The C-terminal Region of Fibroblast Growth Factor-1 is Crucial for its Biological Activity and High Level Protein Expression in Mammalian Cells

References

• Baird A., Schubert D., Ling N., Guillemin R. Receptor-and heparin-binding domains of basic fibroblast growth factor. Proc. Nail. Acad. Sci. USA 1988; 85: 2324–2328
   PubMed Web of Science ®Google Scholar
• Basilico C., Moscatelli D. The FGF family of growth factors and oncogenes. Adv. Cancer. Res. 1992; 59: 115–165
   PubMed Web of Science ®Google Scholar
• Blaber M., DiSalvo J., Thomas K. A. X-ray crystal structure of human acidic fibroblast growth factor. Biochemistry 1996; 35: 2086–2094
   PubMed Web of Science ®Google Scholar
• Burgess W. H., Maciag T. The heparin-binding (fibroblast) growth factor family of proteins. Annu. Rev. Biochem. 1989; 58: 575–606
   PubMed Web of Science ®Google Scholar
• Cardin A. D., Weintraub H. J. Molecular modeling of protein-glycosaminoglycan interactions. Arteriosclerosis 1989; 9: 21–32
   PubMedGoogle Scholar
• Ciechanover A., Schwartz A. L. The ubiquitinmediated proteolytic pathway: mechanisms of recognition of the proteolytic substrate and involvement in the degradation of native cellular proteins. FASEB J. 1994; 8: 182–191
   PubMed Web of Science ®Google Scholar
• Cohn M. J., Izpisua-Belmonte J. C., Abud H., Heath J. K., Tickle C. Fibroblast growth factors induce additional limb development from the flank of chick embryos. Cell 1995; 80: 739–746
   PubMed Web of Science ®Google Scholar
• Danilenko D. M., Ring B. D., Yanagihara D., Benson W., Wiemann B., Starnes C. O., Pierce G. F. Keratinocyte growth factor is an important endogenous mediator of hair follicle growth, development, and differentiation. Normalization of the nu/nu follicular differentiation defect and amelioration of chemotherapy-induced alopecia. Am. J. Pathol. 1995; 147: 145–154
   PubMed Web of Science ®Google Scholar
• Dionne C. A., Crumley G., Bellot F., Kaplow J. M., Searfoss G., Ruta M., Burgess W. H., Jaye M., Schlessinger J. Cloning and expression of two distinct high-affinity receptors cross-reacting with acidic and basic fibroblast growth factors. EMBO J. 1990; 9: 2685–2692
   PubMed Web of Science ®Google Scholar
• Ferran D. S., Sobel M., Harris R. B. Design and synthesis of a helix heparin-binding peptide. Biochemistry 1992; 31: 5010–5016
   Google Scholar
• Forough R., Engleka K., Thompson J. A., Jackson A., Imamura T., Maciag T. Differential expression in Escherichia coli of the alpha and beta forms of heparin-binding acidic fibroblast growth factor-1: potential role of RNA secondary structure. Biochim. Biophys. Acta. 1991; 1090: 293–298
   PubMed Web of Science ®Google Scholar
• Harper J. W., Lobb R. R. Reductive methylation of lysine residues in acidic fibroblast growth factor: effect on mitogenic activity and heparin affinity. Biochemistry. 1988; 27: 671–678
   PubMedGoogle Scholar
• Hershko A. The ubiquitin pathway for protein degradation. Trends. Biochem. Sci. 1991; 16: 265–268
   PubMedGoogle Scholar
• Imamura T., Engleka K., Zhan X., Tokita Y., Forough R., Roeder D., Jackson A., Maier J. A., Hla T., Maciag T. Recovery of mitogenic activity of a growth factor mutant with a nuclear translocation sequence. Science 1990; 249: 1567–1570
   PubMed Web of Science ®Google Scholar
• Imamura T., Oka S., Tanahashi T., Okita Y. Cell cycle-dependent nuclear localization of exogenously added fibroblast growth factor-1 in BALB/c3T3 and human vascular endothelial cells. Exp. Cell. Res. 1994; 215: 363–372
   PubMedGoogle Scholar
• Imamura T., Tokita Y., Mitsui Y. Identification of a heparin-binding growth factor-1 nuclear translocation sequence by deletion mutation analysis. J. Biol. Chem. 1992; 267: 5676–5679
   PubMed Web of Science ®Google Scholar
• Jackson A., Friedman S., Zhan X., Engleka K. A., Forough R., Maciag T. Heat shock induces the release of fibroblast growth factor 1 from NIH3T3 cells. Proc. Natl. Acad. Sci. USA 1992; 89: 10691–10695
   PubMed Web of Science ®Google Scholar
• Kiefer P., Acland P., Pappin D., Peters G., Dickson C. Competition between nuclear localization and secretory signals determines the subcellular fate of a single CUG-initiated form of FGF3. EMBO. J. 1994; 13: 4126–4136
   PubMed Web of Science ®Google Scholar
• Miyamoto M., Naruo K., Seko C., Matsumoto S., Kondo T., Kurokawa T. Molecular cloning of a novel cytokine cDNA encoding the ninth member of the fibroblast growth factor family, which has a unique secretion property. Mol. Cell Biol. 1993; 13: 4251–4259
   PubMed Web of Science ®Google Scholar
• Ochiya T., Sakamoto H., Tsukamoto M., Sugimura T., Terada M. Hst-1 (FGF-4) antisense oligonucleotides block murine limb development. J. Cell Biol. 1995; 130: 997–1003
   Google Scholar
• Ozawa K., Uruno T., Miyakawa K., Seo M., Imamura T. Expression of the fibroblast growth factor family and their receptor family genes during mouse brain development. Brain. Res. Mol. Brain Res. 1996; 41: 279–288
   PubMedGoogle Scholar
• Quarto N., Finger F. P., Rifkin D. B. The NH2-lerminal extension of high molecular weight bFGF is a nuclear targeting signal. J. Cell Physiol. 1991; 147: 311–318
   PubMed Web of Science ®Google Scholar
• Rechsteiner M., Hoffman L., Dubiel W. The multicatalytic and 26 S proteases. J. Biol. Chem. 1993; 268: 6065–6068
   PubMed Web of Science ®Google Scholar
• Rock K. L., Gramm C., Rothstein L., Clark K., Stein R., Dick L., Hwang D., Goldberg A. L. Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell 1994; 78: 761–771
   PubMed Web of Science ®Google Scholar
• Ruta M., Burgess W., Givol D., Epstein J., Neiger N., Kaplow J., Crumley G., Dionne C., Jaye M., Schlessinger J. Receptor for acidic fibroblast growth factor is related to the tyrosine kinase encoded by the fms-like gene (FLG). Proc. Natl. Acad. Sci. USA 1989; 86: 8722–8726
   PubMed Web of Science ®Google Scholar
• Seno M., Sasada R., Kurokawa T., Igarashi K. Carboxyl-terminal structure of basic fibroblast growth factor significantly contributes to its affinity for heparin. Eur. J. Biochem. 1990; 188: 239–245
   PubMedGoogle Scholar
• Spivak-Kroizman T., Lemmon M. A., Dikic I., Lad bury J. E., Pinchasi D., Huang J., Jaye M., Crumley G., Schlessinger J., Tax I. Heparin-induced oligomerization of FGF molecules is responsible for FGF receptor dimerization, activation, and cell proliferation. Cell 1994; 79: 1015–1024
   PubMed Web of Science ®Google Scholar
• Tanaka A., Miyamoto K., Minamino N., Takeda M., Sato B., Matsuo H., Matsumoto K. Cloning and characterization of an androgen-induced growth factor essential for the androgen-dependent growth of mouse mammary carcinoma cells. Proc. Natl. Acad. Sci. USA 1992; 89: 8928–8932
   PubMed Web of Science ®Google Scholar
• Tanaka K., Tamura T., Yoshimura T., Ichihara A. Proteasomes: protein and gene structures. New Biol. 1992; 4: 173–187
   PubMedGoogle Scholar
• Traenckner E. B., Wilk S., Baeuerle P. A. A proteasome inhibitor prevents activation of NF-kappa B and stabilizes a newly phosphorylated form of I kappa B-alpha that is still bound to NP-kappa B. EMBO. J. 1994; 13: 5433–5441
   PubMed Web of Science ®Google Scholar
• Zhu X., Komiya H., Chirino A., Faham S., Fox G. M., Arakawa T., Hsu B. T., Rees D. C. Three-dimensional structures of acidic and basic fibroblast growth factors. Science 1991; 251: 90–93
   PubMed Web of Science ®Google Scholar