Cross-chimeric analysis of selectivity of secretin and VPAC1 receptor activation

Journal of Pharmacology and Experimental Therapeutics

Volumn 295, Issue 2, 2000, Pages 682-688

  Park, C G ^a   Ganguli, S C ^a   Pinon, D I ^a   Hadac, E M ^a   Miller, L J ^a  

^a MAYO CLINIC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

SECRETIN; VASOACTIVE INTESTINAL POLYPEPTIDE; VASOACTIVE INTESTINAL POLYPEPTIDE RECEPTOR;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; CHIMERA; CHO CELL; CONCENTRATION RESPONSE; CONTROLLED STUDY; DRUG RECEPTOR BINDING; MOLECULAR INTERACTION; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; ANIMAL; BINDING SITES; CHIMERIC PROTEINS; CHO CELLS; COS CELLS; HAMSTERS; LIGANDS; MOLECULAR SEQUENCE DATA; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, GASTROINTESTINAL HORMONE; RECEPTORS, VASOACTIVE INTESTINAL PEPTIDE; SECRETIN; SEQUENCE HOMOLOGY, AMINO ACID; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY; SUPPORT, NON-U.S. GOV'T; SUPPORT, U.S. GOV'T, P.H.S.; VASOACTIVE INTESTINAL PEPTIDE;

EID: 0033780267     PISSN: 00223565     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (19)

1. Highly conserved aspartate 68, tryptophane 73 and glycine 109 in the N-terminal extracellular domain of the human VIP receptor are essential for its ability to bind VIP
2. The arrangement of the transmembrane helices in the secretin receptor family of G-protein-coupled receptors
3. Interaction of peptides related to secretin with hormone receptors on pancreatic acinar cells
4. Importance of the amino acid in position 15 of VIP and secretin in influencing their interactions with membrane receptors on pancreatic acinal cells
5. Mutational analysis of cysteine residues within the extracellular domains of the human vasoactive intestinal peptide (VIP) 1 receptor identifies seven mutants that are defective in VIP binding
6. The C-terminus ends of secretin and VIP interact with the N-terminal domains of their receptors
7. Multiple extracellular loop domains contribute critical determinants for agonist binding and activation of the secretin receptor
8. Critical contributions of amino-terminal extracellular domains in agonist binding and activation of secretin and vasoactive intestinal polypeptide receptors. Studies of chimeric receptors
9. Molecular cloning and expression of a cDNA encoding the secretin receptor
10. Functional expression and tissue distribution of a novel receptor for vasoactive intestinal polypeptide
11. High level transient expression of a chloramphenicol acetyl transferase gene by DEAE-dextran mediated DNA transfection coupled with a dimethyl sulfoxide or glycerol shock treatment
12. Site-directed mutagenesis of human vasoactive intestinal peptide receptor subtypes VIP1 and VIP2: Evidence for difference in the structure-function relationship
13. Molecular mapping of epitopes involved in ligand activation of the human receptor for the neuropeptide, VIP, based on hybrids with the human secretin receptor
14. Secretin and vasoactive intestinal peptide receptors: Members of a unique family of G protein-coupled receptors
15. Intrinsic photoaffinity labeling of native and recombinant rat pancreatic secretin receptors
16. Properties of chimeric secretin and VIP receptor proteins indicate the importance of the N-terminal domain for ligand discrimination
17. Mutational analysis of extracellular cysteine residues of rat secretin receptor shows that disulfide bridges are essential for receptor function
18. Lysine 173 residue within the first exoloop of rat secretin receptor is involved in carboxylate moiety recognition of asp 3 in secretin
19. The C-terminal part of VIP is important for receptor binding and activation, as evidenced by chimeric constructs of VIP/secretin