Processing, Secretion, and Biological Properties of a Novel Growth Factor of the Fibroblast Growth Factor Family with Oncogenic Potential

LITERATURE CITED

• Friedman, D., Gospodarowicz, and J. C. Flddes. 1986. Human basic fibroblast growth factor: nucleotide sequence and genomic organization. EMBO J. 5:2523–2528.
   PubMedGoogle Scholar
• Abrabazo, J. A., A. Mercia, I. L. WbaBg, A. Tunsolo, I. F'riedman, X. A. Afjerrild, D. Gaspodarowicz, and T. C. 'lddes. 1986. Nucleotide sequence of a bovine clone encoding the angiogenic protein, basic fibroblast growth factor. Science 233:545–548.
   PubMedGoogle Scholar
• Delll-Bovi, P., and C. Baslllco. 1987. Isolation of a rearranged human transforming gene following transfection of Kapnsi sar- coma DNA. Proc. Natl. Acad. Sci. USA 84:5660–5664.
   PubMedGoogle Scholar
• Delli-Bovi, P., A. M. Curatola, F. G. Kern, A. Greco, M. Ittmann, and C. Baslllco. 1987. An oncogene isolated by trans- fection of Kaposi's sarcoma DNA encodes a growth factor that is a member of the FGF family. Cell 50:729–737.
   PubMed Web of Science ®Google Scholar
• Dickson, C., and P. Gordon. 1987. Potential oncogene product related to growth factors. Nature (London) 326:833.
   PubMed Web of Science ®Google Scholar
• Irrnec, A. J., D. G. Bole, and R. J. Kaufmn. 1987. The relationship of N-linked glycosylation and heavy chain-binding protein association with the secretion of glycoproteins. J. Cell Biol. 105:2665–2674.
   PubMedGoogle Scholar
• Folkman, J., C. C. Heudenschild, and B. R. Zetter. 1979. Long-term culture of capillary endothelial cells. Proc. Natl. Acad. Sci. USA 76:5217–5221.
   PubMed Web of Science ®Google Scholar
• Folkmen, J., and M. Klagsbrun. 1987. Angiogenic factors. Science 235:442–447.
   PubMedGoogle Scholar
• Gluzman, Y. 1981. SV40-transformed simian cells support the replication of early SV40 mutants. Cell 23:175–182.
   PubMed Web of Science ®Google Scholar
• Gmpodarowicz, D., and J. Cheng. 1986. Heparin protects basic and acidic FGF from inactivation. J. Cell. Physiol. 128:47W84.
   Google Scholar
• Goepodaroulcz, D., G. Neufeld, and L. Schweigerer. 1987. Fibroblast growth factor: structural and biological properties. J. Cell. Physiol. Suppl. 5:15–26.
   Google Scholar
• Gross, I. L., D. Moseatelll, E. A. JeKe, and D. B. Ritbin. 1982. Plasminogen activator and collagenase production by cultured capillary endothelial cells. J. Cell Biol. 95:974–981.
   PubMed Web of Science ®Google Scholar
• Hewick, R. M., M. W. Hunkaplller, L. E. Hood, and W. J. Dreyer. 1981. A gas-liquid solid phase peptide and protein sequenator. J. Biol. Chem. 256:7990–7997.
   PubMed Web of Science ®Google Scholar
• Kaplan, P. L., M. Anderson, and B. Ozanne. 1982. Transforming growth factor(s) production enables cells to grow in the absence of serum: an autocrine system. Proc. Natl. Acad. Sci. USA 79:489.
   Google Scholar
• Kimelmen, D., and M. Kirschner. 1987. Synergistic induction of mesoderm by FGF and TGF-β and the identification of an mRNA coding for FGF in the early Xenopus embryo. Cell 51:86W77.
   Google Scholar
• Luthman, H., and G. Magnusson. 1983. High e&ciency polyoma DNA transfection of chloroquine treated cells. Nucleic Acids Res. 11:1295–1308.
   PubMed Web of Science ®Google Scholar
• Mzxsre, R., G. Casey, S. Brookes, M. Dixoa, G. Peters, and C. Dickson. 1986. Sequence, topogmphy and protein coding poten- tial of mouse int-2: a putative oncogene activated by mouse mammary tumour virus. EMBO J. 5:919–924.
   PubMedGoogle Scholar
• Mosmtelli, D., M. Presta, and D. B. Rifkin. 1986. Purihcation of a factor from human placenta that stimulates capillary endothe- lial cell protease production, DNA synthesis, and migration. Proc. Natl. Acad. Sci. USA 83:2091–2095.
   PubMedGoogle Scholar
• Okayame, H., and P. Berg. 1982. High-e&ciency cloning of full-length cDNA. Mol. Cell. Biol. 2:161–170.
   PubMedGoogle Scholar
• Presta, M., D. Mosmtelli, J. Joseph-Silverstein, and D. B. Rlfkin. 1986. Purification from a human hepatoma cell line of a basic fibroblast growth factor-like molecule that stimulates capillary endothelial cell plasminogen activator production, DNA synthe- sis, and migration. Mol. Cell. Biol. 6:4060–4066.
   PubMed Web of Science ®Google Scholar
• Sabatini, D. D., C. Areibicb, T. Morimoto, and M. Adesnik. 1982. Mechanisms for the incorporation of proteins in mem- branes and organelles. J. Cen Biol. 92:1–22.
   PubMed Web of Science ®Google Scholar
• Scbreiber, A. B., J. Kenney, W. J. Kowalskl, R. Friesel, T. Mehlman, and T. Mcieg. 1985. Interaction of endothelial cell growth factor with heparin: characterization by receptor and antibody recognition. Proc. Natl. Acad. Sci. USA 82:6138–6142.
   PubMedGoogle Scholar
• Sporn, M. B., and A. B. Roberts. 1985. Autocrine growth factors and cancer. Nature (London) 313:74S–747.
   Google Scholar
• Tatra, M., T. Yoshida, K. Mlyagawc, H. Sakemoto, M. Terada, and T. Sugimura. 1987. cDNA sequence of human transforming gene hst and identification of the coding sequence required for transforming activity. Proc. Natl. Acad. Sci. USA 84:2980–2984.
   PubMedGoogle Scholar
• von HeJjne, G. 1984. How signai sequences maintain cleavage specificity. J. Mol. Biol. 173:243–251.
   PubMedGoogle Scholar
• von HeiJne, G. 1986. A new method for predicting signal sequence cleavage sites. Nucleic Acids Res. 14:4683–4690.
   PubMed Web of Science ®Google Scholar
• Weehs, D. L., and D. A. Melton. 1987. A maternal mRNA localized to the vegetal hemisphere in Xenopus eggs codes for a growth factor related to TGF-β. Cell 51:861–867.
   PubMedGoogle Scholar
• Wong, G. G., J. S. Witek, P. A. Temple, K. M. Wilkens, A. C. Leery, D. P. Lexenberg, S. S. Jones, E. L. Brown, R. M. Kay, E. C. Orr, C. S. Shoemaker, D. W. Golde, R. J. Kaufman, R. M. Hewick, E. A. Wang, and S. C. Clark. 1985. Human GM-CSF: molecular cloning of the complementary DNA and purification of the natural and recombinant proteins. Science 228:81M15.
   Google Scholar
• Yoshida, T., K. Mlyegawa, H. Odeglrl, H. Sekemoto, P. F. R. Little, M. Terada, and T. Suglmura. 1987. Genomic sequence of hst, a transforming gene encoding a protein homologous to fibroblast growth factors and the int-2 encoded protein. Proc. Natl. Acad. Sci. USA 84:7305–7309.
   PubMed Web of Science ®Google Scholar
• Zben, X., and M. Goldfarb. 1986. Growth factor requirements of oncogene-transformed NIH 3T3 and BALB/c 3T3 cells cul- tured in defined media. Mol. Ce8. Biol. 6:3541–3544.
   PubMedGoogle Scholar