Abstract

The GFRα1 cDNA was amplified by RT-PCR from fetal rat hippocampus. The soluble recombinant GFRa1 and its mutants were obtained from an Escherichia coli expression system. The biological activity of soluble GFRα1 and its mutants were evaluated in PC12 cells. The results suggest that the central domain of GFRα1 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 GFRα1.

Keywords: glial cell line-derived neurotrophic factor receptor, mutation, expression, pc12 cells, surival and differentiation