Mobility of cholera toxin receptors on rat lymphocyte membranes.
Fluorescein-labeled cholera toxin binds detectably to 40-60% of rat mesenteric lymph node cells and induces a temperature-dependent redistribution (patch and cap formation) of cell surface toxin receptors. The redistribution is inhibited by several "metabolic," "microtubule," and "microfilament" inhibitors, by concanavalin A, and by anticholera toxin IgG. Various studies indicate that cholera toxin is at least bivalent, and that this property may be related to both the induction of receptor redistribution and to the activation of adenylate cyclase. Membrane components which are probably identical to the sialo-glycolipid, GM1 ganglioside, appear to be mobile in the plane of the membrane. The possible role of toxin multivalency and receptor mobility in the mechanism of toxin action is considered.
D000262:Adenylyl Cyclases / Q000378:metabolism; D000818:Animals; D000937:Antigen-Antibody Reactions; D001665:Binding Sites; D001667:Binding, Competitive; D002462:Cell Membrane / Q000187:drug effects / Q000378:metabolism / Q000648:ultrastructure; D004768:Enterotoxins / Q000378:metabolism* / Q000494:pharmacology; D005732:Gangliosides; D008214:Lymphocytes / Q000187:drug effects / Q000378:metabolism* / Q000648:ultrastructure; D008856:Microscopy, Fluorescence; D011485:Protein Binding; D051381:Rats; D011955:Receptors, Drug; D012685:Sepharose; D014734:Vibrio cholerae / Q000276:immunology
D004768:Enterotoxins; D005732:Gangliosides; D011955:Receptors, Drug; D012685:Sepharose; D000262:Adenylyl Cyclases