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cDNA cloning and expression of a human FGF receptor which binds acidic and basic FGF
S Wennström1, C Sandström, L Claesson-Welsh
1Ludwig Institute for Cancer Research, Biomedical Center, Uppsala, Sweden.
Growth Factors (Chur, Switzerland)
|January 1, 1991
Summary
Researchers identified a human fibroblast growth factor (FGF) receptor cDNA clone, phFGFR, which encodes a protein with high affinity for both acidic FGF (aFGF) and basic FGF (bFGF). This discovery advances understanding of FGF receptor signaling pathways.
Area of Science:
- Molecular Biology
- Cell Biology
- Biochemistry
Background:
- Fibroblast Growth Factors (FGFs) are crucial signaling molecules involved in various cellular processes.
- FGF receptors (FGFRs) mediate FGF signaling, playing key roles in development and disease.
- Characterization of specific FGFRs is essential for understanding their function and therapeutic potential.
Purpose of the Study:
- To isolate and characterize a cDNA clone encoding a human FGF receptor.
- To determine the binding affinities of acidic FGF (aFGF) and basic FGF (bFGF) to the identified receptor.
Main Methods:
- cDNA cloning and sequencing to identify the open reading frame.
- Transient expression in COS-1 cells for protein production.
- Immunoprecipitation and Western blotting to detect receptor forms.
- Crosslinking assays and Scatchard analysis to assess ligand binding.
Main Results:
- A cDNA clone, phFGFR, encoding an 820 amino acid polypeptide (hFGFR-1) was isolated.
- hFGFR-1 exhibits a mature form of 130 kDa and a precursor of 115 kDa.
- Binding studies revealed high affinity for both aFGF (Kd=25 pM) and bFGF (Kd=41 pM).
Conclusions:
- The phFGFR clone encodes a human FGF receptor (hFGFR-1) with high affinity for both aFGF and bFGF.
- This receptor plays a significant role in mediating FGF signaling.
- Further research into hFGFR-1 can elucidate its involvement in physiological and pathological processes.