Lectin binding to human gastric adenocarcinomas and adjacent tissues.

The binding of lectins to paraffin sections of nine gastric carcinomas and adjacent mucosa was examined by fluorescence microscopy. A battery of nine lectins was employed, and both intestinal and diffusely infiltrating tumors were tested. Wheat germ agglutinin and Ricinus communis agglutinin I appeared to bind to both mucus and nonmucus glycoproteins; these lectins labeled tumor cells, benign epithelial cells, and nonepithelial tissues strongly and consistently. Peanut agglutin, soybean agglutinin, Dolichos biflorus agglutinin, Bandeiraea simpifolica agglutinin, and Ulex europaeus agglutinin I bound extensively to mucosubstances in vacuoles and apices of benign epithelial cells but often bound to tumor cells focally and in some cases not at all. Neuraminidase digestion enhanced lectin staining in some tumors; but in others, especially those of the diffusely infiltrating type, neuraminidase digestion did not enhance the staining of tumor cells. The results suggest that the decrease in the proportion of tumor cells labeling with lectin relative to superficial epithelial cells can be due either to the oversialylation of mucoproteins or to the loss of glycosylating enzyme activity. Concanavalin A did not bind to mucosubstances in the vacuoles or apices of benign epithelium, but bound to mucus vacuoles of metaplastic epithelium and to coarse cytoplasmic granules in two of the tumors examined. This suggests either the abnormal addition of mannose to mucus glycoprotein or the production of a distinct glycoprotein by some gastric tumors.