The structure of the oligosaccharides of alpha3beta1 integrin from human ureter epithelium [HCV29] cell line

• Autorzy: Litynska A. , Pochec E. , Hoja-Lukowicz D. , Kremser E. , Laidler P. , Amoresano A. , Monti C.
• Języki publikacji: EN

Abstrakty

EN

There is a growing line of evidence that glycosylation of a and β subunits is impor­tant for the function of integrins. Integrin a3β1, 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 sul- fate/polyacrylamide gel electrophoresis followed by Western blotting on Immobilon P and on-blot deglycosylation with peptide .-glycosidase-F. Profiles of N-glycans for each subunit were obtained by matrix-assisted laser desorption/ionization mass spec- trometry. Our findings demonstrated, in both subunits of integrin a3β1, the presence of complex type oligosaccharides with a wide heterogeneity. Bi- tri- and tetra- antennary structures were the most common, while high-mannose type structures were minor. Also the presence of short poly-. -acetyllactosamine entities was shown. These results show that while the predominant oligosaccharides of both subunits are identical, some slight differences between them do exist.

Słowa kluczowe

EN

cell proliferation; adhesive interaction; cell line; migration; cell; man; extracellular matrix; glycosylation; oligosaccharide; protein; epithelium; differentiation

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2002
• Tom: 49
• Numer: 2
• Opis fizyczny: p.491-500,fig.

Twórcy

autor

Litynska A.

• Jagiellonian University, R.Ingardena 6, 30-060 Krakow, Poland

autor

Pochec E.

autor

Hoja-Lukowicz D.

autor

Kremser E.

autor

Laidler P.

autor

Amoresano A.

autor

Monti C.

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