Abstract
Endothelial cells and smooth muscle cells, the most abundant cell types in the blood vessel wall, normally have a low replication rate in the adult animal. However, endothelial cell proliferation and concomitant neovascularization is associated with tumor growth and the pathogenesis of numerous angiogenesis-dependent diseases.1 Also, accelerated smooth muscle cell replication plays a central role in atherogenesis,2 vascular graft stenosis,3 and restenosis of vessels following angioplasty or atherectomy.4 Fibroblast growth factor (FGF)-1 and FGF-2, also commonly known as acidic and basic FGF, respectively, are two of the polypeptide mitogens that are likely to be important mediators of vascular cell growth in vivo. They are both potent angiogenic factors5,6 and smooth muscle cell mitogens.7,8 They are expressed by vessel wall cells9,10 and by monocyte-derived macrophages within human atheroma.9,10 FGF-2 has also been detected in human platelets11 and T lymphocytes.12 Direct evidence for the involvement of FGF-2 in rat balloon injury-induced medial smooth muscle cell proliferation was reported by Lindner and Reidy.13 Therefore, it is possible that inhibition of FGF expression or action may be of therapeutic benefit in the treatment of human cardiovascular disease. One strategy that may prove effective for inhibition of FGF mitogenic activity is to interrupt the FGF intracellular signaling pathway. In this review, we describe our approach to identify proteins that are involved in FGF-1 mitogenic signal transduction and thus potential targets for therapeutic intervention.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
J. Folkman and Y. Shing, Angiogenesis, J. Biol. Chem. 267:10931 (1992).
R. Ross, The pathogenesis of atherosclerosis: A perspective for the 1990’s, Nature 362:801 (1993).
A.W. Clowes, Intimal hyperplasia and graft failure, Cardiovasc. Pathol. 2:1795 (1993).
J.N. Wilcox, Molecular biology: Insight into the causes and prevention of restenosis after arterial intervention, Am. J. Cardiol. 72:88E (1993).
L-Q. Pu, A.D. Sniderman, R. Brassard, K.J. Lachapelle, A.M. Graham, R. Lisbona, and J.F. Symes, Enhanced revascularization of the ischemic limb by angiogenic therapy, Circulation 88:208 (1993).
E.R. Edelman, M.A. Nugent, L.T. Smith, and M.J. Karnovsky, Basic fibroblast growth factor enhances the coupling of intimai hyperplasia and proliferation of vasa vasorum in injured rat arteries, J. Clin. Invest. 89:465 (1992).
S. Banai, M.T. Jaklitsch, W. Casscells, M. Shou, S. Shrivastav, R. Correa, S.E. Epstein, and E.F. Unger, Effects of acidic fibroblast growth factor on normal and ischemic myocardium, Circ. Res. 69:76 (1991).
V. Lindner, D.A. Lappi, A. Baird, R.A. Majack, and M.A. Reidy, Role of basic fibroblast growth factor in vascular lesion formation, Circ. Res. 68:106 (1991).
E. Brogi, J.A. Winkles, R. Underwood, S.K. Clinton, G.F. Alberts, and P. Libby, Distinct patterns of expression of fibroblast growth factors and their receptors in human atheroma and non-atherosclerotic arteries: Association of acidic FGF with plaque microvessels and macrophages, J. Clin. Invest. 92:2408 (1993).
S.E. Hughes, D. Crossman, and P.A. Hall, Expression of basic and acidic fibroblast growth factors and their receptor in normal and atherosclerotic human arteries, Cardiovasc. Res. 27:1214 (1993).
G. Brunner, H. Nguyen, J. Gabrilove, D.B. Rifkin, and E.L. Wilson, Basic fibroblast growth factor expression in human bone marrow and peripheral blood cells, Blood 81:631 (1993).
S. Blotnick, G.E. Peoples, M.R. Freeman, T.J. Eberlein, and M. Klagsbrun, T lymphocytes synthesize and export heparin-binding epidermal growth factor-like growth factor and basic fibroblast growth factor, mitogens for vascular cells and fibroblasts: Differential production and release by CD4+ and CD8+ T cells, Proc. Natl. Acad. Sci. USA 91:2890 (1994).
V. Lindner and M.A. Reidy, Proliferation of smooth muscle cells after vascular injury is inhibited by an antibody against basic fibroblast growth factor, Proc. Natl. Acad. Sci. USA 88:3739 (1991).
W.H. Burgess, A.M. Shaheen, M. Rayera, M. Jaye, P.J. Donohue, and J.A. Winkles, Possible dissociation of the heparin-binding and mitogenic activities of heparin-binding (acidic fibroblast) growth factor-1 from its receptor-binding activities by site-directed mutagenesis of a single lysine residue, J. Cell Biol. 111:2129 (1990).
W.H. Burgess, C.A. Dionne, J. Kaplow, R. Mudd, R. Friesel, A. Zilberstein, J. Schlessinger, and M. Jaye, Characterization and cDNA cloning of phospholipase C-gamma, a major substrate for heparin-binding growth factor 1 (acidic fibroblast growth factor)-activated tyrosine kinase, Mol. Cell. Biol. 10:4770 (1990).
J-K. Wang, G. Gao, and M. Goldfarb, Fibroblast growth factor receptors have different signaling and mitogenic potentials, Mol. Cell. Biol. 14:181 (1994).
D.K. Morrison, D.R. Kaplan, U. Rapp, and T.M. Roberts, Signal transduction from membrane to cytoplasm: Growth factors and membrane-bound oncogene products increase Raf-1 phosphorylation and associated protein kinase activity, Proc. Natl. Acad. Sci. USA 85:8855 (1988).
X. Zhan, X. Hu, B. Hampton, W.H. Burgess, R. Friesel, and T. Maciag, Murine cortactin is phosphorylated in response to fibroblast growth factor-1 on tyrosine residues late in the G1, phase of the BALB/c 3T3 cell cycle, J. Biol. Chem. 268:24427 (1993).
K.G. Peters, J. Marie, E. Wilson, H.E. Ives, J. Escobedo, M. Del Rosario, D. Mirda, and L.T. Williams, Point mutation of an FGF receptor abolishes phosphatidylinositol turnover and Ca2+ flux but not mitogenesis, Nature 358:678 (1992).
M. Mohammadi, C.A. Dionne, W. Li, N. Li, T. Spivak, A.M. Honegger, M. Jaye, and J. Schlessinger, Point mutation in FGF receptor eliminates phosphatidylinositol hydrolysis without affecting mitogenesis, Nature 358:681 (1992).
G.T. Williams, A.S. Abler, and L.F. Lau, Regulation of gene expression by serum growth factors, in: “Molecular and Cellular Approaches to The Control of Proliferation and Differentiation,” G.S. Stein and J.B. Lian, eds., Academic Press, Inc., New York (1992).
W.H. Burgess, A.M. Shaheen, B. Hampton, P.J. Donohue, and J.A. Winkles, Structure-function studies of heparin-binding (acidic fibroblast) growth factor-1 using site-directed mutagenesis, J. Cell. Biochem. 45:131 (1991).
Y. Furukawa, H. Piwnica-Worms, T.J. Ernst, Y. Kanakura, and J.D. Griffin, Cdc2 gene expression at the G1, to S transition in human lymphocytes, Science 250:805 (1990).
L.D. Kerr, J.T. Holt, and L.M. Matrisian, Growth factors regulate transin gene expression by c-fos-dependent and c-fos-independent pathways, Science 242:1424 (1988).
P.J. Donohue, G.F. Alberts, B.S. Hampton, and J.A. Winkles, A delayed-early gene activated by fibroblast growth factor-1 encodes a protein related to aldose reductase, J. Biol. Chem. 269:8604 (1994).
D.K.W. Hsu, P.J. Donohue, G.F. Alberts, and J.A. Winkles, Fibroblast growth factor-1 induces phosphofructokinase, fatty acid synthase and Ca2+-ATPase mRNA expression in NIH 3T3 cells, Biochem. Biophys. Res. Commun. 197:1483 (1993).
J.T. Holt, T. Venkat-Gopal, A.D. Moulton, and A.W. Nienhuis, Inducible production of c-fos antisense RNA inhibits 3T3 cell proliferation, Proc. Natl. Acad. Sci. USA 83:4794 (1986).
K. Nishikura and J.M. Murray, Antisense RNA of proto-oncogene c-fos blocks renewed growth of quiescent 3T3 cells, Mol. Cell. Biol. 7:639 (1987).
K. Kovary and R. Bravo, The jun and fos protein families are both required for cell cycle progression in fibroblasts, Mol. Cell. Biol. 11:4466 (1991).
M.A. Brach, H-J. Gruss, C. Sott, and F. Herrmann, The mitogenic response to tumor necrosis factor alpha requires cjun/AP-1, Mol. Cell. Biol. 13:4284 (1993).
Y. Shi, H.G. Hutchinson, D.J. Hall, and A. Zalewski, Downregulation of c-myc expression by antisense oligonucleotides inhibits proliferation of human smooth muscle cells, Circulation 88:1190 (1993).
S. Biro, Y-M. Fu, Z-X. Yu, and S.E. Epstein, Inhibitory effects of antisense oligodeoxynucleotides targeting c-myc mRNA on smooth muscle cell proliferation and migration, Proc. Natl. Acad. Sci. USA 90:654 (1993).
M.R. Bennett, S. Anglin, J.R. McEwan, R. Jagoe, A.C. Newby, and G.I. Evan, Inhibition of vascular smooth muscle cell proliferation in vitro and in vivo by c-myc antisense oligodeoxynucleotides, J. Clin. Invest. 93:820 (1994).
M. Simons and R.D. Rosenberg, Antisense nonmuscle myosin heavy chain and c-myb oligonucleotides suppress smooth muscle cell proliferation in vitro, Circ. Res. 70:835 (1992).
L.S. Mulcahy, M.R. Smith, and D.W. Stacey, Requirement for ras proto-oncogene function during serum-stimulated growth of NIH 3T3 cells, Nature 313:241 (1985).
W.E. Mercer, D. Nelson, A.B. DeLeo, L.J. Old, and R. Baserga, Microinjection of monoclonal antibody to protein p53 inhibits serum-induced DNA synthesis in 3T3 cells, Proc. Natl. Acad. Sci. USA 79:6309 (1982).
D. Jaskulski, J.K. DeRiel, W.E. Mercer, B. Calabretta, and R. Baserga, Inhibition of cellular proliferation by antisense oligodeoxynucleotides to PCNA cyclin, Science 240:1544 (1988).
E. Speir and S.E. Epstein, Inhibition of smooth muscle cell proliferation by an antisense oligodeoxynucleotide targeting the messenger RNA encoding proliferating cell nuclear antigen, Circulation 86:538 (1992).
M. Simons, E.R. Edelman, J-L. DeKeyser, R. Langer, and R.D. Rosenberg, Antisense c-myb oligonucleotides inhibit intimai arterial smooth muscle cell accumulation in vivo, Nature 359:67 (1992).
J. Abe, W. Zhou, J. Taguchi, N. Takuwa, K. Mild, H. Okazaki, K. Kurokawa, M. Kumada, and Y. Takuwa, Suppression of neointimal smooth muscle cell accumulation in vivo by antisense cdc2 and cdk2 oligonucleotides in rat carotid artery, Biochem. Biophys. Res. Commun. 198:16 (1994).
L.F. Lau and D. Nathans, Identification of a set of genes expressed during the G0/G1, transition of cultured mouse cells, EMBO J. 4:3145 (1985).
J.M. Almendral, D. Sommer, H. MacDonald-Bravo, J. Burckhardt, J. Perera, and R. Bravo, Complexity of the early genetic response to growth factors in mouse fibroblasts, Mol. Cell. Biol. 8:2140 (1988).
E. Boeggeman, A.S. Masibay, P.K. Qasba, and T. Sreevalsan, Identification and partial characterization of genes that are transactivated by different pathways in quiescent mouse cells stimulated with serum, J. Cell. Physiol. 145:286 (1990).
T. Nikaido, D.W. Bradley, and A.B. Pardee, Molecular cloning of transcripts that accumulate during the late G, phase in cultured mouse cells, Ezp. Cell Res. 192:102 (1991).
A. Lanahan, J.B. Williams, L.K. Sanders, and D. Nathans, Growth factor-induced delayed early response genes, Mol. Cell. Biol. 12:3919 (1992).
S. Vincent, L. Marty, L. LeGallic, P. Jeanteur, and P. Fort, Characterization of late response genes sequentially expressed during renewed growth of fibroblastic cells, Oncogene 8:1603 (1993).
S.V. Tavtigian, S.D. Zabludoff, and B.J. Wold, Cloning of mid-G, serum response genes and identification of a subset regulated by conditional myc expression, Mol. Biol. Cell 5:375 (1994).
B.H. Cochran, A.C. Reffel, and C.D. Stiles, Molecular cloning of gene sequences regulated by platelet-derived growth factor, Cell 33:939 (1983).
M. Gomperts, J.C. Pascall, and K.D. Brown, The nucleotide sequence of a cDNA encoding an EGF-inducible gene indicates the existence of a new family of mitogen-induced genes, Oncogene 5:1081 (1990).
P. Zumstein and C.D. Stiles, Molecular cloning of gene sequences that are regulated by insulin-like growth factor I, J. Biol. Chem. 262:11252 (1987).
J.A. Fernandez-Pol, D.J. Klos, and P.D. Hamilton, A growth factor-inducible gene encodes a novel nuclear protein with zinc finger structure, J. Biol. Chem. 268:21198 (1993).
T.H. Lee, G.W. Lee, E.B. Ziff, and J. Vilcek, Isolation and characterization of eight tumor necrosis factor-induced gene sequences from human fibroblasts, Mol. Cell. Biol. 10:1982 (1990).
V.V. Rangnekar, S. Waheed, T.J. Davies, F.G. Toback, and V.M. Rangnekar, Antimitogenic and mitogenic actions of interleukin-1 in diverse cell types are associated with induction of gro gene expression, J. Biol. Chem. 266:2415 (1991).
D.E. Sabath, P.L. Podolin, P.G. Comber, and M.B. Prystowsky, cDNA cloning and characterization of interleukin 2-induced genes in a cloned T helplymphocyte, J. Biol. Chem. 265:12671 (1990).
C. Beadling, K.W. Johnson, and K.A. Smith, Isolation of interleukin-2-induced immediate-early genes, Proc. Natl. Acad. Sci. USA 90:2719 (1993).
H. Matsushime, M.F. Roussel, R.A. Ashmun, and C.J. Shen, Colony-stimulating factor 1 regulates novel cyclins during the G1, phase of the cell cycle, Cell 65:701 (1991).
P. Liang and A.B. Pardee, Differential display of eukaryotic messenger RNA by means of the polymerase chain reaction, Science 257:967 (1992).
J. Welsh, K. Chada, S.S. Dalal, R. Cheng, D. Ralph, and M. McClelland, Arbitrarily primed PCR fingerprinting of RNA, Nucleic Acids Res. 20:4965 (1992).
D. Bauer, H. Muller, J. Reich, H. Riedel, V. Ahrenkiel, P. Warthoe, and M. Strauss, Identification of differentially expressed mRNA species by an improved display technique (DDRT-PCR), Nucleic Acids Res. 21:4272 (1993).
Y. Yoshitake and K. Nishikawa, Distribution of fibroblast growth factors in cultured tumor cells and their transplants, In Vitro Cell. Del. Biol. 28A:419 (1992).
M. Ii, H. Yoshida, Y. Aramaki, H. Masuya, T. Hada, M. Terada, M. Hatanaka, and Y. Ichimori, Improved enzyme immunoassay for human basic fibroblast growth factor using a new enhanced chemiluminescence system, Biochem. Biophys. Res. Commun. 193:540 (1993).
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1995 Springer Science+Business Media New York
About this chapter
Cite this chapter
Winkles, J.A., Donohue, P.J., Hsu, D.K.W., Guo, Y., Alberts, G.F., Peifley, K.A. (1995). Identification of FGF-1-Inducible Genes by Differential Display. In: Gallo, L.L. (eds) Cardiovascular Disease. GWUMC Department of Biochemistry Annual Spring Symposia. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1959-1_15
Download citation
DOI: https://doi.org/10.1007/978-1-4615-1959-1_15
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4613-5805-3
Online ISBN: 978-1-4615-1959-1
eBook Packages: Springer Book Archive