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Structural features in heparin that interact with VEGF165 and modulate its biological activity
K Ono1, H Hattori, S Takeshita
1National Defense Medical College, Department of Surgery II, 3-2 Namiki, Tokorozawa, Saitama, 359-8513 Japan.
Glycobiology
|June 11, 1999
Summary
Heparin
Area of Science:
- Biochemistry
- Molecular Biology
- Cell Biology
Background:
- Vascular endothelial growth factor (VEGF165) is a key regulator of endothelial cell proliferation.
- Heparin and its derivatives are known to interact with growth factors, modulating their activity.
Purpose of the Study:
- To investigate the specific structural features of heparin required for interaction with VEGF165.
- To compare the interaction requirements of VEGF165 with those of other heparin-binding growth factors like FGF-2 and HGF.
Main Methods:
- Enzyme-linked immunosorbent assay (ELISA) to assess VEGF165-heparin interactions.
- Cell proliferation assays using human umbilical vein endothelial cells (HUVECs).
- Utilized various chemically modified heparin derivatives (N-desulfated, N-acetylated, 6-O-desulfated, 2-O-desulfated).
Main Results:
- Native heparin interacted with VEGF165, while N-desulfated, N-acetylated, and 6-O-desulfated heparin did not.
- 2-O-desulfated heparin retained interaction with VEGF165 but lost interaction with FGF-2 and HGF.
- Both native and 2-O-desulfated heparin showed inhibitory effects on VEGF165-induced HUVEC proliferation at high concentrations.
Conclusions:
- The structural requirements for heparin's specific interaction with VEGF165 differ from those for FGF-2 and HGF.
- A high content of 2-O-sulfate groups in heparin is not essential for VEGF165 binding but is crucial for its mitogenic activity.