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Altered glycosylation of membrane glycoproteins in human uroepithelial cell lines

✍ Scribed by Henri Debray; Zhu Qin; Philippe Delannoy; Jean Montreuil; Danuta Duś; Czeslaw Radzikowski; Britta Christensen; Jørgen Kieler

Publisher
John Wiley and Sons
Year
1986
Tongue
French
Weight
513 KB
Volume
37
Category
Article
ISSN
0020-7136

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✦ Synopsis

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 Ill) possess more highly branched, tri-and tetraantennary N-acetyllactosaminic glycans, with less biantennary glycans than the 2 non-tumorigenic, noninvasive (TGr 11) 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 111 cells. The possible relationship between altered glycosylation of membrane glycoproteins and the expression of a malignant phenotype is discussed.

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