N-acetylgalactosamine, N-acetylglucosamine and sialic acid expression in primary breast cancers.
Binding of the lectin from Helix pomatia (HPA), which recognises N-acetylgalactosamine and N-acetylglucosamine glycans, is a predictor of metastasis and poor prognosis in a number of human adenocarcinomas, including breast cancer. The glycoproteins to which it binds in these tumours have been only partially characterised, and the mechanisms underlying their biosynthesis remain unknown. In this study, 111 primary breast cancers were assessed for binding of HPA and labelling characteristics were compared directly with those of Dolichos biflorus agglutinin and soybean agglutinin, both of which also recognise N-acetylgalactosamine, Griffonia simplicifolia agglutinin II, which recognises N-acetylglucosamine, and Limax flavus agglutinin, Sambucus nigra agglutinin and Maackia amurensis lectin I, all of which recognise sialic acids. Results indicate that the HPA-binding partners expressed by cancer cells are predominantly N-acetylgalactosamine glycans, but some recognition of N-acetylglucosamine species is also likely. There was no evidence to support the hypothesis that overexpression of these moieties results from failure in sialylation. Alternative mechanisms, for example alterations in levels of activity of appropriate glycosyl transferases or disruption in transport and processing mechanisms leading to failure of normal chain extension of glycans may be responsible, and these are areas that warrant further investigation.
Brooks
S A
SA
Research School of Biological and Molecular Sciences, Oxford Brookes University, Headington, UK. sbrooks@brookes.ac.uk
Carter
T M
TM
D000116:Acetylgalactosamine / Q000032:analysis* / Q000502:physiology; D000117:Acetylglucosamine / Q000032:analysis* / Q000502:physiology; D000373:Agglutinins / Q000032:analysis; D001943:Breast Neoplasms / Q000737:chemistry* / Q000503:physiopathology; D005260:Female; D006031:Glycosylation; D006651:Histocytochemistry; D006801:Humans; D037102:Lectins / Q000032:analysis*; D019158:N-Acetylneuraminic Acid / Q000032:analysis* / Q000502:physiology; D037121:Plant Lectins; D054788:Ribosome Inactivating Proteins; D030262:Soybean Proteins; D013194:Staining and Labeling; D010835:Phytohemagglutinins
D000116:Acetylgalactosamine; D000117:Acetylglucosamine; D000373:Agglutinins; D037102:Lectins; D019158:N-Acetylneuraminic Acid; D037121:Plant Lectins; D054788:Ribosome Inactivating Proteins; D030262:Soybean Proteins; C038095:Helix lectin; C050600:Sambucus nigra lectins; C028824:soybean lectin; D010835:Phytohemagglutinins