Open AccessDual Function of Macrophage Galactose/N‐Acetylgalactosamine‐specific Lectins: Glycoprotein Uptake and Tumoricidal Cellular Recognition
Author(s) -
Kawakami Kyoko,
Yamamoto Kazuo,
Toyoshima Satoshi,
Osawa Toshiaki,
Irimura Tatsuro
Publication year - 1994
Publication title -
japanese journal of cancer research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.035
H-Index - 141
eISSN - 1349-7006
pISSN - 0910-5050
DOI - 10.1111/j.1349-7006.1994.tb02423.x
Subject(s) - lectin , internalization , recombinant dna , macrophage , glycoprotein , biochemistry , in vitro , chemistry , bovine serum albumin , biology , receptor , gene
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.