Core 2 beta 1,6-N-acetylglucosaminyltransferases and alpha 1,3-fucosyltransferases regulate the synthesis of O-glycans on selectin ligands on oral cavity carcinoma cells
J. Renkonen et al., Core 2 beta 1,6-N-acetylglucosaminyltransferases and alpha 1,3-fucosyltransferases regulate the synthesis of O-glycans on selectin ligands on oral cavity carcinoma cells, APMIS, 109(7-8), 2001, pp. 500-506
Selectin-dependent cell binding has importance in the extravasation of bloo
d-circulating tumor cells and in the generation of metastases. Cell surface
glycoproteins; decorated with sialylated, fucosylated epitopes, such as si
alyl Lewis(x) (sLe(x)) are ligands for selectins. Not only terminal sLex mo
ieties but also proximal core structures contribute to the formation of bin
ding epitopes for selectins. Core 2 beta1,6-N-acetylglucosaminyltransferase
s (C2GnT) and alpha1,3-fucosyltransferases (alpha1,3-FucT) have been sugges
ted to be the rate-limiting enzymes in the synthesis of selectin ligands. W
e analyzed oral cavity epithelial carcinoma cell lines and showed their exp
ression of RNA transcripts for C2GnT and alpha1,3-FucT, identified alpha1,3
-FucT enzyme activities, and analyzed the cell surface sLe(x) expression le
vels. Neither the pattern of expressed enzymes nor the alpha1,3-FucT activi
ty directly predicted the binding capacity of E-selectin. However, only the
sLe(x)-expressing cell lines were capable of binding to E-selectin, but no
t to P-selectin, thus putatively promoting the selectin-mediated metastasis
. These findings suggest that C2GnT in combination with alpha1,3-Fuc-T cont
ribute to the selectin-mediated metastasis in oral cavity carcinomas.