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

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. and Drechsler, K. and Hanisch, F.G. and Sheehan, J. and Manske, M. and Ogorek, D. and Klussmann, E. and Hanski, M.L. and Blank, M. and Xing, P.X. and McKenzie, I.F.C. and 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 (U.S.A.)
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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