Interaction of substance P, compound 48/80 and mastoparan with the α-subunit C-terminus of G protein

• Published in: Immunology letters Vol. 25; no. 4; pp. 355 - 358
• Main Authors: MOUSLI, M, BRONNER, C, BOCKAERT, J, ROUOT, B, LANDRY, Y
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier 01.09.1990
• Subjects: Amino Acid Sequence; Analytical, structural and metabolic biochemistry; Animals; Antibodies - immunology; Binding and carrier proteins; Biological and medical sciences; Cattle; Enzyme Activation - drug effects; Fundamental and applied biological sciences. Psychology; GTP Phosphohydrolases - metabolism; GTP-Binding Proteins - metabolism; Molecular Sequence Data; p-Methoxy-N-methylphenethylamine - pharmacology; Peptide Fragments - immunology; Peptides; Pertussis Toxin; Protein Binding; Proteins; Substance P - metabolism; Virulence Factors, Bordetella - pharmacology; Wasp Venoms - pharmacology; DGTPase; Brain; GTP; Bovine; Enzyme; Substance P; Molecular interaction; Subunit; Proteins; C terminal-Sequence; Binding protein; Vertebrata; Mammalia; Enzymatic activity; Neurotransmitter; Mast cell; Artiodactyla; Ungulata; G protein
• ISSN: 0165-2478; 1879-0542
• DOI: 10.1016/0165-2478(90)90207-7

Pretreatment of purified calf brain G proteins with activated pertussis toxin or antibodies raised against the C-terminus of their alpha subunits prevented the increase in GTPase activity induced by substance P, compound 48/80 and mastoparan. These results suggest that these mast cell secretagogues activate G proteins directly via an interaction with the C-terminus of alpha subunits of G proteins by mimicking the agonist-liganded receptors.