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Five FGF receptors with distinct expression patterns

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Angiogenesis

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

  • Publisher Name: Birkhäuser, Basel

  • Print ISBN: 978-3-0348-7003-0

  • Online ISBN: 978-3-0348-7001-6

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