BIOMAT Database Logo BIOMAT Database Logo

Binding of vasoactive intestinal peptide and its stimulation of adenylate cyclase through two classes of receptors in rat liver membranes. Effects of 12 secretin analogues and 2 secretin fragments. 1981

M Waelbroeck, and P Robberecht, and P De Neef, and P Chatelain, and J Christophe

1. Vasoactive intestinal peptide (VIP) receptors were identified in crude rat hepatic membranes by 125I-labelled VIP binding and by the ability of VIP to stimulate adenylate cyclase activity. The specificity of these receptors was evaluated by the capacity of secretin, synthetic secretin analogues, and secretin fragments to inhibit 125I-labelled VIP binding and to stimulate adenylate cyclase. 2. The results were compatible with the existence of two classes of VIP binding sites that could be distinguished according to their affinity for VIP and their specificity. High-affinity sites were more specific for VIP as secretin was 175 times less potent than VIP for recognition of these sites while being only 33 times less potent than VIP for recognition of low-affinity sites. 3. Secretin analogues, monosubstituted in position 2, 3, 4 or 6 were less potent than secretin for adenylate cyclase stimulation as well as for the recognition of the two classes of receptors. [Val5]secretin was more potent than secretin and appeared definitely more VIP-like than secretin; [Ala4, Val5] and [D-Ala4,Val5]secretin were equipotent to secretin. 4. The fragment secretin (7-27) was unable to recognize VIP receptors and to stimulate adenylate cyclase. The substituted fragment [Gln9,Asn15]secretin (5-27) recognized these receptors with weak potency but could not activate the enzyme.

UI MeSH Term Description Entries
D008099 Liver A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances. Livers
D008566 Membranes Thin layers of tissue which cover parts of the body, separate adjacent cavities, or connect adjacent structures. Membrane Tissue,Membrane,Membrane Tissues,Tissue, Membrane,Tissues, Membrane
D010446 Peptide Fragments Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques. Peptide Fragment,Fragment, Peptide,Fragments, Peptide
D011485 Protein Binding The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. Plasma Protein Binding Capacity,Binding, Protein
D011919 Rats, Inbred Strains Genetically identical individuals developed from brother and sister matings which have been carried out for twenty or more generations or by parent x offspring matings carried out with certain restrictions. This also includes animals with a long history of closed colony breeding. August Rats,Inbred Rat Strains,Inbred Strain of Rat,Inbred Strain of Rats,Inbred Strains of Rats,Rat, Inbred Strain,August Rat,Inbred Rat Strain,Inbred Strain Rat,Inbred Strain Rats,Inbred Strains Rat,Inbred Strains Rats,Rat Inbred Strain,Rat Inbred Strains,Rat Strain, Inbred,Rat Strains, Inbred,Rat, August,Rat, Inbred Strains,Rats Inbred Strain,Rats Inbred Strains,Rats, August,Rats, Inbred Strain,Strain Rat, Inbred,Strain Rats, Inbred,Strain, Inbred Rat,Strains, Inbred Rat
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
D004789 Enzyme Activation Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme. Activation, Enzyme,Activations, Enzyme,Enzyme Activations
D005768 Gastrointestinal Hormones HORMONES secreted by the gastrointestinal mucosa that affect the timing or the quality of secretion of digestive enzymes, and regulate the motor activity of the digestive system organs. Enteric Hormone,Enteric Hormones,Gastrointestinal Hormone,Intestinal Hormone,Intestinal Hormones,Hormone, Enteric,Hormone, Gastrointestinal,Hormone, Intestinal,Hormones, Enteric,Hormones, Gastrointestinal,Hormones, Intestinal
D000262 Adenylyl Cyclases Enzymes of the lyase class that catalyze the formation of CYCLIC AMP and pyrophosphate from ATP. Adenyl Cyclase,Adenylate Cyclase,3',5'-cyclic AMP Synthetase,Adenylyl Cyclase,3',5' cyclic AMP Synthetase,AMP Synthetase, 3',5'-cyclic,Cyclase, Adenyl,Cyclase, Adenylate,Cyclase, Adenylyl,Cyclases, Adenylyl,Synthetase, 3',5'-cyclic AMP
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia

Related Publications

M Waelbroeck, and P Robberecht, and P De Neef, and P Chatelain, and J Christophe
Effects of vasoactive intestinal peptide, secretin, and related peptides on rat colonic transport and adenylate cyclase activity.
September 1977, Gastroenterology,
M Waelbroeck, and P Robberecht, and P De Neef, and P Chatelain, and J Christophe
Characterization of a vasoactive intestinal peptide-sensitive adenylate cyclase in rat intestinal epithelial cell membranes.
December 1978, Biochimica et biophysica acta,
M Waelbroeck, and P Robberecht, and P De Neef, and P Chatelain, and J Christophe
Stimulation of retinal adenylate cyclase by vasoactive intestinal peptide (VIP).
March 1981, European journal of pharmacology,
M Waelbroeck, and P Robberecht, and P De Neef, and P Chatelain, and J Christophe
Vasoactive intestinal peptide and intraocular pressure: adenylate cyclase activation and binding sites for vasoactive intestinal peptide in membranes of ocular ciliary processes.
April 1987, The Journal of pharmacology and experimental therapeutics,
M Waelbroeck, and P Robberecht, and P De Neef, and P Chatelain, and J Christophe
Vasoactive intestinal polypeptide and glucagon: stimulation of adenylate cyclase activity via distinct receptors in liver and fat cell membranes.
August 1973, Biochemical and biophysical research communications,
M Waelbroeck, and P Robberecht, and P De Neef, and P Chatelain, and J Christophe
Vasoactive intestinal peptide stimulation of human renal adenylate cyclase in vitro.
April 1990, The Journal of physiology,
M Waelbroeck, and P Robberecht, and P De Neef, and P Chatelain, and J Christophe
Effect of secretin, glucagon and vasoactive intestinal peptide on the hormone-sensitive rat cardiac adenylate cyclase [proceedings].
October 1979, Archives internationales de physiologie et de biochimie,
M Waelbroeck, and P Robberecht, and P De Neef, and P Chatelain, and J Christophe
Interactions of glucagon, gut glucagon, vasoactive intestinal polypeptide and secretin with liver and fat cell plasma membranes: binding to specific sites and stimulation of adenylate cyclase.
September 1974, Endocrinology,
M Waelbroeck, and P Robberecht, and P De Neef, and P Chatelain, and J Christophe
[Receptors for vasoactic intestinal peptide (VIP) in human colonic adenocarcinoma membranes: specific binding and stimulation of adenylate cyclase].
January 1978, Comptes rendus hebdomadaires des seances de l'Academie des sciences. Serie D: Sciences naturelles,
M Waelbroeck, and P Robberecht, and P De Neef, and P Chatelain, and J Christophe
Secretin binding sites coupled with adenylate cyclase in rat fundic membranes.
January 1981, Peptides,
Copied contents to your clipboard!