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J Biol Chem, Vol. 274, Issue 24, 16831-16837, June 11, 1999
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From the NG2 is a transmembrane chondroitin sulfate
proteoglycan that is expressed by immature progenitor cells in several
developmental lineages and by some types of malignant cells. In
vitro studies have suggested that NG2 participates in growth
factor activation of the platelet-derived growth factor- The Burnham Institute Cancer Research
Center, La Jolla, California 92037
receptor.
In this study the ability of recombinant NG2 core protein to interact
with several different growth factors (epidermal growth factor (EGF),
basic fibroblast growth factor (bFGF), platelet-derived growth factor (PDGF)-AA, PDGF-BB, vascular endothelial growth factor
(VEGF)165 and transforming growth factor (TGF)-
1) was
investigated using two different assay systems: enzyme-linked
immunosorbent assay-type solid-phase binding and an optical biosensor
(BIAcore) system. High-affinity binding of bFGF and PDGF-AA to the core
protein of NG2 could be demonstrated with both types of assays. Using both the BIAcore software analysis program and nonlinear regression analysis of the solid phase binding data, KD values
in the low nanomolar range were obtained for binding of each of these growth factors to NG2. The results further indicate that NG2 contains at least two binding sites for each of these two growth factors. PDGF-BB, TGF-1, VEGF, and EGF exhibited little or no binding to NG2
in either type of assay. These data suggest that NG2 can have an
important role in organizing and presenting some types of mitogenic
growth factors at the cell surface.
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