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Glycosylation of proteins in healthy and neoplastic human salivary glands – a preliminary study
-
Małgorzata Borzym-Kluczyk
,
Iwona Radziejewska
Published/Copyright:
February 3, 2011
Abstract
Background: In cancer tissue, altered glycosylation of proteins is observed. There are some typical changes; for example, sialyl-Lewisa/x glycoforms are more abundant in many types of cancers. The current study investigated the differences in glycosylation of proteins between neoplastic and healthy human salivary glands.
Methods: Sugar structures on proteins with a molecular mass above 30 kDa were determined by enzyme-linked immunosorbent assay (ELISA) with biotinylated lectins.
Results: The expression of sialic acid in cancer tissues was higher in comparison with healthy ones. The same observations were revealed for Fuc α1-6, α1-2, T, Tn antigens and α1-6 mannose.
Conclusions: Glycosylation of proteins in cancer salivary gland tissues is altered in comparison with healthy tissue.
Received: 2010-10-4
Accepted: 2010-12-8
Published Online: 2011-02-03
Published in Print: 2011-05-01
©2011 by Walter de Gruyter Berlin New York
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- Genetics and Molecular Diagnostics
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- Identification of Bcl-2/IgH fusion sequences using real-time PCR and chip-based microcapillary electrophoresis
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