Biomaterial Database

Receptors for cholera toxin and Escherichia coli heat-labile enterotoxin revisited. 1994

J Holmgren

Department of Medical Microbiology and Immunology, University of Göteborg, Sweden.

UI	MeSH Term	Description	Entries
D008969	Molecular Sequence Data	Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.	Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D011956	Receptors, Cell Surface	Cell surface proteins that bind signalling molecules external to the cell with high affinity and convert this extracellular event into one or more intracellular signals that alter the behavior of the target cell (From Alberts, Molecular Biology of the Cell, 2nd ed, pp693-5). Cell surface receptors, unlike enzymes, do not chemically alter their ligands.	Cell Surface Receptor,Cell Surface Receptors,Hormone Receptors, Cell Surface,Receptors, Endogenous Substances,Cell Surface Hormone Receptors,Endogenous Substances Receptors,Receptor, Cell Surface,Surface Receptor, Cell
D002240	Carbohydrate Sequence	The sequence of carbohydrates within POLYSACCHARIDES; GLYCOPROTEINS; and GLYCOLIPIDS.	Carbohydrate Sequences,Sequence, Carbohydrate,Sequences, Carbohydrate
D002772	Cholera Toxin	An ENTEROTOXIN from VIBRIO CHOLERAE. It consists of two major protomers, the heavy (H) or A subunit and the B protomer which consists of 5 light (L) or B subunits. The catalytic A subunit is proteolytically cleaved into fragments A1 and A2. The A1 fragment is a MONO(ADP-RIBOSE) TRANSFERASE. The B protomer binds cholera toxin to intestinal epithelial cells and facilitates the uptake of the A1 fragment. The A1 catalyzed transfer of ADP-RIBOSE to the alpha subunits of heterotrimeric G PROTEINS activates the production of CYCLIC AMP. Increased levels of cyclic AMP are thought to modulate release of fluid and electrolytes from intestinal crypt cells.	Cholera Toxin A,Cholera Toxin B,Cholera Toxin Protomer A,Cholera Toxin Protomer B,Cholera Toxin Subunit A,Cholera Toxin Subunit B,Choleragen,Choleragenoid,Cholera Enterotoxin CT,Cholera Exotoxin,Cholera Toxin A Subunit,Cholera Toxin B Subunit,Procholeragenoid,Enterotoxin CT, Cholera,Exotoxin, Cholera,Toxin A, Cholera,Toxin B, Cholera,Toxin, Cholera
D004768	Enterotoxins	Substances that are toxic to the intestinal tract causing vomiting, diarrhea, etc.; most common enterotoxins are produced by bacteria.	Staphylococcal Enterotoxin,Enterotoxin,Staphylococcal Enterotoxins,Enterotoxin, Staphylococcal,Enterotoxins, Staphylococcal
D005677	G(M1) Ganglioside	A specific monosialoganglioside that accumulates abnormally within the nervous system due to a deficiency of GM1-b-galactosidase, resulting in GM1 gangliosidosis.	GM1 Ganglioside,Monosialosyl Tetraglycosyl Ceramide,GM1a Monosialoganglioside,Ceramide, Monosialosyl Tetraglycosyl,Ganglioside, GM1,Monosialoganglioside, GM1a,Tetraglycosyl Ceramide, Monosialosyl
D006162	Guanylate Cyclase	An enzyme that catalyzes the conversion of GTP to 3',5'-cyclic GMP and pyrophosphate. It also acts on ITP and dGTP. (From Enzyme Nomenclature, 1992) EC 4.6.1.2.	Guanyl Cyclase,Deoxyguanylate Cyclase,Guanylyl Cyclase,Inosinate Cyclase,Cyclase, Deoxyguanylate,Cyclase, Guanyl,Cyclase, Guanylate,Cyclase, Guanylyl,Cyclase, Inosinate
D006358	Hot Temperature	Presence of warmth or heat or a temperature notably higher than an accustomed norm.	Heat,Hot Temperatures,Temperature, Hot,Temperatures, Hot
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000074261	Receptors, Enterotoxin	Guanylate cyclase-coupled receptors that bind bacterial ENTEROTOXINS, as well as the endogenous peptides guanylin and uroguanylin. Ligand binding stimulates production of CYCLIC GMP by EPITHELIAL CELLS of the intestinal lumen, altering barrier permeability and mucus secretion. Mutations in the gene (GUCY2C) encoding this receptor are associated with some cases of hereditary diarrhea (Diarrhea 6) and MECONIUM ILEUS.	Enterotoxin Receptor,Enterotoxin Receptors,Enterotoxin-Guanylin Receptor,Enterotoxin-Guanylin Receptors,GC-C Receptor,GC-C Receptors,Guanyl Cyclase-C Receptor,Guanyl Cyclase-C Receptors,Guanylin-Uroguanylin Receptor,Guanylin-Uroguanylin Receptors,Guanylyl Cyclase C,Heat-Stable Enterotoxin Receptor,Heat-Stable Enterotoxin Receptors,Receptor, Enterotoxin,Receptor, Guanyl Cyclase-C,Receptors, Guanyl Cyclase-C,Cyclase C, Guanylyl,Cyclase-C Receptors, Guanyl,Enterotoxin Guanylin Receptor,Enterotoxin Guanylin Receptors,Enterotoxin Receptor, Heat-Stable,Enterotoxin Receptors, Heat-Stable,GC C Receptor,GC C Receptors,Guanyl Cyclase C Receptor,Guanyl Cyclase C Receptors,Guanylin Uroguanylin Receptor,Guanylin Uroguanylin Receptors,Heat Stable Enterotoxin Receptor,Heat Stable Enterotoxin Receptors,Receptor, Enterotoxin-Guanylin,Receptor, GC-C,Receptor, Guanyl Cyclase C,Receptor, Guanylin-Uroguanylin,Receptor, Heat-Stable Enterotoxin,Receptors, Enterotoxin-Guanylin,Receptors, GC-C,Receptors, Guanyl Cyclase C,Receptors, Guanylin-Uroguanylin,Receptors, Heat-Stable Enterotoxin