Differences of alpha(3)beta(1) integrin glycans from different human bladder cell lines

Expression as well as properties of integrins are altered upon transformati on. Cell adhesion regulated by integrins is modulated by glycosylation, one of the most frequent biochemical alteration associated with tumorogenesis. Characterisation of carbohydrate moieties of alpha(3)beta(1) integrin on t he cultured human bladder carcinoma (T-24, Hu456, HCV 29T) and human normal meter and bladder epithelium (HCV29, Hu609) cell lines was carried out aft er an electrophoresis and blotting, followed by immunochemical identificati on of alpha(3) and beta(1) integrin chains and analysis of their carbohydra tes moieties using highly specific digoxigenin-labelled lectins. In all the studied cell lines alpha(3)beta(1) integrin was glycosylated although in g eneral each subunit differently. Basic structures recognized in beta(1) sub unit were tri- or tetraantennary complex type glycans in some cases sialyla ted (T-24, HCV 29, HCV 29T) and fucosylated (Hu609, HCV 29T). Positive reac tion with Phaseolus vulgaris agglutinin and Datura stramonium agglutinin su ggesting the presence of beta 1-6 branched N-linked oligosaccharides was fo und in cancerous cell lines (T-24, Hu456) as well as in normal bladder epit helium cells (Hu609). High mannose type glycan was found only in beta(1) su bmit from Hu456 transitional cell cancer line. On the other hand as submit was much less glycosylated except the invasive cancer cell line T-24 where high mannose as well as sialylated tri- or tetraantennary complex type glyc ans were detected. This observation suggests that changes in glycosylation profile attributed to invasive phenotype are rather associated with as not beta(1) subunit.