High-affinity binding of basic fibroblast growth factor and platelet-derived growth factor-AA to the core protein of the NG2 proteoglycan
| Autor: | Michael A. Burg, Kathryn A. Grako, Lothar Goretzki, William B. Stallcup |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
Receptor
Platelet-Derived Growth Factor alpha Basic fibroblast growth factor Biology Biochemistry chemistry.chemical_compound Growth factor receptor Epidermal growth factor Growth factor receptor inhibitor Receptors Platelet-Derived Growth Factor Antigens Molecular Biology Platelet-Derived Growth Factor Fibroblast growth factor receptor 2 Cell Biology Fibroblast growth factor receptor 4 Fibroblast growth factor receptor 3 Surface Plasmon Resonance Molecular biology Receptors Fibroblast Growth Factor Peptide Fragments Recombinant Proteins Platelet-Derived Growth Factor-AA nervous system chemistry Fibroblast Growth Factor 2 Proteoglycans Protein Binding |
| Zdroj: | The Journal of biological chemistry. 274(24) |
| ISSN: | 0021-9258 |
| Popis: | 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-alpha 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)-beta1) 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-beta1, 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. |
| Databáze: | OpenAIRE |
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