Abstract
The fibroblast growth factors (FGF) constitute a polypeptide family whose members can interact with cell surface receptors to modulate gene expression for cell proliferation and differentiation. Seven structurally related heparin binding FGFs are known. The first discovered members of the family were aFGF and bFGF, also called HBGF-1/ ECGF (heparin binding growth factor/endothelial cell growth factor) and HBGF-2, respectively. The tertiary fold of bFGF is similar to that of interleukin-1 [1–3]. Amino acid sequence analysis demonstrates 55% identity between aFGF and bFGF. Sequence homology and similar biological responses suggest that they are derived from a common ancestral gene. Both aFGF and bFGF also lack an N-terminal signal peptide sequence (Fig. 1) and thus their mechanism of secretion is unknown.
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© 1992 Birkhäuser Verlag Basel/Switzerland
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Korhonen, J. et al. (1992). Five FGF receptors with distinct expression patterns. In: Steiner, R., Weisz, P.B., Langer, R. (eds) Angiogenesis. Experientia Supplementum, vol 61. Birkhäuser, Basel. https://doi.org/10.1007/978-3-0348-7001-6_16
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DOI: https://doi.org/10.1007/978-3-0348-7001-6_16
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