Biosynthesis and secretion of mucin-related products in Hs746T gastric cancer cells.
We have previously studied the biosynthesis and secretion of mucin in the normal human stomach and reported that the tetramer of the 60-kDa subunit of mucin core protein was synthesized and highly glycosylated, and that only high molecular weight mucin was secreted. In this study, we investigated the mucin-related products of a gastric cancer cell line (Hs746T). Analysis of intracellular and extracellular products immunoprecipitated with an anti-apomucin monoclonal antibody revealed that a 110-kDa protein, the dimer of the 55-kDa subunit, was synthesized and secreted. Tunicamycin treatment inhibited the secretion of the 110-kDa protein. These findings suggest that N-glycosylation may be involved in the secretory mechanism of the mucin-related product.
Sano
S
S
First Department of Internal Medicine, Kochi Medical School, Japan.
Okazaki
K
K
Yamamoto
Y
Y
D000230:Adenocarcinoma / Q000378:metabolism*; D002460:Cell Line; D006031:Glycosylation; D006801:Humans; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase / Q000494:pharmacology; D009077:Mucins / Q000096:biosynthesis / Q000378:metabolism*; D013274:Stomach Neoplasms / Q000378:metabolism*; D014407:Tumor Cells, Cultured; D014415:Tunicamycin / Q000494:pharmacology
D009077:Mucins; D014415:Tunicamycin; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase