Basic fibroblast growth factor is released from endothelial extracellular matrix in a biologically active form

✍ Scribed by M. Presta; J. A. M. Maier; M. Rusnati; G. Ragnotti

• Publisher: John Wiley and Sons
• Year: 1989
• Tongue: English
• Weight: 730 KB
• Volume: 140
• Category: Article
• ISSN: 0021-9541
• DOI: 10.1002/jcp.1041400109

✦ Synopsis

Basic fibroblast growth factor (bFGF) binds to heparin-like molecules present in the extracellular matrix (ECM) of transformed fetal bovine aortic endothelial G M 7373 cells. Binding of bFGF to ECM can be competed by heparin or heparan sulfate, and ECM-bound bFGF can be released by treating the cells with heparinase or heparatinase. After binding to ECM, bFGF is slowly released into the medium in a biologically active form, as shown by its capacity to induce an increase of cell-associated plasminogen activator activity and cell proliferation. The increase is prevented upon removal of ECM-bound bFGF by a neutral 2 M NaCl wash. Soluble heparin and heparan sulfate reduce the amount of ECMbound bFGF released into the medium, possibly competing with ECM polysaccharides for heparinase-like enzymes produced by endothelial cells, suggesting that these enzymes are involved in the mobilization of ECM-bound bFGF.