Heparin fibroblast growth factor

Heparin was immobilized on the WPG-P A and the sorbent was used for isolation of the fibroblast growth factor from bovine hypophysis. Mitogenic activity of the factor purified on the heparin-WPG-PA and Heparin-Sepharose, as estimated with mice fibroblasts of line N1H-3T3, was virtually the same [130]. 

Burgess WH, Maciag T (1989) The heparin-binding (fibroblast) growth-factor family of proteins. Annu Rev Biochem 58 575-606... 

In other studies, mast cells have been shown to be abundant in the marrow of osteoporotic patients, and heparin, which is contained within the secretory granules of connective tissue (peritoneal)-type mast cells, has been shown to enhance bone resorption and to inhibit bone-cell replication and collagen synthesis in vitro [130]. Moreover, heparin is known to bind growth factors such as fibroblast growth factor and may therefore be important in limiting their availability [134], Taken together, these various studies suggest a possible involvement of mast cells in the homeostasis of bone, but much more work is needed before any definitive conclusions can be drawn. 

One key NMR-based study has focused on the evaluation of the dynamic properties of heparin-like hexasaccharides.20 The analysis of Tj, T2 and NOE 13C-NMR data of biologically active synthetic compounds has shown that the sulphation pattern strongly influences the internal dynamics, and supports the importance of the GAGs flexibility on the selectivity of the interaction with fibroblast growth factors. 

Fromm, J.R., R.E. Hileman, E.E. Caldwell, J.M. Weiler, and R.J. Linhardt. 1995. Differences in the interaction of heparin with arginine and lysine and the importance of these basic amino acids in the binding of heparin to acidic fibroblast growth factor. Arch Biochem Biophys 323 279-287. 

S Faham, RJ Linhardt, DC Rees. Diversity does make a difference fibroblast growth factor—heparin interactions. Curr Opin Struct Biol 8 578—586, 1998. 

Faham S, Hileman RE, Fromm JR, Linhardt RJ, Rees DC, Heparin structure and interactions with basic fibroblast growth factor. Science I 996 271 (5252) I I I 6-1 120. 

The data for specificity are equally surprising. As shown in Table 20.1, an aptamer aimed at basic fibroblast growth factor (bFGF) does not bind tightly to other members of the FGF family or to other proteins known to interact with an acidic substance, heparin (these data were reported in [5]). Similar data exist for aptamers aimed at several reverse transcriptases, serine proteases, P- and L-selectin, and cytokines such as VEGF and PDGF. Aptamers in vitro show extreme specificity for their intended targets. 

S. Faham, R. E. Hileman, J. R. Fromm, R. J. Linhardt, and D. C. Rees. Heparin structure and mteractions with basic fibroblast growth factor. Science, 271 ( 5252), 1116-1120, 1996. 

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