title: Effects of lectins and tunicamycin on IL-1 binding to YT cells.
abstract: Specific binding of iodinated-interleukin-1 alpha or beta to YT cells could be inhibited by the lectins wheat germ agglutinin (WGA) and concanavalin A (Con A). WGA and Con A inhibition of IL-1 binding was abrogated by previous exposure of these plant proteins to the lectin-specific sugars N-acetylglucosamine (GlcNAc) and methyl glucoside (MG), respectively. Tunicamycin, an inhibitor of glycosylation, decreased interleukin-1 (IL-1) binding to YT cells, but also reduced total protein synthesis. These observations suggest that carbohydrate moieties on or near the interleukin-1 receptor may be important for optimal receptor binding of IL-1 to intact YT cells.
authors: Hypersensitivity Diseases Research, Upjohn Company, Kalamazoo, MI 49001.
authors: S C
authors: SC
authors: Speziale
authors: L C
authors: LC
authors: Ginsberg
authors: J W
authors: JW
authors: Paslay
mesh_terms: D000117:Acetylglucosamine / Q000494:pharmacology; D001667:Binding, Competitive / Q000187:drug effects; D002460:Cell Line; D003208:Concanavalin A / Q000494:pharmacology*; D006801:Humans; D007375:Interleukin-1 / Q000378:metabolism*; D008757:Methylglucosides / Q000494:pharmacology; D014176:Protein Biosynthesis; D011994:Recombinant Proteins / Q000378:metabolism; D014415:Tunicamycin / Q000494:pharmacology*; D014909:Wheat Germ Agglutinins / Q000494:pharmacology*
chemical_list: D007375:Interleukin-1; D008757:Methylglucosides; D011994:Recombinant Proteins; D014909:Wheat Germ Agglutinins; D003208:Concanavalin A; D014415:Tunicamycin; D000117:Acetylglucosamine