In the 1950s, pioneering studies by Erslev and others conclusively demonstrated the presence of a humoral factor capable of stimulating erythropoiesis (1,2). It was not until 1977, however, that Miyake et al. (3) isolated human erythropoietin (HuEPO) from the urine of severely anemic patients. Although preparation of the pure hormone allowed amino-acid sequencing of small EPO peptide fragments, it wasn't until 1983, with the use of unique probing strategies of a genomic library that the human EPO gene was cloned (4). In this chapter, we review the clinical pharmacology of recombinant human erythropoietin (rHuEPO), including its chemistry, pharmacologic actions, pharmacokinetics, pharmacodynamics, and activity in various patient populations. In addition, newer erythropoietic proteins, such as darbepoetin alfa, as well as some ongoing research approaches to creating other new erythropoietic molecules, are discussed.

From: Cancer Drug Discovery and Development Hematopoietic Growth Factors in Oncology: Basic Science and Clinical Therapeutics Edited by: G. Morstyn, M. A. Foote, and G. J. Lieschke © Humana Press Inc., Totowa, NJ

Fig. 1. EPO undergoes post-translational glycosylation at three specific asparagine residues (Asn24, Asn38, and Asn83) and one serine residue (Ser126).

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