Interleukin 1 secretion by human monocytes stimulated by the isolated polysaccharide region of the Bordetella pertussis endotoxin.
The isolated polysaccharide chain, PS-1, of the Bordetella pertussis endotoxin was examined by isoelectric focusing, SDS-polyacrylamide gel electrophoresis and gel filtration for heterogeneity and for possible contamination by the parent endotoxin. This polysaccharide, previously found to be a very potent, macrophage-dependent, polyclonal B-cell activator and to mediate the specific binding of the endotoxin to macrophages, stimulated the interleukin 1 (IL 1) secretion by human monocytes; its potency was similar to that measured for the endotoxin. It was concluded that endotoxin-induced IL 1 production may be initiated by the interaction of the polysaccharide chain of the B. pertussis endotoxin and a specific structure present on macrophages.
D000328:Adult; D000911:Antibodies, Monoclonal / Q000276:immunology; D001886:Bordetella pertussis; D002478:Cells, Cultured; D002850:Chromatography, Gel; D003165:Complement System Proteins / Q000276:immunology; D003602:Cytotoxicity, Immunologic; D004591:Electrophoresis, Polyacrylamide Gel; D004731:Endotoxins / Q000494:pharmacology*; D006801:Humans; D007375:Interleukin-1 / Q000096:biosynthesis*; D007525:Isoelectric Focusing; D009000:Monocytes / Q000187:drug effects / Q000276:immunology*; D011135:Polysaccharides, Bacterial / Q000494:pharmacology*; D013268:Stimulation, Chemical
D000911:Antibodies, Monoclonal; D004731:Endotoxins; D007375:Interleukin-1; D011135:Polysaccharides, Bacterial; D003165:Complement System Proteins