Altered glycosylation of the MUC-1 protein core contributes to the colon carcinoma-associated increase of mucin-bound sialyl-Lewis(x) expression

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Item Type:	Article
Title:	Altered glycosylation of the MUC-1 protein core contributes to the colon carcinoma-associated increase of mucin-bound sialyl-Lewis(x) expression
Creators Name:	Hanski, C., Drechsler, K., Hanisch, F.G., Sheehan, J., Manske, M., Ogorek, D., Klussmann, E., Hanski, M.L., Blank, M., Xing, P.X., McKenzie, I.F.C., Devine, P.L. and Riecken, E.O.
Abstract:	The mucin carbohydrate epitope sialyl-Le(x), detected with the monoclonal antibody AM-3, is strongly overexpressed in > 90% of human colon carcinomas. We show here that in colon carcinoma one of the mucin cores bearing the sialyl-Le(x) group is MUC-1, whereas sialyl-Le(x) present in normal colon is not detectable on MUC-1. The amounts of MUC-1 core detectable with the monoclonal antibody BC3 in extracts of tumor tissue are 60-180% of those in normal tissue. Two other carbohydrate epitopes located on MUC-1 in mucins from normal and tumor tissue have also been characterized. In contrast to sialyl-Le(x), their expression on MUC-1 is variable and does not correlate with the malignant transformation of colonic mucosa. The transfer of the sialyl-Le(x) group onto the MUC-1 core contributes to the colon carcinoma-associated overexpression of the sialyl-Le(x) epitope.
Keywords:	Antigens, Carcinoma, Colon, Colonic Neoplasms, Enzyme-Linked Immunosorbent Assay, Epitopes, Glycosylation, Mucins
Source:	Cancer Research
ISSN:	0008-5472
Publisher:	American Association for Cancer Research
Volume:	53
Number:	17
Page Range:	4082-4088
Date:	1 September 1993
Official Publication:	http://cancerres.aacrjournals.org/content/53/17/4082.abstract
PubMed:	View item in PubMed

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