Interaction de la lectine de Robinia pseudo acacia et de la Concanavaline A avec les surfaces membranaires des hepatocytes normaux et tumoraux de rat

Abstract

In order to approach the structure of Robinia pseudo-acacia lectin and Concanavalin A receptor sites on the surface of normal and transformed cells, simple sugars, oligosaccharides and glycopeptides were used as inhibitors. Concanavalin A was inhibited by the simple sugars whereas lectin from Robinia was not inhibited by any monosaccharides or disaccharides. In addition, the plasma glycoproteins and glycopeptides released from urines, inhibited the action of both lectins on the growth of the two cell types, but were not more potent inhibitors than simple sugars. Interesting results were obtained with urinary glycopeptides which showed a selective inhibition depending on the kind of lectin and on the normal or transformed state of hepatocytes. Cellular glycopeptides released by proteolysis from normal and tumoral rat hepatocytes also selectively inhibited the lectin effects on cellular growth; these glycopeptides use or would act as components of receptor sites for both lectins. These results suggest that the structure of the receptor sites for both lectins on the same cell, and those for the same lectin on the normal and tumoral cells are different.