Abstract
BackgroundThe aim of the present study was to determine whether stage of invasiveness of bladder cancer cell lines contributes to alterations in glycan pattern of their cadherins.ResultsHuman non-malignant epithelial cell of ureter HCV29, v-raf transfected HCV29 line (BC3726) and transitional cell cancers of urine bladder Hu456 and T24 were grown in cell culture. Equal amounts of protein from each cell extracts were separated by SDS-PAGE electrophoresis and were blotted on an Immobilon P membrane. Cadherins were immunodetected using anti-pan cadherin mAb and lectin blotting assays were performed, in parallel. N-oligosaccharides were analysed by specific reaction with Galanthus nivalis agglutinin (GNA), Sambucus nigra agglutinin (SNA), Maackia amurensis agglutinin (MAA), Datura stramonium agglutinin (DSA), Aleuria aurantia agglutinin (AAA), Phaseolus vulgaris agglutinin (PHA-L) and wheat germ agglutinin (WGA). The cadherin from HCV29 cell line possessed bi- and/or 2,4-branched triantennary complex type glycans, some of which were α2,6-sialylated. The cadherin from BC3726 cell line exhibited exclusively high mannose type glycans. Cadherins from Hu456 and T24 cell lines expressed high mannose type glycans as well as β1,6-branched oligosaccharides with poly-N-acetyllactosamine structures and α2,3-linked sialic acid residues. Additionally, the presence of fucose and α2,6-sialic acid residues on the cadherin from T24 cell line was detected.ConclusionsThese results indicate that N-glycosylation pattern of cadherin from bladder cancer cell line undergoes modification during carcinogenesis.
Highlights
The aim of the present study was to determine whether stage of invasiveness of bladder cancer cell lines contributes to alterations in glycan pattern of their cadherins
Manα1,2ManManα1,6ManManα1,3ManNeuAcα2,6GalNeuAcα2,3GalGalβ1,4GlcNAcFucα1,6GlcNAc-Asn Fucα1,2Galβ1,4GlcNAcGalβ1,4(Fucα1,3)GlaNAcGalβ1,4GlcNAcβ1,6(Galβ1,4GlcNAcβ1,2) ManαGlcNAcβ1,4ManNeuAαGalGlcNAcβ1,4GlcNAcoligosaccharides was ascertained in cadherins from BC3726, Hu456 and T24 cell lines as indicated by the positive reaction with Galanthus nivalis agglutinin (GNA)
The Datura stramonium agglutinin (DSA) binding to cadherin from HCV29 cell line indicated the presence of terminal disaccharide(s) Galβ1,4GlcNAc (N-acetyllactosamine unit) in biantennary complex type and/or in 2,4branched triantennary species
Summary
The aim of the present study was to determine whether stage of invasiveness of bladder cancer cell lines contributes to alterations in glycan pattern of their cadherins. Cadherins comprise a family of calcium-dependent transmembrane cell-cell adhesion molecules, generally thought to be homophilic cell adhesion proteins [1]. The homophilic binding of cadherins is regulated by extracellular and intracellular signals, which modulate cadherin activity [2] without a concomitant changes in cadherin expression. The signals that modulate cadherin activity are not completely characterized. Cadherins are glycosylated [3]. Yoshimura et al [6] have shown that the suppression of metastasis in murine melanoma B16-hm cells expressing N-acetylglucosaminyltransferase III was at least partly due to increased level of glycosylated E-cadherin. The authors imply that glycosylation is one of the important events in the process of metastasis
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