Kyoung Ro Kim, Yeon Kyu Kim, Dong Gyun Kang, Hyung Joon Cha
언어
영어(ENG)
URL
https://www.earticle.net/Article/A192562
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원문정보
초록
영어
Previously, we showed that simple paucimannosidic N-glycan structures in insect Drosophila S2 cells arise mainly because of β-N-acetylglucosaminidase (GlcNAcase) action, which removes terminal N-acetylglucosamine (GlcNAc) residues. In an earlier report, we suppressed GlcNAcase activity and clearly demonstrated that more complex N-glycanswithtwo terminal GlcNAc residues were synthesized. In the present work, we investigated synergistic effects of N-acetylglucosaminyltransferase II and/or β -1,4-galactosyltransferase co-expressions (by recombinant baculoviral infection) and GlcNAcase suppression (by knock-out screening) on N-glycan patterns. Using HPLC and MALDI-TOF MS analyses, we found that the N-glycosylation pattern of human erythropoietin secreted by engineered S2 cells expressing glycosyltransferase but not GlcNAcase was complete except for sialylation; N-glycan structures had two terminal galactose residues. Therefore, it will be possible to express complete functional human therapeutic glycoprotein in engineered Drosophila cells by suppressing GlcNAcase and co-expressing additional glycosyltransferases of N-glycosylation pathway.
저자
Kyoung Ro Kim [ Department of chemical Engineering, Pohang University of Science and Technology ]
Yeon Kyu Kim [ Department of chemical Engineering, Pohang University of Science and Technology ]
Dong Gyun Kang [ Department of chemical Engineering, Pohang University of Science and Technology ]
Hyung Joon Cha [ Department of chemical Engineering, Pohang University 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.