Open AccessB3GNT2, a Polylactosamine Synthase, Regulates Glycosylation of EGFR in H7721 Human Hepatocellular Carcinoma Cells
Author(s) -
Hao Qiu,
Weiming Duan,
Ji Shu,
Hongxia Cheng,
Weiping Wang,
Xin-En Huang,
Huili Chen
Publication year - 2015
Publication title -
asian pacific journal of cancer prevention
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.512
H-Index - 75
eISSN - 2476-762X
pISSN - 1513-7368
DOI - 10.7314/apjcp.2014.15.24.10875
Subject(s) - retinoic acid , extracellular , glycosylation , hepatocellular carcinoma , epidermal growth factor receptor , signal transduction , cancer research , receptor , glycosyltransferase , chemistry , microbiology and biotechnology , biology , enzyme , biochemistry , gene
The epidermal growth factor receptor (EGFR) is an important surface receptor with N-glycans in its extracellular domain, whose glycosylation is essential for its function, especially in tumor cells. Here, we demonstrated that polylactosamine is markedly increased in H7721 hepatocellular carcinoma cells after treatment with EGF, while it apparently declined after exposure to all-trans retinoic acid (ATRA). In the study of the enzymatic mechanism of this phenomenon, we explored changes in the expression of poly-N-acetyllactosamine (PLN) branching glycosyltransferases using RT-PCR. Among the four glycosyltransferases with altered expression, GnT-V was most elevated by EGF, while GnT-V and B3GNT2 were most declined by ATRA. Next, we conducted co-immunoprecipitation experiments to test whether B3GNT2 and EGFR associate with each other. We observed that EGFR is a B3GNT2-targeting protein in H7721 cells. Taken together, these findings indicated that the altered expression of B3GNT2 will remodel the PLN stucture of EGFR in H7721 cells, which may modify downstream signal transduction.