Publications & Reports

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, Mckenzie IF, Devine PL, Riecken EO
Klinikum Steglitz, Freien Universitat Berlin, Germany.

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.

Publication

  • Journal: Cancer Research
  • Published: 01/09/1993
  • Volume: 53
  • Issue: 17
  • Pagination: 4082-4088