PEANUT LECTIN-BINDING SITES IN LARGE BOWEL CARCINOMA

  • 1 January 1982
    • journal article
    • research article
    • Vol. 47  (4) , 383-390
Abstract
Peanut lectin binds to B-D-Gal-(1 .fwdarw. 3)-D-GalNac which provides antigenic determination for the T (TAg) blood group antigen. Human rectosigmoid carcinomas (33) and 15 corresponding controls for their ability to express peanut lectin-binding sites. In controls TAg was localized to the supranuclear portion of the cell. In cancers a cytostructural relocalization of TAg with the following 2 major patterns was noticed: localization to the region of the glycocalyx and localization intracytoplasmically in the apical portion of the cell. These 2 patterns were associated with glandular differentiation. Less frequently noted or in association with the above was a mucin glob-like pattern and/or a fine diffuse granular intracytoplasmic pattern associated with solid, nonglandular areas. The more poorly differentiated cancers less frequently expressed peanut lectin-binding sites. Benign (nontransitional zone) epithelium in those patients whose tumor expressed TAg was negative for peanut lectin-binding sites in 66% of the cases. Reduced tumoral glycosyltransferases may explain this increased synthesis of TAg in cancers compared with controls, if TAg is considered an incomplete glycoprotein of the MN blood group system.

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