A naturally occurring secreted form of fibroblast growth factor (FGF) receptor 1 binds basic FGF in preference over acidic FGF

Alternatively spliced variants of fibroblast growth factor receptor 1 mRNA are predicted to encode secreted forms and membrane-bound forms of receptors. The predicted amino acid sequences of these receptor variants differ in a portion of the extracellular region. In this study, we characterized the...

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Bibliographic Details
Published in:The Journal of biological chemistry 1992-08, Vol.267 (23), p.16076-16080
Main Authors: DUAN, D.-S. R, WERNER, S, WILLIAMS, L. T
Format: Article
Language:English
Subjects:
Animals
binding
Biological and medical sciences
Cell receptors
Cell structures and functions
Chickens
CHO Cells
Cricetinae
Cross-Linking Reagents
fibroblast growth factor
fibroblast growth factor (acidic)
fibroblast growth factor (basic)
Fibroblast Growth Factor 1 - metabolism
Fibroblast Growth Factor 2 - metabolism
Fundamental and applied biological sciences. Psychology
Hormone receptors. Growth factor receptors. Cytokine receptors. Prostaglandin receptors
Humans
Kinetics
Macromolecular Substances
man
Molecular and cellular biology
Protein Conformation
receptors
Receptors, Cell Surface - genetics
Receptors, Cell Surface - isolation & purification
Receptors, Cell Surface - metabolism
Receptors, Fibroblast Growth Factor
specificity
Transfection
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Summary:Alternatively spliced variants of fibroblast growth factor receptor 1 mRNA are predicted to encode secreted forms and membrane-bound forms of receptors. The predicted amino acid sequences of these receptor variants differ in a portion of the extracellular region. In this study, we characterized the function of one of these splice variants which was predicted by its cDNA to be a secreted FGF receptor. We expressed this secreted form of the human FGFR1 (sFGFR1) in Chinese hamster ovary cells. The sFGFR1 protein oligomerized upon ligand binding. Surprisingly, the sFGFR1 preferentially bound basic FGF over acidic FGF. In cross-linking experiments, the sFGFR1 showed higher binding affinity for basic FGF (Kd approximately 30 nM) than for acidic FGF (Kd greater than 300 nM). These results suggest that this secreted form of FGF receptor has an unusual ligand binding specificity that may be important for its biological role in vivo.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(18)41968-0