@article {Porowska:2004:1107-3756:459,
title = "Inhibition of the O-glycan elongation limits MUC1 incorporation to cell membrane of human endometrial carcinoma cells",
journal = "International Journal of Molecular Medicine",
parent_itemid = "infobike://sp/ijmm",
publishercode ="sp",
year = "2004",
volume = "13",
number = "3",
publication date ="2004-03-01T00:00:00",
pages = "459-464",
itemtype = "ARTICLE",
issn = "1107-3756",
eissn = "1791-244X",
url = "https://www.ingentaconnect.com/content/sp/ijmm/2004/00000013/00000003/art00018",
author = "Porowska and Paszkiewicz-Gadek and Anchim and Wolczynski and Gindzienski",
abstract = "We have studied how benzyl-N-acetyl--D-galactosaminide, O-glycosylation inhibitor, affects the polymorphism and shedding of membrane-bound MUC1 mucin, and change in adhesive properties of cancer cells. In endometrial adenocarcinoma cells (Ishikawa line), high molecular weight
MUC1 mucin was shed from cellular membrane and could be detected in culture medium 24 h after [14C]threonine labelling. Short-time (2 days) exposure of these cells to benzyl-N-acetyl--D-galactosaminide was associated with a reduction in sialic acid level and increase in T antigen content
in cellular MUC1 mucin. These changes could be inverted after removal of the inhibitor. A longer, 6-day action of the inhibitor induced a decrease in sialic acid and T antigen levels in cellular MUC1 mucin. Benzyl-N-acetyl--D-galactosaminide treatment caused the occurrence of a few
incompletely glycosylated glycoforms of MUC1 in cells, but not in culture medium. Adhesion of endometrial cells to ECM compounds (type I collagen) was increased by benzyl-N-acetyl--D-galactosaminide treatment, indicating that glycosylation of extracellular domain of MUC1 can modulate
adhesive properties of cells.",
}