Glycosylation is one of the most important post-translational modifications in mammalian cells. This catalytic reaction is processed by adding the various functional sugar moieties to protein through ER and Golgi apparatus. Most therapeutic proteins for human diseases are glycosylated and the glycan structures have been shown to affect therapeutic efficacy. In vivo half-life of therapeutic glycoproteins, in particular, is determined mainly by sialic acid capping at the end sites of N-linked glycans. The non-sialylated glycoproteins have significantly shorter in vivo half-life, because the exposed galactose residues are recognized, captured by asialoglycoprotein receptors (ASGPR) in hepatocytes and immediately degraded. Thus, it is greatly important to increase the terminal sialic acid contents of therapeutic glycoproteins for longer acting of therapeutics. In this presentation, the enhancement of sialylation of recombinant human erythropoietin as a model protein in CHO cells through sialylation pathway engineering approach will be discussed with the experimental data.
저자
Jung Hoe Kim [ 김정회 | Department of Biological Sciences, Korea Advanced Institute of Science and Technology ]
본 학회는 화학, 생화학, 분자생물학, 미생물학, 식품공학, 의학, 약학, 유전공학 및 생물공학, 환경 및 기타 공업 등 전 분야의 탄수화물관련 이론과 기술을 연구 발전시키고 산학협동을 통해 이를 보급하여 국내 관련 산업의 발전 및 국민생활의 과학화에 기여하고자 하며, 이러한 목표와 비젼의 실현을 위해 회원들이 적극적인 참여와 활동을 전개하고자 한다.