Secretion of biologically active recombinant human erythropoietin in mammalian cell culture

Erythropoietin is the main hormone involved in the process of erythroid differentiation. Human EPO is a highly glycosilated protein, and its natural source for purification is the urine of patients with severe aplastic anemia. Here we report on the secretion of biologically active rhEPO by Chinese hamster ovary cells. Erythropoietin (EPO) is the main hormone involved in the process of erythroid differentiation. Human EPO is a highly glycosilated protein, and its natural source for purification is the urine of patients with severe aplastic anemia. The need of hEPO in the world is growing dramatically, while production from urine is step-limiting. The protein is too complex to be produced in active form by recombinant technology in bacteria or yeast. The only reliable source for recombinant hEPO are mammalian cells, where the cloned hEPO cDNA had been expressed (1, 2). Here we report on the secretion of biologically active rhEPO by Chinese hamster ovary (CHO) cells