Control of Cell Proliferation by Heparan Sulfate and Heparin-Binding Growth Factors

• References

• 1 Gallagher JT, Lyon M, Steward WP. Structure and function of heparan sulfate proteoglycans. Biochem. J. 1986; 236: 313-325
• 2 Kjellen L, Lindahl U. Proteoglycans: structures and interaction. Annu. Rev. Biochem. 1991; 60: 443-475
• 3 Jackson RL, Busch SJ, Cardin AL. Glycosaminoglycans: molecular properties, protein interactions, and role in physiological processes. Physiol. Rev. 1991; 71: 481-539
• 4 Gitay-Goren H, Soker S, Vlodavsky I, Neufeld G. Cell surface associated heparin-like molecules are required for the binding of vascular endothelial growth factor (VEGF) to its cell surface receptors. J. Biol. Chem. 1992; 267: 6093-6098
• 5 Ruoslahti E, Yamaguchi Y. Proteoglycans as modulators of growth factor activities. Cell 1991; 64: 867-869
• 6 Vlodavsky I, Bar-Shavit R, Korner G, Fuks Z. Extracellular matrix- bound growth factors, enzymes and plasma proteins. In: Basement Membranes: Cellular and Molecular Aspects. Timpl DH R, Orlando R. (eds). Academic Press; Orlando, FL: 1993. pp 327-343
• 7 Yayon A, Klagsbrun M, Esko JD, Leder P, Ornitz DM. Cell surface, heparin-like molecules are required for binding of basic fibroblast growth factor to its high affinity receptor. Cell 1991; 64: 841-848
• 8 Lindahl U. Biosynthesis of heparin and related polysaccharides. In: Heparin: Chemical and Biological Properties, Clinical Applications.. Lane DA, Lindahl U. eds) Edward Arnold; London: 1989. pp. 159-189
• 9 Ornitz DM, Yayon A, Flanagan JG, Svahn CM, Levi E, Lederxy P. Heparin is required for cell-free binding of bFGF to a soluble receptor and for mitogenesis in whole cells. Mol. Cell Biol 1992; 12: 240-247
• 10 Rapraeger A, Krufka A, Olwin BR. Requirement of heparan sulfate for bFGF-d fibroblast growth and myoblast differentiation. Science 1991; 252: 1705-1708
• 11 Turnbull JE, Femig DG, Ke Y, Wilkinson M, Gallagher JT. Identification of basic fibroblast growth factor binding sequence in fibroblast heparan sulfate. J. Biol. Chem. 1992; 267: 10337-10341
• 12 Aviezer D, Levy E, Safran M, Svahn C, Buddecke E, Schmidt A, David G, Vlodavsky I, Yayon A. Differential structural requirements of heparin and heparan sulfate proteoglycans that promote binding of basic fibroblast growth factor to its receptor. J. Biol. Chem. 1994; 269: 114-121
• 13 Ishihara M, Tyrell DJ, Stauber GB, Brown S, Cousens L, Stack RJ. Preparation of affinity -fractionated heparin-derived oligosaccharides and their effects on selected biological activities mediated by basic fibroblast growth factor. J. Biol. Chem. 1993; 263: 4675-4683
• 14 Guimond S, Maccarana M, Olwin BB, Lindahl U, Rapraeger AC. Activating and inhibiting sequences for FGF-2 (Basic FGF). J Biol. Chem. 1993; 268: 23906-23914
• 15 Spivak-Kroizman T, Lemmon MA, Dikic I, Ladbury JE, Pinchasi D, Huang J, Jaye M, Crumley G, Schlessinger J, Lax I. Heparin- induced oligomerization of FGF molecules is responsible for FGF receptor dimerization, activation, and cell proliferation. Cell 1994; 79: 1015-1024
• 16 Benezra M, Ben-Sasson SA, Regan J, Chang M, Bar-Shavit R, Vlodavsky I. Antiproliferative activity towards vascular smooth muscle cells and receptor binding of heparin-mimicking anionic aromatic compounds. Arteriosclerosis and Throm. 1994; 14: 1989-1992
• 17 Benezra M, Vlodavsky I, Yayon A, Bar-Shavit R, Ben-Sasson S. Reversal of bFGF-mediated autocrine cell transformation by aromatic anionic compounds. Cancer Res 1992; 52: 5656-5662
• 18 Miao HQ, Esko JD, Fritz TA, Yayon A, Vlodavsky I. Restoration of bFGF-receptor binding by heparan sulfate primed on /J-D-xylo- sides. J. Cell Biochem.. 1995 in press
• 19 Bashkin P, Doctrow S, Klagsbrun M, Svahn CM, Folkman J, Vlodavsky I. Basic fibroblast growth factor binds to subendothelial extracellular matrix and is released by heparitinase and heparin-like molecules. Biochemistry 1989; 28: 1737-1743
• 20 Sasisekharan R, Moses MA, Nugent MA, Cooney CL, Langer R. Heparinase inhibits neovascularization. Proc. Natl. Acad. Sci USA 1994; 91: 1524-1528
• 21 Vlodavsky I, Bar-Shavit R, Ishai-Michaeli R, Bashkin P, Fuks Z. Extracellular sequestration and release of fibroblast growth factor: a regulatory mechanism. Trends Biochem Sci 1991; 16: 268-271
• 22 Gospodarowicz D, Delgado D, Vlodavsky I. Permissive effect of the extracellular matrix on cell proliferation in-vitro. Proc. Natl. Acad. Sci. USA 1980; 77: 4094-4098
• 23 Vlodavsky I, Liu GM, Gospodarowicz D. Morphological appearance, growth behavior and migratory activity of human tumor cells maintained on extracellular matrix vs. plastic. Cell 1980; 19: 607-616
• 24 Vlodavsky I, Folkman J, Sullivan R, Fridman R, Ishai-Michaeli R, Sasse J, Klagsbrun M. Endothelial cell-derived basic fibroblast growth factor: synthesis and deposition into subendothelial extracellular matrix. Proc. Natl. Acad. Sci. USA 1987; 84: 2292-2296
• 25 Cardon-Cardo C, Vlodavsky I, Haimovitz-Friedman A, Hicklin D, Fuks Z. Expression of basic fibroblast growth factor in normal human tissues. Lab. Invest. 1990; 63: 832-840
• 26 Saksela O, Moscatelli D, Sommer A, Rifkin DB. Endothelial cell- derived heparan sulfate binds basic fibroblast growth factor and protects it from proteolytic degradation. J. Cell Biol. 1988; 107: 743-751
• 27 Benezra M, Vlodavsky I, Ishai-Michaeli R, Neufeld G, Bar-Shavit R. Thrombin-induced release of active basic fibroblast growth factor-heparan sulfate complexes from subendothelial extracellular matrix. Blood 1993; 81: 3324-3331
• 28 Rogelj S, Klagsbrun M, Atzmon R, Kurokawa M, Haimovitz A, Fuks Z, Vlodavsky I. Basic fibroblast growth factor is an extracellular matrix component required for supporting the proliferation of vascular endothelial cells and the differentiation of PC 12 cells. J. Cell Biol. 1989; 109: 823-831
• 29 Fritz TA, Lugemwa FN, Sarkar AK, Esko JD. Biosynthesis of heparan sulfate on /3-D-xylosides depends on aglycone structure. J. Biol.. Chem. 1994; 269: 300-307
• 30 Aviezer D, Hecht D, Safran M, Eisinger M, David G, Yayon A. Perlecan, basal lamina proteoglycan, promotes basic fibroblast growth factor-receptor binding, mitogenesis, and angiogenesis. Cell 1994; 79: 1005-1013
• 31 Schmidt A, Yoshida K, Buddecke E. The antiproliferative activity of arterial heparan sulfate resides in domains enriched with 2-0- sulfated uronic acid residues. J. Biol. Chem. 1992; 267: 19242-19247
• 32 Mascarelli F, Fuhrmann G, Courtois Y. aFGF binding to low and high affinity receptors induces both aFGF and aFGF receptors dimerization. Growth Factors 1993; 8: 211-233
• 33 Flaumenhaft R, Moscatelli D, Rifkin DB. Heparin and heparan sulfate increase the radius of diffusion and action of basic fibroblast growth factor. J. Cell Biol. 1990; 111: 1651-1659