| First Author | Asada M | Year | 2009 |
| Journal | Biochim Biophys Acta | Volume | 1790 |
| Issue | 1 | Pages | 40-8 |
| PubMed ID | 18835578 | Mgi Jnum | J:144422 |
| Mgi Id | MGI:3830914 | Doi | 10.1016/j.bbagen.2008.09.001 |
| Citation | Asada M, et al. (2009) Glycosaminoglycan affinity of the complete fibroblast growth factor family. Biochim Biophys Acta 1790(1):40-8 |
| abstractText | BACKGROUND: Many fibroblast growth factor family proteins (FGFs) bind to the heparan sulfate/heparin (HP) subtypes of sulfated glycosaminoglycans (GAGs), and a few have recently been reported to also interact with chondroitin sulfate (CS), another sulfated GAG subtype. METHODS: To gain additional insight into this interaction, we prepared all currently known FGFs (i.e., FGF1-FGF23) and assessed their affinity for HP, CS-B, CS-D and CS-E. In addition, midkine, hepatocyte growth factor and pleiotrophin were studied as other known HP-binding proteins. RESULTS: We found that members of the FGF19 subfamily (i.e., FGF15, 19, 21 and 23) had little or no affinity for HP; all of the other secretable growth factors tested had strong affinities for HP, as was indicated by the finding that their elution from HP-Sepharose columns required 1.0-1.5 M NaCl. We also found that FGF3, 6, 8 and 22 had strong affinities for CS-E, while FGF5 had a moderate affinity for CS-D. The interactions between FGFs and GAGs thus appear to be more diverse than previously understood. GENERAL SIGNIFICANCE: This is noteworthy, as the differential interactions of these growth factors with GAGs may be key determinants of their specific biological activities. |
