Comparison of receptors for cholera and Escherichia coli enterotoxins in human intestine.
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.
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
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