Dual function of macrophage galactose/N-acetylgalactosamine-specific lectins: glycoprotein uptake and tumoricidal cellular recognition.

We investigated whether the interaction of peritoneal macrophages with extracellular ligands is mediated by C-type lectins specific for galactose and N-acetylgalactosamine. The carbohydrate-binding domain of mouse galactose/N-acetylgalactosamine-specific lectin was prepared in a recombinant form. The purified recombinant lectins were tested for competitive inhibition against glycoprotein uptake and against tumoricidal effect. Thioglycolate-elicited macrophages internalized galactosylated bovine serum albumin in vitro. The internalization was blocked by recombinant macrophage lectins. Activated macrophages obtained after intraperitoneal injection of a nonspecific immune potentiator, OK432, did not internalize galactosylated bovine serum albumin. These cells elicited a cytotoxic effect against P815 murine mastocytoma cells, and the effect was blocked by recombinant macrophage lectins. These results indicated that galactose/N-acetylgalactosamine-specific C-type lectins expressed on the surface of inflammatory macrophages and on activated tumoricidal macrophages mediate two distinct functions, i.e. glycoprotein uptake and tumoricidal effector mechanisms.