The binding of peroxidase-labelled lectins to human breast epithelium. IV--The reactivity of breast carcinomas to peanut, soy bean and Dolichos biflorus agglutinins.

The binding of the lectins from peanut, soy bean and Dolichos biflorus (specific for galactose and/or N-acetyl-D-galactosamine), to human breast carcinomas has been investigated. In contrast to the consistent pattern found in normal breast the reactivity of carcinomas to peanut lectin is varied, the most striking differences being prominent binding without desialation in some tumours and virtual lack of reactivity in others. There tends to be a greater degree of binding of soy bean agglutinin to carcinomas than normal although this is not absolute, and the reverse applies to Dolichos biflorus agglutinin. Comparison of the binding of the three lectins has revealed a complex heterogeneity of the carbohydrate chains within individual tumours and between different carcinomas. A significant relationship between peanut lectin binding, with the use of neuraminidase, and tumour differentiation as been found, and to a lesser extent with soy bean agglutinin when desialation is performed. However, the pattern of reactivity of the carcinomas with these three lectins does not appear to be related to local lymph node metastasis.