TY - JOUR
T1 - Cell surface, heparin-like molecules are required for binding of basic fibroblast growth factor to its high affinity receptor
AU - Yayon, Avner
AU - Klagsbrun, Michael
AU - Esko, Jeffrey D.
AU - Leder, Philip
AU - Ornitz, David M.
N1 - Funding Information:
This work was supported by grants from the Israel Cancer Research Fund (A. Y.), National Institutes of Health grants CA 37329 and CA 45548 (M. K.) and GM 33063 and CA 46482 (J. D. E.), and by E. I. DuPont de Nemours Co., Inc. and the Howard Hughes Medical Institute (P L., D. M. 0.) The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked “advertisement” in accordance with 18 USC Section 1734 solely to indicate this fact.
PY - 1991/2/22
Y1 - 1991/2/22
N2 - The role of low affinity, heparin-like binding sites for basic fibroblast growth factor (bFGF) was investigated noglycans. Heparan sulfate-deficient mutants transfected to express a cloned mouse FGF receptor cDNA are not able to bind bFGF. It is demonstrated that free heparin and heparan sulfate can reconstitute a low affinity receptor that is, in turn, required for the high affinity binding of bFGF. These studies suggest that the low affinity receptor is an accessory molecule required for binding of bFGF to the high affinity site. Such an obligatory interaction of low and high affinity FGF receptors suggests a physiological role for heparin-like, low affinity receptors and constitutes a novel mechanism for the regulation of growth factor-receptor interactions.
AB - The role of low affinity, heparin-like binding sites for basic fibroblast growth factor (bFGF) was investigated noglycans. Heparan sulfate-deficient mutants transfected to express a cloned mouse FGF receptor cDNA are not able to bind bFGF. It is demonstrated that free heparin and heparan sulfate can reconstitute a low affinity receptor that is, in turn, required for the high affinity binding of bFGF. These studies suggest that the low affinity receptor is an accessory molecule required for binding of bFGF to the high affinity site. Such an obligatory interaction of low and high affinity FGF receptors suggests a physiological role for heparin-like, low affinity receptors and constitutes a novel mechanism for the regulation of growth factor-receptor interactions.
UR - http://www.scopus.com/inward/record.url?scp=0025976838&partnerID=8YFLogxK
U2 - 10.1016/0092-8674(91)90512-W
DO - 10.1016/0092-8674(91)90512-W
M3 - Article
C2 - 1847668
AN - SCOPUS:0025976838
SN - 0092-8674
VL - 64
SP - 841
EP - 848
JO - Cell
JF - Cell
IS - 4
ER -