caa a22 4500 47703800X CHVBK 20180405111309.0 cr unu---uuuuu 170330e19960601xx s 000 0 eng 10.1007/BF00437470 doi (NATIONALLICENCE)springer-10.1007/BF00437470 Involvement of heparan sulfate and related molecules in sequestration and growth promoting activity of fibroblast growth factor [Elektronische Daten] [Israel Vlodavsky, Hua-Quan Miao, Benjamin Medalion, Pamela Danagher, Dina Ron] Heparan sulfate proteoglycans (HSPGs) are ubiquitous macromolecules associated with the cell surface and extracellular matrix (ECM) of a wide range of cells of vertebrate and invertebrate tissues [1,2]. The basic HSPG structure consists of a protein core to which several linear heparan sulfate (HS) chains are covalently attached. The polysaccharide chains are typically composed of repeating hexuronic and D-glucosamine disaccharide units that are substituted to a varying extent with N- and O-linked sulfate moieties and N-linked acetyl groups [1,2]. Beside serving as a scaffold for the attachment of various ECM components (e.g., collagen, laminin, fibronectin), the binding of HS to certain proteins has been suggested to induce a conformational change which may lead to the exposure of novel reactive determinants or conversely stabilize an innert protein configuration [1-4]. Of particular significance is the interaction of HS with fibroblast growth factors (FGFs), mediating their sequestration, stabilization and high affinity receptor binding and signaling [3-7]. Cellular responses to FGFs may hence be modulated by metabolic inhibitors of HS synthesis and sulfation, HS-degrading enzymes, and synthetic mimetics of heparin/HS. In the present review we focus on the involvement of HS in basic FGF (bFGF) receptor binding and mitogenic activity and its modulation by species of heparin, HS, and synthetic polyanionic ‘heparin-mimicking' compounds. The results are discussed in relation to the current thoughts on the dual involvement of low and high affinity receptor sites in the growth promoting and angiogenic activities of bFGF and other heparin-binding growth factors. Kluwer Academic Publishers, 1996 heparin-mimicking compounds nationallicence extracellular matrix nationallicence heparan sulfate degrading enzymes nationallicence FGF-receptor binding nationallicence Vlodavsky Israel Department of Oncology, Hadassah-Hebrew University Hospital, Jerusalem, Israel aut Miao Hua-Quan Department of Oncology, Hadassah-Hebrew University Hospital, Jerusalem, Israel aut Medalion Benjamin Department of Oncology, Hadassah-Hebrew University Hospital, Jerusalem, Israel aut Danagher Pamela IBEX Technologies, Montreal, Canada aut Ron Dina Department of Biology, Technion, Israel Institute of Technology, Haifa, Israel aut Cancer and Metastasis Reviews Kluwer Academic Publishers; http://www.wkap.nl 15/2(1996-06-01), 177-186 0167-7659 15:2<177 1996 15 10555 https://doi.org/10.1007/BF00437470 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF00437470 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Vlodavsky Israel Department of Oncology, Hadassah-Hebrew University Hospital, Jerusalem, Israel aut NATIONALLICENCE 700 1- Miao Hua-Quan Department of Oncology, Hadassah-Hebrew University Hospital, Jerusalem, Israel aut NATIONALLICENCE 700 1- Medalion Benjamin Department of Oncology, Hadassah-Hebrew University Hospital, Jerusalem, Israel aut NATIONALLICENCE 700 1- Danagher Pamela IBEX Technologies, Montreal, Canada aut NATIONALLICENCE 700 1- Ron Dina Department of Biology, Technion, Israel Institute of Technology, Haifa, Israel aut NATIONALLICENCE 773 0- Cancer and Metastasis Reviews Kluwer Academic Publishers; http://www.wkap.nl 15/2(1996-06-01), 177-186 0167-7659 15:2<177 1996 15 10555 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer