Altered glycosylation of membrane glycoproteins in human uroepithelial cell lines.
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, noninvasive (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.
D002460:Cell Line; D002471:Cell Transformation, Neoplastic / Q000378:metabolism*; D002846:Chromatography, Affinity; D006020:Glycopeptides / Q000032:analysis; D006023:Glycoproteins / Q000378:metabolism*; D006801:Humans; D037102:Lectins; D008565:Membrane Proteins / Q000378:metabolism*; D010641:Phenotype; D011134:Polysaccharides / Q000032:analysis; D014513:Ureter / Q000032:analysis; D001743:Urinary Bladder / Q000032:analysis; D001749:Urinary Bladder Neoplasms / Q000032:analysis
D006020:Glycopeptides; D006023:Glycoproteins; D037102:Lectins; D008565:Membrane Proteins; D011134:Polysaccharides