Guo Peng, Zhang Ying, Shen Zong-hou, Zhang Xia-ying, Chen Hui-li
Key Laboratory of Glycoconjugate Research, Ministry of Health, Department of Biochemistry, Shanghai Medical College, Fudan University, Shanghai 200032, PR China.
FEBS Lett. 2004 Mar 26;562(1-3):93-8. doi: 10.1016/S0014-5793(04)00188-7.
Transfection of sense cDNA of N-acetylglucosaminyltransferase V (GnTV) into H7721 human hepatocellular carcinoma cells resulted in the decreased expression of surface sialyl Lewis X (SLe(x)), a sialylated fucose-containing antigen. The enzymatic mechanisms were speculated to be the concomitantly decreased expression of alpha1,3-fucosyltransferase (FucT)-III, -VI, -VII and the branching enzyme of O-glycans, core 2-beta1,6-N-acetylglucosaminyltransferase (C2GnT)-I, -II. These two glycosyltransferase families were suggested to be the key enzymes in the synthesis of SLe(x). The expression of alpha2,3-sialyltransferase (ST3)-IV, but not ST3-I, -II and -III was elevated by sense GnTV. However, it did not cause the increase of SLe(x) synthesis. Transfection of antisense GnTV into H7721 cells showed entirely opposite effects on the expression of above-mentioned SLe(x) and glycosyltransferases as the sense GnTV.
将N-乙酰葡糖胺基转移酶V（GnTV）的正义cDNA转染至H7721人肝癌细胞中，导致表面唾液酸化路易斯X（SLe(x)）表达降低，SLe(x)是一种含唾液酸的岩藻糖抗原。推测其酶促机制是α1,3-岩藻糖基转移酶（FucT）-III、-VI、-VII以及O-聚糖分支酶、核心2-β1,6-N-乙酰葡糖胺基转移酶（C2GnT）-I、-II的表达同时降低。这两个糖基转移酶家族被认为是SLe(x)合成中的关键酶。正义GnTV使α2,3-唾液酸转移酶（ST3）-IV的表达升高，但ST3-I、-II和-III的表达未升高。然而，这并未导致SLe(x)合成增加。将反义GnTV转染至H7721细胞中，对上述SLe(x)和糖基转移酶表达的影响与正义GnTV完全相反。
