title: FGF3 from Xenopus laevis.
abstract: Fibroblast growth factor 3 (FGF3) was first identified as the product of a cellular oncogene activated by mouse mammary tumour virus but its normal role appears to be in the developing embryo. To gain further insights into its function, we have isolated sequences encoding the FGF3 homologue in Xenopus laevis, XFGF3. COS-1 cells transfected with XFGF3 cDNA express a 31 kDa product, p31, generated by signal peptide cleavage and Asn-linked glycosylation at the single consensus site. This product is secreted and becomes associated with the cell surface and extracellular matrix. Proteolytic cleavage of p31 in the extracellular compartment results in an amino-terminally truncated product, p27, that is also glycosylated. Both p31 and p27 bind quantitatively to heparin-Sepharose and can be displaced from the cell surface and extracellular matrix by soluble heparin. Conditioned medium containing these two proteins is capable of inducing transient morphological transformation of NIH3T3 cells and of stimulating DNA synthesis in quiescent C57MG and BALB/MK cells which express different isoforms of FGF receptors 1 and 2. Since XFGF3 behaves very differently from its mouse counterpart, we constructed chimeras in which amino-terminal sequences from XFGF3 were fused with carboxy-terminal sequences from mouse FGF3. Increasing the contribution from mouse FGF3 led to a more restricted host range for the chimeric ligand.
authors.affiliation: Imperial Cancer Research Fund, London, UK.
authors.forename: P
authors.initials: P
authors.lastname: Kiefer
authors.forename: M
authors.initials: M
authors.lastname: Mathieu
authors.forename: M J
authors.initials: MJ
authors.lastname: Close
authors.forename: G
authors.initials: G
authors.lastname: Peters
authors.forename: C
authors.initials: C
authors.lastname: Dickson
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002455:Cell Division / Q000187:drug effects; D002478:Cells, Cultured; D002847:Chromatography, Agarose; D005109:Extracellular Matrix / Q000737:chemistry; D051518:Fibroblast Growth Factor 3; D005346:Fibroblast Growth Factors / Q000096:biosynthesis / Q000235:genetics* / Q000494:pharmacology; D006031:Glycosylation; D051379:Mice; D008969:Molecular Sequence Data; D005810:Multigene Family; D010442:Peptide Chain Initiation, Translational; D011499:Protein Processing, Post-Translational; D011518:Proto-Oncogene Proteins / Q000096:biosynthesis / Q000235:genetics* / Q000494:pharmacology; D016364:Reading Frames / Q000235:genetics; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis; D011994:Recombinant Proteins / Q000096:biosynthesis; D017421:Sequence Analysis; D017386:Sequence Homology, Amino Acid; D013329:Structure-Activity Relationship; D014162:Transfection; D029867:Xenopus Proteins; D014982:Xenopus laevis / Q000235:genetics*
chemical_list: C489198:FGF3 protein, Xenopus; C489197:Fgf3 protein, mouse; D051518:Fibroblast Growth Factor 3; D011518:Proto-Oncogene Proteins; D011993:Recombinant Fusion Proteins; D011994:Recombinant Proteins; D029867:Xenopus Proteins; D005346:Fibroblast Growth Factors