Abstract
The GFRalpha1 cDNA was amplified by RT-PCR from fetal rat hippocampus. The soluble recombinant GFRalpha1 and its mutants were obtained from an Escherichia coli expression system. The biological activity of soluble GFRalpha1 and its mutants were evaluated in PC12 cells. The results suggest that the central domain of GFRalpha1 is a crucial determinant for ligand binding. This established a solid basis for further study to find the key amino acid mediating the binding of GDNF and GFRalpha1.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Cell Differentiation / drug effects
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Cell Survival / drug effects
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DNA Primers / genetics
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Escherichia coli / metabolism
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Gene Deletion
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Glial Cell Line-Derived Neurotrophic Factor Receptors
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Hippocampus / chemistry
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Humans
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Models, Molecular
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PC12 Cells
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Protein Binding
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Protein Structure, Secondary
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Protein Structure, Tertiary / genetics
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Proto-Oncogene Proteins / genetics*
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Proto-Oncogene Proteins / metabolism*
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Proto-Oncogene Proteins / pharmacology
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Proto-Oncogene Proteins c-ret
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Rats
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Receptor Protein-Tyrosine Kinases / genetics*
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Receptor Protein-Tyrosine Kinases / metabolism*
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Receptor Protein-Tyrosine Kinases / pharmacology
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Recombinant Proteins / pharmacology
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Structure-Activity Relationship
Substances
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DNA Primers
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GFRA1 protein, human
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Gfra1 protein, rat
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Glial Cell Line-Derived Neurotrophic Factor Receptors
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Proto-Oncogene Proteins
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Recombinant Proteins
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Proto-Oncogene Proteins c-ret
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Receptor Protein-Tyrosine Kinases