Tachibana H, Jiyoun K, Taniguchi K, Ushio Y, Teruya K, Osada K, Inoue Y, Shirahata S, Murakami H
Graduate School of Genetic Resources Technology, Kyushu University, Fukuoka, Japan.
In Vitro Cell Dev Biol Anim. 1996 Mar;32(3):178-83. doi: 10.1007/BF02723683.
We have characterized the effects of serum and N-acetylglucosamine in a glucose-deprived condition on the glycosylation of antibody light chains, as well as the resulting biological properties of those antibodies. We have chosen for our investigation the human hybridoma lines producing monoclonal antibodies reactive to lung adenocarcinoma. Each antibody possess a N-glycosylated carbohydrate chain in the hypervariable region of the light chains. When the cell lines were grown in the absence of glucose, variant light chains with varying molecular masses were found to be secreted. Analysis of these light chains produced in a glucose-deprived condition revealed that the changed molecular-mass of the variant light chains is due to different glycosylation. Addition of N-acetylglucosamine or fetal calf serum to the glucose-free medium led to the creation of other light chains that exhibit increased antigen binding activity.
我们已经研究了血清和N-乙酰葡糖胺在葡萄糖缺乏条件下对抗体轻链糖基化的影响，以及这些抗体由此产生的生物学特性。我们选择了产生对肺腺癌有反应的单克隆抗体的人杂交瘤细胞系进行研究。每种抗体在轻链的高变区都有一条N-糖基化的碳水化合物链。当细胞系在无葡萄糖的情况下生长时，发现分泌出了分子量不同的变异轻链。对在葡萄糖缺乏条件下产生的这些轻链的分析表明，变异轻链分子量的变化是由于不同的糖基化所致。向无葡萄糖培养基中添加N-乙酰葡糖胺或胎牛血清会导致产生其他具有增强抗原结合活性的轻链。
