Glycosylation of proteins in healthy and neoplastic human salivary glands – a preliminary study

Małgorzata Borzym-Kluczyk; Iwona Radziejewska; Marzanna Cechowska-Pasko

doi:10.1515/CCLM.2011.137

Published by De Gruyter February 3, 2011

Glycosylation of proteins in healthy and neoplastic human salivary glands – a preliminary study

Małgorzata Borzym-Kluczyk , Iwona Radziejewska and Marzanna Cechowska-Pasko

From the journal Clinical Chemistry and Laboratory Medicine

https://doi.org/10.1515/CCLM.2011.137

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Abstract

Background: In cancer tissue, altered glycosylation of proteins is observed. There are some typical changes; for example, sialyl-Lewis^a/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.

Keywords: biotinylated lectins; ELISA; glycosylation; salivary gland

Corresponding author: Małgorzata Borzym-Kluczyk, PhD, Department of Pharmaceutical Biochemistry, Medical University, Mickiewicza 2A, 15-230 Białystok, Poland Phone: +48 0857 485689

Received: 2010-10-4

Accepted: 2010-12-8

Published Online: 2011-02-03

Published in Print: 2011-05-01

Glycosylation of proteins in healthy and neoplastic human salivary glands – a preliminary study

Abstract

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