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Glycobiology, 1999, Vol. 9, No. 12 1307-1311
© 1999 Oxford University Press

An {alpha}2,3sialyltransferase (ST3Gal I) is elevated in primary breast carcinomas

Joy Burchella, Richard Poulsom4, Andrew Hanby3, Caroline Whitehouseb, Lucienne Cooper, Henrik Clausen5, David Miles and Joyce Taylor-Papadimitriou

Imperial Cancer Research Fund Breast Cancer Biology Groupand 3Hedley Atkins/ICRFBreast Pathology, Guy’s Hospital, London SE1 9RT, UK, 4In situ HybridizationService and Histopathology Unit, Imperial Cancer Research Fund,44 Lincoln’s Inn Fields, London WC2A 3PX, UK, 5Department of Oral Diagnostics,School of Dentistry, University of Copenhagen, DK2200 Copenhagen,Denmark

The MUC1 mucin is expressed on the luminal surfaceof most simple epithelial cells but in carcinomas, especially thoseof the breast and ovary, MUC1 is upregulated and aberrantly glycosylated.MUC1 contains a large amount of O-linked glycans which, in the mucinexpressed by normal mammary epithelial cells, consist mainly ofcore 2 based structures carrying polylactosamine chains. However,the mucin expressed by breast carcinomas has shorter side-chains, oftenconsisting of sialylated core 1 (Galß1–3GalNAc). in situ hybridization of primary breasttissue showed that a sialyltransferase (ST3Gal I), responsible foradding sialic acid to core 1 thereby terminating chain extension,is elevated in primary breast carcinomas when compared to normalor benign tissue. Furthermore, the level of mRNA expression encodingST3Gal I is correlated to the intensity of staining seen with theantibody SM3, which specifically recognises underglycosylated, tumourassociated MUC1. Thus, the aberrant glycosylation of MUC1 seen inbreast carcinomas appears to be due, at least in part, to the elevationof ST3Gal I.

a Correspondenceto: Dr Joy Burchell, ICRF Breast Cancer Biology Group, 3rd Floor,Thomas Guy House, Guy’s Hospital, London SE1 9RT, UK

b Presentaddress: Cancer Genetics Laboratory, 8th Floor, Guy’s Tower, Guy’s Hospital, London SE1 9RT, UK


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