Binding patterns of 51 monoclonal antibodies to peptide and carbohydrate epitopes of the epithelial mucin (MUC1) on tissue sections of adenolymphomas of the parotid (Warthin's tumours): role of epitope masking by glycans.

Warthin's tumours provide a unique opportunity to distinguish and compare monoclonal antibodies (mAbs) to the epithelial mucin, MUC1. In this study, we have applied the range of anti-MUC1 antibodies submitted to the ISOBM TD-4 Workshop for this purpose. mAbs and lectins against MUC1-associated carbohydrate epitopes were also included. Among 39 mAbs to peptide epitopes of MUC1, eight distinct types of staining patterns towards the two epithelial cell layers of Warthin's tumours could be observed. A majority of 27 mAbs reacted preferentially (17) or exclusively (10) with columnar cells, whereas 10 mAbs favoured basal cells (1 of them almost exclusively). The observed staining patterns revealed no correlation with the epitopes. However, after carbohydrate-specific periodate oxidation, 33 of the mAbs stained columnar and basal cells equally well, indicating that epitope masking by glycan side chains was in most cases responsible for the different staining patterns. The results demonstrate the profound impact of glycosylation on immunohistochemistry. Among carbohydrate epitopes, sialyl-TF, sialyl-Le(x), sialyl-dimeric Le(x) and Tn were expressed on both columnar and basal cells (the s-TF3 isomer on columnar cells only). The carcinoma-associated Thomsen-Friedenreich epitope was absent.