The Basic Fibroblast Growth Factor Isoforms: Endogenous and Exogenous Behavior View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

1993

AUTHORS

Natalina Quarto , Gérard Bouche , Béatrix Bugler , Catherine Chailleux , Hervé Prats , Anne-Catherine Prats , Ana-Maria Roman , Isabelle Truchet , François Amalric

ABSTRACT

The fibroblast growth factors (FGFs) constitute a family of at least seven structurally related polypeptides sharing 35-55% sequence homology. The acidic FGF (FGF-1) and basic FGF (FGF-2) are the prototypes. Other members of this family include int-2 (FGF-3), K-fgf (FGF4), FGF-5, FGF-6 and KGF (FGF-7). They are potent modulators of cell function proliferation, motility, differentiation and survival. Furthermore, they play an important role in normal physiological processes such as embryonic development, angiogenesis, nervous cell system differentiation and wound-repair (Rifkin and Moscatelli, 1989; Burgess and Maciag, 1989). The FGFs exert their biological activity through a complex interaction with high and low affinity receptors. To date, four human genes have been identified each encoding a distinct high affinity receptor (Kd of l0-11). Each of these genes encodes multiple proteins derived from alternative mRNA splicing (Houssaint et al., 1990; Johnson et al., 1990; Partanen et al., 1991). Despite their structural similarities, these high affinity receptors may differ in their ability to bind various members of FGF family. The heparin sulfate proteoglycans (HSPGs) are the low affinity receptors (Kd of 10-9) which are essential for bFGF activity and high affinity binding (Moscatelli, 1987; Yayon et al., 1991; Rapraeger et al., 1991). Recently, syndecan, an integral membrane HSPG, has been identified as a low affinity binding site for bFGF (Kiefer et al., 1990). Basic FGF has several unique properties that differentiate it from other growth factors. One of these is the lack of a signal peptide normally required for vectorial transfer into the endoplasmic reticulum and for secretion (Abraham et al., 1986a). A second property of bFGF, shared with FGF-3, is the use of CUG codons for the initiation of translation of High Molecular Weight (HMW) isoforms, in addition to the canonic AUG codon used to generate the Low Molecular Weight bFGF (LMWbFGF) form (Florkiewicz and Sommer, 1989; Prats et al., 1989). In this paper, we will review some developments in the biology of bFGF(FGF-2), which have recently been achieved by ourselves and other authors. More... »

PAGES

147-158

References to SciGraph publications

Book

TITLE

Growth Factors, Peptides and Receptors

ISBN

978-0-306-44484-5
978-1-4615-2846-3

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-1-4615-2846-3_15

DOI

http://dx.doi.org/10.1007/978-1-4615-2846-3_15

DIMENSIONS

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40 schema:description The fibroblast growth factors (FGFs) constitute a family of at least seven structurally related polypeptides sharing 35-55% sequence homology. The acidic FGF (FGF-1) and basic FGF (FGF-2) are the prototypes. Other members of this family include int-2 (FGF-3), K-fgf (FGF4), FGF-5, FGF-6 and KGF (FGF-7). They are potent modulators of cell function proliferation, motility, differentiation and survival. Furthermore, they play an important role in normal physiological processes such as embryonic development, angiogenesis, nervous cell system differentiation and wound-repair (Rifkin and Moscatelli, 1989; Burgess and Maciag, 1989). The FGFs exert their biological activity through a complex interaction with high and low affinity receptors. To date, four human genes have been identified each encoding a distinct high affinity receptor (Kd of l0-11). Each of these genes encodes multiple proteins derived from alternative mRNA splicing (Houssaint et al., 1990; Johnson et al., 1990; Partanen et al., 1991). Despite their structural similarities, these high affinity receptors may differ in their ability to bind various members of FGF family. The heparin sulfate proteoglycans (HSPGs) are the low affinity receptors (Kd of 10-9) which are essential for bFGF activity and high affinity binding (Moscatelli, 1987; Yayon et al., 1991; Rapraeger et al., 1991). Recently, syndecan, an integral membrane HSPG, has been identified as a low affinity binding site for bFGF (Kiefer et al., 1990). Basic FGF has several unique properties that differentiate it from other growth factors. One of these is the lack of a signal peptide normally required for vectorial transfer into the endoplasmic reticulum and for secretion (Abraham et al., 1986a). A second property of bFGF, shared with FGF-3, is the use of CUG codons for the initiation of translation of High Molecular Weight (HMW) isoforms, in addition to the canonic AUG codon used to generate the Low Molecular Weight bFGF (LMWbFGF) form (Florkiewicz and Sommer, 1989; Prats et al., 1989). In this paper, we will review some developments in the biology of bFGF(FGF-2), which have recently been achieved by ourselves and other authors.
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