Heparin and Heparan Sulfate Increase the Radius of Diffusion and Action of Basic Fibroblast Growth Factor

• Published in: The Journal of cell biology Vol. 111; no. 4; pp. 1651 - 1659
• Main Authors: Flaumenhaft, Robert, Moscatelli, David, Rifkin, Daniel B.
• Format: Journal Article
• Language: English
• Published: United States Rockefeller University Press 01-10-1990; The Rockefeller University Press
• Subjects: Animals; Cattle; Cell lines; Cells; Cells, Cultured; Cricetinae; Cultured cells; Cytochrome c Group - metabolism; Cytochromes; Diffusion; Endothelial cells; Fibrin; Fibroblast Growth Factor 2 - metabolism; Fibroblast Growth Factor 2 - physiology; Fibroblast growth factors; Gels; Heparin; Heparin - metabolism; Heparin - physiology; Heparitin Sulfate - metabolism; Heparitin Sulfate - physiology; Immunodiffusion; Iodine Radioisotopes; Mast cells; Protein Binding; Sepharose; Sulfates; Swine
• ISSN: 0021-9525; 1540-8140
• DOI: 10.1083/jcb.111.4.1651

The radius of diffusion of basic FGF (bFGF) in the presence and in the absence of the glycosaminoglycans heparin and heparan sulfate was measured. Iodinated 125 I- bFGF diffuses further in agarose, fibrin, and on a monolayer of bovine aortic endothelial (BAE) cells in the presence of heparin than in its absence. Heparan sulfates affected the diffusion of 125 I- bFGF in a manner similar to, though less pronounced than, heparin. When applied at the center of a monolayer of BAE cells, bFGF plus heparin stimulated morphological changes at a 10-fold greater radius than bFGF alone. These results suggest that bFGF-heparin and/or heparan sulfate complexes may be more effective than bFGF alone in stimulating cells located away from the bFGF source because the bFGF-glycosaminoglycan complex partitions into the soluble phase rather than binding to insoluble glycosaminoglycans in the extracellular matrix. Thus, the complex of bFGF and glycosaminoglycan may represent one of the active forms of bFGF in vivo.