FGFb is a member of the fibroblast growth factor (FGF) family which includes 23 members. FGFb is expressed in almost all tissues and play important roles in a variety of normal and pathological processes, including development, wound healing and neoplastic transformation. FGFb is mitogenic for many cell types, both epithelial and mesenchymal. FGFb shows potent angiogenic activity and has been implicated in tumor angiogenesis. In prostate, bladder, and renal cancers, FGFb regulates the induction of metalloproteinases (MMP) that degrade extracellular matrix proteins, thus facilitating tumor metastasis . FGFb binds to a family of four distinct, high affinity tyrosine kinase receptors, designated FGFR-1 to -4. In addition, FGFb binds to the ECM, and heparan sulfate (HS) is an essential and dynamic regulator of fibroblast growth factor (FGF) signaling. Two fundamentally different crystallographic models have been proposed to explain, at the molecular level, how HS/heparin enables FGF and FGF receptor (FGFR) to assemble into a functional dimer on the cell surface, although there is controversy regarding the exact manner by which this occurs.
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Description:
FGFb is a member of the fibroblast growth factor (FGF) family which includes 23 members. FGFb is expressed in almost all tissues and play important roles in a variety of normal and pathological processes, including development, wound healing and neoplastic transformation. FGFb is mitogenic for many cell types, both epithelial and mesenchymal. FGFb shows potent angiogenic activity and has been implicated in tumor angiogenesis. In prostate, bladder, and renal cancers, FGFb regulates the induction of metalloproteinases (MMP) that degrade extracellular matrix proteins, thus facilitating tumor metastasis . FGFb binds to a family of four distinct, high affinity tyrosine kinase receptors, designated FGFR-1 to -4. In addition, FGFb binds to the ECM, and heparan sulfate (HS) is an essential and dynamic regulator of fibroblast growth factor (FGF) signaling. Two fundamentally different crystallographic models have been proposed to explain, at the molecular level, how HS/heparin enables FGF and FGF receptor (FGFR) to assemble into a functional dimer on the cell surface, although there is controversy regarding the exact manner by which this occurs.
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