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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.

Hanski C, Drechsler K, Hanisch FG, Sheehan J, Manske M, Ogorek D, Klussmann E, Hanski ML, Blank M, Xing PX

  • Journal Cancer research

  • Published 24 Sep 1993

  • Volume 53

  • ISSUE 17

  • Pagination 4082-8

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.