O-GlcNAc(O-linked-N-acetylglucosamine) modification is one of the protein post- translational modifications that is involved in many cellular processes, including signal transduction, transcription, translation, cell proliferation and apoptosis. It is known that, on some proteins, this modification can affect the O-phosphorylation state of the proteins. UDP-GlcNAc, the precursor of O-GlcNAc, is mainly synthesized from glucose by HBP(Hexosamine Biosynthetic Pathway), which is sensitive to glucose concentration. Here, we confirmed that there is an inevitable decrease in the glucose concentration in the media during cell culture by the cell metabolism. Because O-GlcNAc is sensitive to the glucose concentration, the decrease is supposed to affect the cellular processes. In this study, the decrease in glucose concentration during cell culture was assessed in many cell lines. In some cell lines, the concentration decreased to a much lower level compared to the original. With this change, the O-GlcNAc level also appeared to decrease.A comparison was made between a glucose- concentration-maintained sample and a non-maintained one, where a difference in insulin signal transduction was observed. The phoshporylation level of Akt was likely to decrease with the maintainence of glucose while the O-GlcNAcylation level of it increased. This means decreased level of acitvated Akt. This was confirmed by checking the downstream protein, GSK(Glycogen synthase kinase), which was found to be less phophorylated under glucose-maintained condition.These findings provide us an evidence of the crosstalk between O-GlcNAcylation and O-phosphorylation on Akt. It corresponds with the insulin insensitivity of type II diabetes. These findings also suggest the importance of glucose condition during cell culturing.
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.