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Biochim Biophys Acta. 2009 Jan 1;1790(1):40-8. doi: 10.1016/j.bbagen.2008.09.001. Epub 2008 Sep 16.

Glycosaminoglycan affinity of the complete fibroblast growth factor family.

Author information

1
Signaling Molecules Research Laboratory, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba, Ibaraki 305-8566, Japan.

Abstract

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.

PMID:
18835578
DOI:
10.1016/j.bbagen.2008.09.001
[Indexed for MEDLINE]

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