The structure of the oligosaccharides of alpha3beta1 integrin from human ureter epithelium (HCV29) cell line.
Acta Biochim Pol
; 49(2): 491-500, 2002.
Article
em En
| MEDLINE
| ID: mdl-12362991
ABSTRACT
There is a growing line of evidence that glycosylation of alpha and beta subunits is important for the function of integrins. Integrin alpha3beta1, 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 alpha3beta1, 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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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Oligossacarídeos
/
Ureter
/
Integrina alfa3beta1
/
Células Epiteliais
Limite:
Humans
Idioma:
En
Revista:
Acta Biochim Pol
Ano de publicação:
2002
Tipo de documento:
Article