Role of FGFs in skeletal muscle and limb development

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Abstract
Fibroblast growth factors (FGFs) are a family of nine proteins that bind to three distinct types of cell surface molecules: (i) FGF receptor tyrosine kinases (FGFR‐1 through FGFR‐4); (ii) a cysteine‐rich FGF receptor (CFR); and (iii) heparan sulfate proteoglycans (HSPGs). Signaling by FGFs requires participation of at least two of these receptors: the FGFRs and HSPGs form a signaling complex. The length and sulfation pattern of the heparan sulfate chain determines both the activity of the signaling complex and, in part, the ligand specificity for FGFR‐1. Thus, the heparan sulfate proteoglycans are likely to play an essential role in signaling. We have recently identified a role for FGF in limb bud development in vivo. In the chick limb bud, ectopic expression of the 18 kDa form of FGF‐2 or FGF‐2 fused to an artificial signal peptide at its amino terminus causes skeletal duplications. These data, and the observations that FGF‐2 is localized to the subjacent mesoderm and the apical ectodermal ridge in the early developing limb, suggest that FGF‐2 plays an important role in limb outgrowth. We propose that FGF‐2 is an apical ectodermal ridgederived factor that participates in limb outgrowth and patterning.

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