main Results:

  • IGFBP7 suppressed VEGF-induced HUVEC tube formation, proliferation, and MEK/ERK phosphorylation.
  • IGFBP7 attenuated VEGF-enhanced COX-2 and VEGF mRNA expression and prostaglandin E(2) secretion.
  • Knockdown of endogenous IGFBP7 increased COX-2 and VEGF mRNA expression; IGFBP7 did not increase caspases in the presence of VEGF.

Conclusions:

  • IGFBP7 modulates VEGF-stimulated angiogenesis by interfering with VEGF expression and signaling pathways.
  • The anti-angiogenic effect of IGFBP7 is not mediated by the induction of apoptosis.
  • IGFBP7 represents a potential target for anti-angiogenic therapies in cancer.

More Related Videos

Modified In Vivo Matrix Gel Plug Assay for Angiogenesis Studies09:03

Modified In Vivo Matrix Gel Plug Assay for Angiogenesis Studies

Published on: June 30, 2023

In Vitro Three-Dimensional Sprouting Assay of Angiogenesis Using Mouse Embryonic Stem Cells for Vascular Disease Modeling and Drug Testing08:04

In Vitro Three-Dimensional Sprouting Assay of Angiogenesis Using Mouse Embryonic Stem Cells for Vascular Disease Modeling and Drug Testing

Published on: May 11, 2021

Related Concept Videos

Regulation of Angiogenesis and Blood Supply01:24

Regulation of Angiogenesis and Blood Supply

Rapidly dividing tumors, embryos, and wounded tissues require more oxygen than usual, lowering the oxygen concentration in the blood. At low oxygen or hypoxic conditions, an oxygen-sensitive transcription factor called the hypoxia-inducible factor 1 or HIF1 is activated. HIF1 is a dimeric protein of alpha (ɑ) and beta (β) subunits.  Under optimal oxygen conditions, HIF1β is present in the nucleus while HIF1ɑ remains in the cytosol. HIF1ɑ is hydroxylated by prolyl hydroxylase and factor...
Mechanism of Angiogenesis01:10

Mechanism of Angiogenesis

Blood vessel formation starts early during embryonic development, around day 7. In the extraembryonic yolk sac, mesodermal precursor cells called hemangioblast proliferate and differentiate into angioblast. Angioblasts express vascular endothelial growth factor receptor 2 or VEGFR2, which binds VEGF-A, a proangiogenic factor, guiding blood vessel formation. VEGF signaling promotes angioblasts to form a blood island in the developing embryo. Angioblasts further differentiate, giving rise to...
PI3K/mTOR/AKT Signaling Pathway01:22

PI3K/mTOR/AKT Signaling Pathway

The mammalian target of rapamycin  (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1  (mTORC1) and mTOR complex 2  (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast,  mTORC2 consists of a rapamycin-insensitive companion...