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
| Autor: | Patrick Robberecht, Jean Christophie, Pierre Chatelain, Philippe De Neef, Magali Waelbroeck |
|---|---|
| Rok vydání: | 1981 |
| Předmět: |
medicine.medical_specialty
Vasoactive intestinal peptide Biophysics Receptors Cell Surface -- metabolism Secretin receptor family Receptors Cell Surface Stimulation Secretin family Membranes -- metabolism digestive system Biochemistry Cyclase Gastrointestinal Hormones -- metabolism Secretin Gastrointestinal Hormones Structure-Activity Relationship fluids and secretions Internal medicine medicine Animals Receptor Molecular Biology Secretin -- analogs & derivatives -- pharmacology Membranes Chemistry Rats Inbred Strains Sciences bio-médicales et agricoles Peptide Fragments digestive system diseases Rats Enzyme Activation Endocrinology Liver Protein Binding -- drug effects Adenylate Cyclase -- metabolism Liver -- metabolism Receptors Vasoactive Intestinal Peptide Vasoactive Intestinal Peptide -- metabolism Peptide Fragments -- pharmacology Cyclase activity hormones hormone substitutes and hormone antagonists Adenylyl Cyclases Protein Binding Vasoactive Intestinal Peptide |
| Zdroj: | Biochimica et biophysica acta, 678 (1 |
| ISSN: | 0304-4165 |
| Popis: | 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. Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. info:eu-repo/semantics/published |
| Databáze: | OpenAIRE |
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