title: Comparison of receptors for cholera and Escherichia coli enterotoxins in human intestine.
abstract: Extraction of lipids from human small intestinal epithelial cells or brush borders removed specific binding sites for cholera toxin completely, but only about 50% of the receptor sites for Escherichia coli heat-labile enterotoxin. Both cholera toxin and E. coli heat-labile enterotoxin bound strongly to ganglioside GM1 in the lipid extract and, to a lesser extent, to another monosialoganglioside and to GD1b. The results suggest that E. coli heat-labile enterotoxin binds to both ganglioside and glycoprotein receptor sites of the human small intestinal epithelium, whereas cholera toxin binding was restricted to the ganglioside receptors.
mesh_terms: D002772:Cholera Toxin / Q000378:metabolism*; D004768:Enterotoxins / Q000378:metabolism; D004926:Escherichia coli / Q000276:immunology; D005732:Gangliosides / Q000378:metabolism; D006017:Glycolipids / Q000378:metabolism; D006162:Guanylate Cyclase; D006801:Humans; D007413:Intestinal Mucosa / Q000166:cytology; D007421:Intestine, Small / Q000378:metabolism*; D007457:Iodine Radioisotopes; D008055:Lipids / Q000302:isolation & purification; D008871:Microvilli / Q000166:cytology; D000074261:Receptors, Enterotoxin; D050705:Receptors, Guanylate Cyclase-Coupled; D011971:Receptors, Immunologic / Q000378:metabolism*; D018000:Receptors, Peptide
chemical_list: D004768:Enterotoxins; D005732:Gangliosides; D006017:Glycolipids; D007457:Iodine Radioisotopes; D008055:Lipids; D011971:Receptors, Immunologic; D018000:Receptors, Peptide; D002772:Cholera Toxin; D006162:Guanylate Cyclase; D000074261:Receptors, Enterotoxin; D050705:Receptors, Guanylate Cyclase-Coupled