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Altered glycosylation of membrane glycoproteins in human uroepithelial cell lines
Author(s) -
Debray Henri,
Qin Zhu,
Delannoy Philippe,
Montreuil Jean,
Duś Danuta,
Radzikowski Czeslaw,
Christensen Britta,
Kieler Jørgen
Publication year - 1986
Publication title -
international journal of cancer
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.475
H-Index - 234
eISSN - 1097-0215
pISSN - 0020-7136
DOI - 10.1002/ijc.2910370421
Subject(s) - glycoprotein , glycosylation , membrane glycoproteins , microbiology and biotechnology , human cell , membrane protein , biology , cell culture , biochemistry , membrane , genetics
Total cellular glycopeptides of 7 human uroepithelial cell lines that differ in the grade of transformation (TGr) were analysed by gel filtration and affinity chromatography on immobilized lectins. The 4 cell lines that are tumorigenic in nude mice and invasive in vitro (TGr III) possess more highly branched, tri‐ and tetraantennary N‐acetyllactosaminic glycans, with less biantennary glycans than the 2 non‐tumorigenic, non‐invasive (TGr II) cell lines examined. The only exception to this general pattern is the third cell line, which is classified as TGr II. The cellular glycopeptide distribution pattern in this cell line is similar to that of the TGr III cells. The possible relationship between altered glycosylation of membrane glycoproteins and the expression of a malignant phenotype is discussed.