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Updated: Jul 29, 2026

Monitoring Functionality and Morphology of Vasculature Recruited by Factors Secreted by Fast-growing Tumor-generating Cells
Published on: November 23, 2014
Angiogenic role for glycodelin in tumorigenesis.
M Song1, S Ramaswamy, S Ramachandran
1Department of Gynecology and Obstetrics, Emory University School of Medicine, Atlanta, GA 30322, USA.
Glycodelin promotes blood vessel formation (angiogenesis) in tumors and embryogenesis. This protein stimulates vascular endothelial growth factor (VEGF) release, crucial for new blood vessel growth.
Area of Science:
- Biochemistry
- Cell Biology
- Oncology
Background:
- Angiogenesis is vital for tumor neovascularization.
- Glycodelin, a hormone-responsive protein, is found in gynecological tumors and endothelial cells.
- High glycodelin levels correlate with gynecological malignancies.
Purpose of the Study:
- To investigate the pro-angiogenic effects of glycodelin and its synthetic peptide (Gp).
- To determine if glycodelin promotes endothelial cell migration and tube formation.
- To explore the role of vascular endothelial growth factor (VEGF) in glycodelin-mediated angiogenesis.
Main Methods:
- Assessed human umbilical cord vein endothelial cell (HUVEC) migration and tube formation.
- Utilized glycodelin-rich amniotic fluid and a synthetic glycodelin peptide (Gp).
- Measured VEGF protein and mRNA expression, and VEGF receptor Flt-1 mRNA expression in various cell lines.
Main Results:
- Amniotic fluid and Gp significantly increased HUVEC migration and tube formation.
- These effects were inhibited by anti-Gp and anti-VEGF antibodies, indicating VEGF mediation.
- Gp elevated VEGF release and mRNA expression in multiple cancer and endothelial cell lines.
- Gp also increased VEGF receptor Flt-1 mRNA expression in HUVECs.
Conclusions:
- Glycodelin promotes angiogenesis, potentially via VEGF.
- Glycodelin may play a significant role in embryogenesis and tumor neovascularization.
- Glycodelin's immunosuppressive properties might also contribute to its role in tumor development.
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Activation of Integrins
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding events provide an effective stimulus.

