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The structure of the oligosaccharides of α3β1 integrin from human ureter epithelium (HCV29) cell line.

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Lityńska A., Pocheć E., Hoja-Łukowicz D., Kremser E., Laidler P., Amoresano A., Monti C.

2002

vol. 49

issue 2

491-500

There is a growing line of evidence that glycosylation of α and β subunits is important for the function of integrins. Integrin α3β1, from human ureter epithelium cell - line HCV29, was isolated by affinity chromatography on laminin GD6 peptide. Characterization of its carbohydrate moieties was carried out using sodium dodecyl sulfate/polyacrylamide gel electrophoresis followed by Western blotting on Immobilon P and on-blot deglycosylation with peptide N-glycosidase-F. Profiles of N-glycans for each subunit were obtained by matrix-assisted laser desorption/ionization mass spectrometry. Our findings demonstrated, in both subunits of integrin α3β1, the presence of complex type oligosaccharides with a wide heterogeneity. Bi- tri- and tetraantennary structures were the most common, while high-mannose type structures were minor. Also the presence of short poly-N-acetyllactosamine entities was shown. These results show that while the predominant oligosaccharides of both subunits are identical, some slight differences between them do exist.

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1 Acta Biochimica Polonica

1 2002

1 Amoresano A.

1 Hoja-Łukowicz D.

1 Kremser E.

1 Laidler P.

1 Lityńska A.

1 Monti C.

1 Pocheć E.

Search results

The structure of the oligosaccharides of α3β1 integrin from human ureter epithelium (HCV29) cell line.