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

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.

• Authors: Małgorzata Borzym-Kluczyk, Iwona Radziejewska, Marzanna Cechowska-Pasko
• Journal: Clinical chemistry and laboratory medicine (Clin Chem Lab Med) Vol. 49 Issue 5 Pg. 885-9 (May 2011) ISSN: 1437-4331 [Electronic] Germany
• PMID: 21288176 (Publication Type: Journal Article)

Chemical References

• Plant Lectins
• Salivary Proteins and Peptides

Topics

• Adult
• Aged
• Enzyme-Linked Immunosorbent Assay (methods)
• Female
• Glycosylation
• Humans
• Male
• Middle Aged
• Molecular Weight
• Plant Lectins (metabolism)
• Salivary Gland Neoplasms (metabolism, pathology)
• Salivary Glands (cytology, metabolism, pathology)
• Salivary Proteins and Peptides (chemistry, metabolism)