Cell surface, heparin-like molecules are required for binding of basic fibroblast growth factor to its high affinity receptor

Avner Yayon, Michael Klagsbrun, Jeffrey D. Esko, Philip Leder, David M. Ornitz

Research output: Contribution to journalArticle

1999 Scopus citations

Abstract

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.

Original languageEnglish
Pages (from-to)841-848
Number of pages8
JournalCell
Volume64
Issue number4
DOIs
StatePublished - Feb 22 1991
Externally publishedYes

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