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Differences of α3β1 integrin glycans from different human bladder cell lines.

100%

Lityńska A., Przybyło M., Książek D., Laidler P.

2000

vol. 47

issue 2

427-434

Expression as well as properties of integrins are altered upon transformation. Cell adhesion regulated by integrins is modulated by glycosylation, one of the most frequent biochemical alteration associated with tumorogenesis. Characterisation of carbohydrate moieties of α3β1 integrin on the cultured human bladder carcinoma (T-24, Hu456, HCV 29T) and human normal ureter and bladder epithelium (HCV 29, Hu609) cell lines was carried out after an electrophoresis and blotting, followed by immunochemical identification of α3 and β1 integrin chains and analysis of their carbohydrates moieties using highly specific digoxigenin-labelled lectins. In all the studied cell lines α3β1 integrin was glycosylated although in general each subunit differently. Basic structures recognized in β1 subunit were tri- or tetraantennary complex type glycans in some cases sialylated (T-24, HCV 29, HCV 29T) and fucosylated (Hu609, HCV 29T). Positive reaction with Phaseolus vulgaris agglutinin and Datura stramonium agglutinin suggesting the presence of β1-6 branched N-linked oligosaccharides was found in cancerous cell lines (T-24, Hu456) as well as in normal bladder epithelium cells (Hu609). High mannose type glycan was found only in β1 subunit from Hu456 transitional cell cancer line. On the other hand α3 subunit was much less glycosylated except the invasive cancer cell line T-24 where high mannose as well as sialylated tri- or tetraantennary complex type glycans were detected. This observation suggests that changes in glycosylation profile attributed to invasive phenotype are rather associated with α3 not β1 subunit.

Expression of β1-integrins and N-cadherin in bladder cancer and melanoma cell lines.

76%

Laidler P., Gil D., Pituch-Noworolska A., Ciołczyk D., Książek D., Przybyło M., Lityńska A.

2000

vol. 47

issue 4

1159-1170

Changes in the expression of integrins and cadherins might contribute to the progression, invasion and metastasis of transitional cell cancer of the bladder and of melanomas. The expression of α5 (P < 0.001), α2 and β1 (P < 0.05 - P < 0.001) integrin subunits in melanoma cells from noncutaneous metastatic sites (WM9, A375) were significantly increased as compared to cutaneous primary tumor (WM35) and metastatic (WM239) cell lines. These differences might be ascribed to the invasive character of melanoma cells and their metastasis to the noncutaneous locations. The significantly heterogeneous expression of β1 integrin subunit in two malignant bladder cancer cell lines (T24 and Hu456) and nonsignificant differences in the expression of α2, α3, and α5 subunits between malignant and non-malignant human bladder cell lines do not allow an unanimous conclusion on the role of these intergrin subunits in the progression of transitional cancer of bladder. The adhesion molecule, expressed in all studied melanoma and bladder cell lines, that reacted with anti-Pan cadherin monoclonal antibodies was identified as N-cadherin except in the HCV29 non-malignant ureter cell line. However, neither this nor any other bladder or melanoma cell line expressed E-cadherin. The obtained results imply that the replacement of E-cadherin by N-cadherin accompanied by a simultaneous increase in expression of a2, a3 and a5 integrin subunits clearly indicates an increase of invasiveness of melanoma and, to a lesser extent, of transitional cell cancer of bladder. High expression of N-cadherin and a5 integrin subunit seems to be associated with the most invasive melanoma phenotype.

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2 Acta Biochimica Polonica

2 2000

2 Książek D.

2 Laidler P.

2 Lityńska A.

2 Przybyło M.

1 Ciołczyk D.

1 Gil D.

1 Pituch-Noworolska A.

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Differences of α3β1 integrin glycans from different human bladder cell lines.

Expression of β1-integrins and N-cadherin in bladder cancer and melanoma cell lines.