EFFECT OF DOXYCYCLINE-REGULATED CHAPERONE EXPRESSION ON RECOMBINANT PROTEIN PRODUCTIVITY IN CHO CELLS

摘要

Human thrombopoietin (hTPO) is a potential therapeutic glycoprotein for the amelioration of thrombocytopenia associated with chemotherapy, irradiation and bone marrow transplantation. Posttranslational modification of a product protein includes various rate-limiting interactions with numerous chaperones and enzymes in the secretory pathway. The efficient secretion of recombinant proteins from eukaryotic cells requires simple targeting the proteins to endoplasmic reticulum (ER) and directing their translocation into lumenal compartment of the ER. Although many groups overexpressed chaperone proteins in recombinant CHO cells (rCHO), effect of elevated ERp57 expression level on the secretion of foreign protein in CHO cells has not been reported yet.