IGFBP-3 and IGFBP-5 association with endothelial cells: role of C-terminal heparin binding domain
| Autor: | B A, Booth, M, Boes, D L, Andress, B L, Dake, M C, Kiefer, C, Maack, R J, Linhardt, K, Bar, E E, Caldwell, J, Weiler |
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| Rok vydání: | 1995 |
| Předmět: |
Chromatography
Binding Sites Glycosylation Heparin Sulfates Molecular Sequence Data Binding Competitive Peptide Fragments Extracellular Matrix Insulin-Like Growth Factor Binding Proteins Heparin Lyase Chlorates Animals Cattle Amino Acid Sequence Endothelium Vascular Heparitin Sulfate Protamines Carrier Proteins Insulin-Like Growth Factor Binding Protein 5 Glycosaminoglycans Polysaccharide-Lyases |
| Zdroj: | Growth regulation. 5(1) |
| ISSN: | 0956-523X |
| Popis: | IGFBP-3 and IGFBP-5, but not the other 4 IGF binding proteins, specifically bound to endothelial cell (EC) monolayers. Charged compounds, such as heparin and heparan sulfate, competed for this binding. Of the 6 IGFBPs, IGFBP-3 and IGFBP-5 had the greatest heparin affinity. Peptides of 18 amino acids were synthesized, corresponding to a common basic region of IGFBP-3 (P3), IGFBP-5 and IGFBP-6 (P6) which contained a heparin binding sequence. P3 and P6 inhibited IGFBP-3 and -5 binding to endothelial cell monolayers and the peptides bound directly to EC extracellular matrix. This suggested that the C-terminal basic segment of IGFBP-3/-5 is important for the association of the binding protein with the EC monolayer. |
| Databáze: | OpenAIRE |
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