The erythropoietin receptor (EPOR) and its cognate ligand, erythropoietin (EPO), are required for maintaining adequate levels of circulating erythrocytes during embryogenesis and adulthood by promoting erythroid mitogenesis, survival, and differentiation. Before the cloning of the EPOR cDNA, radiolabeled EPO was used to demonstrate specific binding to normal erythroid progenitors, murine and human erythroleukemia cells, and cells from human fetal liver. Then in 1989, the EPOR cDNA has been cloned by transfection of recombinant plasmid pools of murine cDNA from murine erythroleukemia (MEL) cell line into COS cells. A single cDNA was isolated that confers to COS cells the ability to bind EPO (D’Andrea et al. 1989). This murine EPOR cDNA, expressed in COS cells, generates high-affinity (30 pM) and low-affinity (210 pM) receptors. In 1990, the human homologue of the murine EPORhas been isolated from an erythroleukemia line and from fetal liver (Jones...
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