Abstract
Erythropoietin (Epo) is a glycoprotein hormone, which is the major regulator of mammalian erythropoiesis. Epo promotes the survival, proliferation and differentiation of erythroid progenitor cells by binding to and activation of the specific cell surface receptor (Epo-R) (D’ Andrea et al. , 1989; reviewed by Youssoufian et al. , 1993). The recently cloned cDNA of the murine Epo-R encodes a protein of 507 amino acids that contains a single hydrophobic membrane spanning domain. The Epo-R is a member of the cytokine receptor family, which include the receptors for granulocyte colonystimulating factor (G-CSF), interleukin-3 (IL-3), IL-4, granulocyte-macrophage colony-stimulating factor (GM-CSF) and several other growth factors (D’Andrea et al. , 1990; Bazan, 1990). Receptor polypeptides in this family share a set of four conserved Cys residues that stabilize the structure of the membrane-distal sub-domain and a five-residue motif located close to the transmembrane domain, Trp-Ser-X-Trp-Ser (WSXWS), that was predicted to be an essential component of the ligand-binding site of cytokine receptors (D’Andrea et al. , 1990; Bazan, 1990). For several members of the cytokine receptor family, generation of high-affinity receptors requires the formation of hetero-oligomers (reviewed by Sato and Miyajima, 1994).
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Just, U., Ahlers, N., Arman, G., Hunt, N., Ostertag, W., Nowock, J. (1996). Erythropoietin and the ENV gp55 of the Spleen Focus Forming Virus (SFFV) Interact Differently with Erythroid Cells in the Mouse and in Tissue Culture. In: Zander, A.R., Ostertag, W., Afanasiev, B.V., Grosveld, F. (eds) Gene Technology. NATO ASI Series, vol 94. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-61122-3_15
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DOI: https://doi.org/10.1007/978-3-642-61122-3_15
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