Heparin-protein interactions fibroblast growth factors

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. 

Sommer A and Rifkin DB. Interaction of Heparin with Human Basic Fibroblast Growth Factor Protection of the Angiogenic Protein from Proteolytic Degradation by a Glycosaminoglycan./Ce/ZPAy io/1989 138(1) 215-220. 

Both CS and DS have been shown to exhibit multiple protein and cellular interactions, including but not limited to fibroblast growth factors, hepatocyte growth factor, tenascin-X, and heparin cofactor With... 

Sommer, A. and Rifldn, D.B. (1989) Interaction of heparin with human basic fibroblast growth factor protection of the angiogenic protein from proteolytic degradation by a gly-cosaminoglycan. J. Cell Physiol. 138 215-220. 

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