Characterization of fibroblast growth factor-2 binding to ribosomes

Growth Factors

Volumn 13, Issue 3-4, 1996, Pages 219-228

  Klein, Sharon ^b,c   Morimoto, Takashi ^b   Rifkin, Daniel B ^a  

^a New York University Medical Center   (United States)

^b NEW YORK UNIVERSITY MEDICAL CENTER   (United States)

^c NEW YORK UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

FGF 2; Polysomes; Puromycin

Indexed keywords

FIBROBLAST GROWTH FACTOR 2; NEUROTROPIC AGENT; PUROMYCIN; RIBONUCLEASE; RIBOSOME PROTEIN; RIBOSOME RNA;

ANIMAL CELL; ARTICLE; BINDING AFFINITY; CELL MEMBRANE; CELL NUCLEUS; CONTROLLED STUDY; CYTOSOL; DNA TRANSFECTION; DRUG BINDING; DRUG BINDING SITE; DRUG SPECIFICITY; MITOCHONDRION; MOUSE; NONHUMAN; PRIORITY JOURNAL; RIBOSOME; STOICHIOMETRY;

ANIMALIA;

EID: 0029957451     PISSN: 08977194     EISSN: None     Source Type: Journal    
DOI: 10.3109/08977199609003223     Document Type: Article

References (54)

1. Abraham, J. A., Mergia, A., Whang, J. L., Tumolo, A., Friedman, J., Hjerrild, K. A., Gospodarowicz, D. and Fiddes, J. C. (1986) Nucleotide sequence of a bovine clone encoding the angiogenic protein, basic fibroblast growth factor. Science 233, 545-548.
2. Aviezer, D., Hecht, D., Safran, M., Eisinger, M., David, G. and Yayon, A. (1994) Perlecan, basal lamina proteoglycan, promotes basic fibroblast growth factor-receptor binding, mitogenesis, and angiogenesis. Cell 79, 1005-1013.
3. Bashkin, P., Doctrow, S., Klagsbrun, M., Svahn, C. M., Folkman, J. and Vlodavsky, I. (1989) Basic fibroblast growth factor binds to subendothelial extracellular matrix and is released by heparitinase and heparin-like molecules. Biochemistry 28, 1737-1743.
4. Basilico, C. and Moscatelli, D. (1992). The FGF family of growth factors and oncogenes. Adv. Can. Res. 59, 115-165.
5. Bikfalvi, A., Klein, S., Pintucci, G., Quarto, N., Mignatti, P. and Rifkin, D. B. (1995) Differential modulation of cell phenotype by different molecular weight forms of basic fibroblast growth factor: possible intracellular signaling by the high molecular weight forms. J. Cell Biol. 129, 233-243.
6. Brigstock, D. R., Sasse, J. and Klagsbrun, M. (1991) Subcellular distribution of basic fibroblast growth factor in human hepatoma cells. Growth Factors 4, 189-196.
7. Bugler, B., Amalric, F. and Prats, H. (1991) Alternative initiation of translation determines cytoplasmic or nuclear localization of basic fibroblast growth factor. Mol. Cell. Biol. 11, 573-577.
8. Connolly, D. T., Stoddard, B. L., Harakas, N. K. and Feder, J. (1987) Human fibroblast-derived growth factor is a mitogen and chemoattractant for endothelial cells. Biochem. Biophys. Res. Commun. 144, 705-712.
9. Dell'Era, P., Presta, M. and Ragnotti, G. (1991) Nuclear localization of endogenous basic fibroblast growth factor in cultured endothelial cells. Exp. Cell Res. 192, 505-510.
10. Dono, R. and Zeller, R. (1994) Cell-type-specific nuclear translocation of fibroblast growth factor-2 isoforms during chicken kidney and limb morphogenesis. Develop. Biol. 163, 316-330.
11. Esch, F., Ueno, N., Baird, A., Hill, F., Denoroy, L., Ling, N., Gospodarowicz, D. and Guillemin, R. (1985) Primary structure of bovine brain acidic fibroblast growth factor (FGF). Biochem. Biophys. Res. Commun. 133, 554-562.
12. Flamme, I. and Risau, W. (1992) Induction of vasculogenesis and hematopoiesis in vitro. Development 116, 435-439.
13. Flamme, I., Breier, G. and Risau, W. (1995) Vascular endothelial growth factor (VEGF) and VEGF receptor 2 (flk-1) are expressed during vasculogenesis and vascular differentiation in the quail embryo. Develop. Biol. 169, 699-712.
14. Florkiewicz, R. Z. and Sommer, A. (1989) Human basic fibroblast growth factor gene encodes four polypeptides: three initiate translation from non-AUG codons. Proc. Natl Acad. Sci. USA 86, 3978-3981.
15. Florkiewicz, R. Z., Baird, A. and Gonzalez, A. M. (1991) Multiple forms of bFGF: differential nuclear and cell surface localization. Growth Factors 4, 265-275.
16. Florkiewicz, R. Z., Majack, R. A., Buechler, R. D. and Florkiewicz, E. (1995) Quantitative export of FGF-2 occurs through an alternative, energy-dependent, non-ER/Golgi pathway. J. Cell. Physiol. 162, 388-399.
17. Fontoura, B. M. A., Sorokina, E. A., David, E. and Carroll, R. B. (1992) p53 is covalently linked to 5.8S rRNA. Mol. Cell. Biol. 12, 5145-5151.
18. Giordano, S., Sherman, L., Lyman, W. and Morrison, R. (1992) Multiple molecular weight forms of basic fibroblast growth factor are developmentally regulated in the central nervous system. Develop. Biol. 152, 293-303.
19. Gospodarowicz, D., Neufeld, G., and Schweigerer, L. (1986) Fibroblast growth factor. Mol. Cell. Endocrinol. 46, 187-204.
20. Gospodarowicz, D., Ferrara, N., Haaparanta, T. and Neufeld, G. (1988) Basic fibroblast growth factor: expression in cultured bovine vascular smooth muscle cells. Eur. J. Cell Biol. 46, 144-151.
21. Gray, N. K. and Hentze, M. W. (1994) Iron regulatory protein prevents binding of the 43S translation pre-initiation complex to ferritin and eALAS mRNAs. EMBO J. 13, 3882-3891.
22. Hatten, M. E., Lynch, M., Rydel, R. E., Sanchez, J., Joseph-Silverstein, J., Moscatelli, D. and Rifkin, D. B. (1988) In vitro neurite extension by granule neurons is dependent upon astrolial-derived fibroblast growth factor. Develop. Biol. 125, 280-289.
23. Jackson, A., Friedman, S., Zhan, X., Engleka, K. A., Forough, R. and Maciag, T. (1992) Heat shock induces the release of fibroblast growth factor 1 from NIH 3T3 cells. Proc. Natl Acad. Sci. USA 89, 10691-10695.
24. Jones, O. T., Earnest, J. P., and McNamee, M. G. (1987) Solubilization and reconstitution of membrane proteins. In Biological Membranes, a Practical Approach. J. B. C. Findlay and W. H. Evans, eds, IRL Press, Oxford, pp. 139-177.
25. Kandel, J., Bossy-Wetzel, E., Radvanyi, F., Klagsbrun, M., Folkman, J. and Hanahan, D. (1991) Neovascularization is associated with a switch to the export of bFGF in the multistep development of fibrosarcoma. Cell 66, 1095-1104.
26. Kimelman, D. (1993) Peptide growth factors and the regulation of early amphibian development. Biochim. Biophys. Acta 1155, 227-237.
27. Liu, L., Doble, B. W. and Kardami, E. (1993) Perinatal phenotype and hypothyroidism are associated with elevated levels of 21.5-to 22-kDa basic fibroblast growth factor in cardiac ventricles. Develop. Biol. 157, 507-516.
28. Marechal, V., Elenbaas, B., Piette, J., Nicolas, J.-C. and Levine, A. J. (1994) The ribosomal L5 protein is associated with mdm-2 and mdm-2-p53 complexes. Mol. Cell. Biol. 14, 7414-7420.
29. McCarthy, J. E. G. and Kollmus, H. (1995) Cytoplasmic mRNA-protein interactions in eukaryotic gene expression. TIBS 20, 191-197.
30. Mignatti, P., Morimoto, T. and Rifkin, D. B. (1991) Basic fibroblast growth factor released by single, isolated cells stimulates their migration in an autocrine manner. Proc. Natl Acad. Sci. USA 88, 11007-11011.
31. Mignatti, P., Morimoto, T. and Rifkin, D. B. (1992) Basic fibroblast growth factor, a protein devoid of secretory signal sequence, is released by cells via a pathway independent of the endoplasmic reticulum-Golgi complex. J. Cell. Physiol. 151, 81-93.
32. Miyamato, M., Naruo, K., Seko, C., Matsumoto, S., Kondo, T. and Kurokawa, T. (1993) 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. 13, 4251-4259.
33. Moscatelli, D., Presta, M., Joseph-Silverstein, J. and Rifkin, D. B. (1986) Both normal and tumor cells produce basic fibroblast growth factor. J. Cell. Physiol. 129, 273-276.
34. Moscatelli, D. (1987) High and low affinity binding sites for basic fibroblast growth factor on cultured cells: absence of a role for low affinity binding in the stimulation of plasminogen activator production by bovine capillary endothelial cells. J. Cell. Physiol. 131, 123-130.
35. Moscatelli, D., Joseph-Silverstein, J., Manejias, R. and Rifkin, D. B. (1987) Mr 25,000 heparin-binding protein from guinea pig brain is a high molecular weight form of basic fibroblast growth factor. Proc. Natl Acad. Sci. USA 84, 5778-5782.
36. Moscatelli, D. and Quarto, N. (1989) Transformation of NIH 3T3 cells with basic fibroblast growth factor of the hst/K-fgf oncogene causes downregulation of the fibroblast growth factor receptor: reversal of morphological transformation and restoration of receptor number by suramin. J. Cell Biol. 109, 2519-2527.
37. Ornitz, D. M., Yayon, A., Flanagan, J. G., Svahn, C. M., Levi, E. and Leder, P. (1992) Heparin is required for cell-free binding of basic fibroblast growth factor to a soluble receptor and for mitogenesis in whole cells. Mol. Cell. Biol. 12, 240-247.
38. Powell, P. P. and Klagsbrun, M. (1991) Three forms of rat basic fibroblast growth factor are made from a single mRNA and localize to the nucleus. J. Cell. Physiol. 148, 202-210.
39. Prats, H., Kaghad, M., Prats, A. C., Klagsbrun, M., Lelias, J. M., Liauzun, P., Chalon, P., Tauber, J. P., Amalric, F., Smith, J. A. and Caput, D. (1989) High molecular mass forms of basic fibroblast growth factor are initiated by alternative CUG codons. Proc. Netl Acad. Sci. USA 86, 1836-1840.
40. Prats, A. C., Vagner, S., Prats, H. and Amalric, F. (1992) cis-acting elements involved in the alternative translation initiation process of human basic fibroblast growth factor mRNA. Mol. Cell. Biol. 12, 4796-4805.
41. Quarto, N., Finger, F. P. and Rifkin, D. B. (1991a) The NH2-terminal extension of high molecular weight bFGF is a nuclear targeting signal. J. Cell. Physiol. 147, 311-318.
42. Quarto, N., Talarico, D., Florkiewicz, R. and Rifkin, D. B. (1991b) Selective expression of high molecular weight basic fibroblast growth factor confers a unique phenotype to NIH 3T3 cells. Cell Regul. 2, 699-708.
43. Renko, M., Quarto, N., Morimoto, T. and Rifkin, D. B. (1990) Nuclear and cytoplasmic localization of different basic fibroblast growth factor species. J. Cell. Physiol. 144, 108-114.
44. Riese, J., Zeller, R. and Dono, R. (1995) Nucleo-cytoplasmic translocation and secretion of fibroblast growth factor-2 during avian gastrulation. Mech. Develop. 49, 13-22.
45. Roghani, M., Mansukhani, A., Dell'Era, P., Bellosta, P., Basilico, C., Rifkin, D. B. and Moscatelli, D. (1994) Heparin increases the affinity of basic fibroblast growth factor for its receptor but is not required for binding. J. Biol. Chem. 269, 3976-3984.
46. Schweigerer, L., Neufeld, G., Friedman, J., Abraham, J. A., Fiddes, J. C. and Gospodarowicz, D. (1987) Capillary endothelial cells express basic fibroblast growth factor, a mitogen that promotes their own growth. Nature 325, 257-259.
47. Smith, J. C. (1993) Mesoderm-inducing factors in early vertebrate development. EMBO J. 12, 4463-4470.
48. Sommer, A., Brewer, M. T., Thompson, R. C., Moscatelli, D., Presta, M. and Rifkin, D. B. (1987) A form of human basic fibroblast growth factor with an extended amino terminus. Biochem. Biophys. Res. Commun. 144, 543-550.
49. Tashiro, Y. and Siekevitz, P. (1965) Localization on hepatic ribosomes of protein newly synthesized in vivo. J. Mol. Biol. 11, 166-173.
50. Vagner, S., Gensac, M. C., Maret, A., Bayard, F., Amalric, F., Prats, H. and Prats, A. C. (1995) Alternative translation of human fibroblast growth factor 2 mRNA occurs by internal entry of ribosomes. Mol. Cell. Biol. 15, 35-44.
51. Vlodavsky, I., Folkman, J., Sullivan, R., Fridman, R., Ishai-Michaeli, R., Sasse J. and Klagsbrun, M. (1987) Endothelial cell-derived basic fibroblast growth factor: synthesis and deposition into subendothelial extracellular matrix. Proc. Netl Acad. Sci. USA 84, 2292-2296.
52. Weich, H. A., Iberg, N., Klagsbrun, M. and Folkman, J. (1990) Expression of acidic and basic fibroblast growth factors in human and bovine vascular smooth muscle cells. Growth Factors 2, 313-320.
53. Wool, I. G., Chan, Y.-L., and Gluck, A. (1996) Mammalian ribosomes: the structure and the evolution of the proteins. In Translational Control. J. W. B. Hershey, M. B. Mathews, and N. Sonenberg, eds, CSHL Press, New York, pp. 685-718.
54. Yayon, A., Klagsbrun, M., Esko, J. D., Leder, P. and Ornitz, D. M. (1991) Cell surface, heparin-like molecules are required for binding of basic fibroblast growth factor to its high affinity receptor. Cell 64, 841-848.