Erythropoietin: Gene Cloning, Protein Structure, and Biological Properties
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Excerpt
The successful cloning of the gene for human erythropoietin (EPO) (Jacobs et al. 1985; Lin et al. 1985) has yielded information on the genetic organization and protein structure of this hormone and has allowed assessment of its biological properties. Biological studies have clearly indicated the clinical potential for this hormone in treatment of various anemias, and initial clinical studies of recombinant-DNA-produced human EPO (r-hEPO)1 are now under way.
EPO, a sialylglycoprotein hormone, is responsible for regulating the rate of red blood cell formation and for maintaining the red blood cell mass (Krantz and Jacobson 1970; Graber and Krantz 1978; Spivak and Graber 1980). EPO is produced primarily by the kidney in adults and by the liver during fetal life and is secreted into the circulation (Jacobsen et al. 1957; Fried 1972; Zanjani et al. 1981). Circulating levels of EPO are approximately 20 mU/ml (Koeffler and Goldwasser 1981; Cotes 1982; Garcia...
