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Part of the book series: Milestones in Drug Therapy ((MDT))

Abstract

Recombinant erythropoietin is a 165-amino acid glycoprotein hormone with a molecular weight of 30.4 kDa that contains 39% carbohydrate [1, 2] and has the same biologic function as the endogenous product of a human gene located on chromosome 7q22 [3, 4]. Both the endogenous material (eEPO), and recombinant human glycoprotein (rHuEPO) bind a single receptor (EPOR) [57]. Although data from one group challenge this concept by suggesting signaling through a heterodimeric receptor including the beta-common cytokine receptor [8], these data have yet to be confirmed by other groups. For some years it had been widely accepted that EPOR was expressed broadly within the body in both normal and diseased tissues (e.g., [9]), but as discussed elsewhere in this book, methodological flaws in almost all of the published data draw this conclusion into doubt. To date, it is possible only to conclude with certainty that EPOR is expressed at effective levels in erythroid tissues in the bone marrow and spleen, so our discussion will focus only on the function of EPOR in that context.

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Molineux, G., Sinclair, A.M. (2009). Biology of erythropoietin. In: Elliott, S.G., Foote, M.A., Molineux, G. (eds) Erythropoietins, Erythropoietic Factors, and Erythropoiesis. Milestones in Drug Therapy. Birkhäuser Basel. https://doi.org/10.1007/978-3-7643-8698-6_3

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