Glycosaminoglycan affinity of the complete fibroblast growth factor family
Glycosaminoglycan affinity of the complete fibroblast growth factor family
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DOI:
10.1016/j.bbagen.2008.09.001
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发表时间:
2009-01-01
影响因子:
3
通讯作者:
Imamura, Toru
中科院分区:
文献类型:
--
作者:
Asada, Masahiro;Shinomiya, Michiyo;Imamura, Toru
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. (C) 2008 Elsevier B.V. All rights reserved.