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Effect of N ‐acetylglucosaminyltransferase V on the expressions of other glycosyltransferases
Author(s) -
Guo Peng,
Zhang Ying,
Shen Zong-hou,
Zhang Xia-ying,
Chen Hui-li
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(04)00188-7
Subject(s) - fucosyltransferase , glycosyltransferase , sialyltransferase , transfection , sialyl lewis x , enzyme , fucose , complementary dna , microbiology and biotechnology , sense (electronics) , chemistry , cell culture , fucosylation , biology , biochemistry , gene , glycoprotein , selectin , cell adhesion molecule , genetics
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 α1,3‐fucosyltransferase (FucT)‐III, ‐VI, ‐VII and the branching enzyme of O ‐glycans, core 2‐β1,6‐ 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 α2,3‐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.