Essential role of extracellular charged residues of the human CCK1 receptor for interactions with SR 146131, SR 27897 and CCK-8S

European Journal of Pharmacology

Volumn 389, Issue 2-3, 2000, Pages 115-124

  Gouldson, Paul ^a   Legoux, Pascale ^a   Carillon, Christine ^a   Dumont, Xavier ^a   Le Fur, Gérard ^a   Ferrara, Pascual ^a   Shire, David ^a  

^a SANOFI   (France)

Author keywords

Charged residue; Cholecystokinin CCK1 receptor; Mutagenesis; SR 146131; SR 27897

Indexed keywords

2 [4 (4 CHLORO 2,5 DIMETHOXYPHENYL) 5 (2 CYCLOHEXYL ETHYL)THIAZOL 2 YLCARBAMOYL] 5,7 DIMETHYL INDOYL 1 YL 1 ACETIC ACID; CHOLECYSTOKININ A RECEPTOR; CHOLECYSTOKININ OCTAPEPTIDE DERIVATIVE; CHOLECYSTOKININ RECEPTOR STIMULATING AGENT; LINTITRIPT; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; DRUG RECEPTOR BINDING; EPITHELIUM CELL; MONKEY; MUTAGENESIS; NONHUMAN; PRIORITY JOURNAL;

AMINO ACID SEQUENCE; ANIMALS; COS CELLS; DOSE-RESPONSE RELATIONSHIP, DRUG; HUMANS; INDOLEACETIC ACIDS; INDOLES; INOSITOL PHOSPHATES; MOLECULAR SEQUENCE DATA; MUTATION; RECEPTOR, CHOLECYSTOKININ A; RECEPTORS, CHOLECYSTOKININ; SINCALIDE; STRUCTURE-ACTIVITY RELATIONSHIP; THIAZOLES;

EID: 0034681373     PISSN: 00142999     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-2999(99)00894-8     Document Type: Article

References (31)

1. Becksickinger A.G., Jung G. Structure-activity relationships of neuropeptide Y analogues with respect to Y-1 and Y-2 receptors. Biopolymers. 37:1995;123-142.
2. Bignon E., Bachy A., Boigegrain R., Brodin R., Cottineau M., Gully D., Herbert J.-M., Keane P., Labie C., Molimard J.-C., Olliero D., Oury-Donat F., Petereau C., Prabonneaud V., Rockstroh M.-P., Schaeffer P., Servant O., Thurneyssen O., Soubrié P., Pascal M., Maffrand J.-P., Le Fur G. SR146131: a new, potent, orally active and selective non-peptide cholecystokinin subtype I receptor agonist: I. In vitro studies. J. Pharmacol. Exp. Ther. 289:1999;742-751.
3. Bodanszky M., Tolle J.C., Gardner J.D., Walker M.D., Mutt V. Cholecystokinin (pancreozymin). Synthesis and properties of the N alpha-acetyl-derivative of cholecystokinin 27-33. Int. J. Pept. Protein Res. 16:1980;402-411.
4. Bouaboula M., Perrachon S., Milligan L., Canat X., Rinaldi-Carmona M., Portier M., Barth F., Calandra B., Pecceu F., Lupker J., Maffrand J.P., Le Fur G., Casellas P. A selective inverse agonist for central cannabinoid receptor inhibits mitogen-activated protein kinase activation stimulated by insulin or insulin-like growth factor 1evidence for a new model of receptor/ligand interactions. J. Biol. Chem. 272:1997;22330-22339.
5. Gigoux V., Escrieut C., Fehrentz J.A., Poirot S., Maigret B., Moroder L., Gully D., Martinez J., Vaysse N., Fourmy D. Arginine 336 and asparagine 333 of the human cholecystokinin-A receptor binding site interact with the penultimate aspartic acid and the C-terminal amide of cholecystokinin. J. Biol. Chem. 274:1999;20457-20464.
6. Gigoux V., Escrieut C., Silvente-Poirot S., Maigret B., Gouilleux L., Fehrentz J.A., Gully D., Moroder L., Vaysse N., Fourmy D. Met-195 of the cholecystokinin-A receptor interacts with the sulfated tyrosine of cholecystokinin and is crucial for receptor transition to high affinity state. J. Biol. Chem. 273:1998;14380-14386.
7. Gouldson P.R., Legoux P., Carillon C., Delpech B., Le Fur G., Ferrara P., Shire D. Contrasting roles of Leu356 in the human CCK1 receptor for antagonist SR 27897 and agonist SR 146131 binding. Eur. J. Pharmacol. 383:1999;341-348.
8. Gully D., Fréhel D., Marcy C., Spinazzé A., Lespy L., Neliat G., Maffrand J.P., Le Fur G. Peripheral biological activity of SR-27,897: a new potent non-peptide antagonist of CCK-A receptors. Eur. J. Pharmacol. 232:1993;13-19.
9. Hadac E.M., Pinon D.I., Ji Z.S., Holicky E.L., Henne R.M., Lybrand T.P., Miller L.J. Direct identification of a second distinct site of contact between cholecystokinin and its receptor. J. Biol. Chem. 273:1998;12988-12993.
10. Horton R.M., Hunt H.D., Ho S.N., Pullen J.K., Pease L.R. Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension. Gene. 77:1989;61-68.
11. Huang S., Fortune K.P., Wank S.A., Kopin A.S., Gardner J.D. Multiple affinity states of different cholecystokinin receptors. J. Biol. Chem. 269:1994;26121-26126.
12. Ji Z.S., Hadac E.M., Henne R.M., Patel S.A., Lybrand T.P., Miller L.J. Direct identification of a distinct site of interaction between the carboxyl-terminal residue of cholecystokinin and the type A cholecystokinin receptor using photoaffinity labeling. J. Biol. Chem. 272:1997;24393-24401.
13. Kennedy K., Escrieut C., Dufresne M., Clerc P., Vaysse N., Fourmy D. Identification of a region of the N-terminal of the human CCKA receptor essential for the high affinity interaction with agonist CCK. Biochem. Biophys. Res. Commun. 213:1995;845-852.
14. Kennedy K., Gigoux V., Escrieut C., Maigret B., Martinez J., Moroder L., Frehel D., Gully D., Vaysse N., Fourmy D. Identification of two amine acids of the human cholecystokinin-A receptor that interact with the N-terminal moiety of cholecystokinin. J. Biol. Chem. 272:1997;2920-2926.
15. Kopin A.S., McBride E.W., Quinn S.M., Kolakowski L.F., Beinborn M. The role of the cholecystokinin-B gastrin receptor transmembrane domains in determining affinity for subtype-selective ligands. J. Biol. Chem. 270:1995;5019-5023.
16. Miloux B., Lupker J.H. Rapid isolation of highly productive recombinant Chinese hamster ovary cell lines. Gene. 149:1994;341-344.
17. Pandya P.K., Huang S.C., Talkad V.D., Wank S.A., Gardner J.D. Biochemical regulation of the three different states of the cholecystokinin (CCK) receptor in pancreatic acini. Biochim. Biophys. Acta. 1224:1994;117-126.
18. Pearson R.K., Miller L.J. Affinity labeling of a novel cholecystokinin-binding protein in rat pancreatic plasmalemma using new short probes for the receptor. J. Biol. Chem. 262:1987;869-876.
19. Sainz E., Akeson M., Mantey S.A., Jensen R.T., Battey J.F. Four amino acid residues are critical for high affinity binding of neuromedin B to the neuromedin B receptor. J. Biol. Chem. 273:1998;15927-15932.
20. Silvente-Poirot S., Escrieut C., Wank S.A. Role of the extracellular domains of the cholecystokinin receptor in agonist binding. Mol. Pharmacol. 54:1998;364-371.
21. Sydow S., Flaccus A., Fischer A., Spiess J. The role of the fourth extracellular domain of the rat corticotrophin-releasing factor receptor type 1 in ligand binding. Eur. J. Biochem. 259:1999;55-62.
22. Talkad V.D., Fortune K.P., Pollo D.A., Shah G.N., Wank S.A., Gardner J.D. Direct demonstration of three different states of the pancreatic cholecystokinin receptor. Proc. Natl. Acad. Sci. U.S.A. 91:1994;1868-1872.
23. Talkad V.D., Patto R.J., Metz D.C., Turner R.J., Fortune K.P., Bhat S.T., Gardner J.D. Characterization of the three different states of the cholecystokinin (CCK) receptor in pancreatic acini. Biochim. Biophys. Acta. 1224:1994;103-116.
24. Tarasova N.I., Stauber R.H., Choi J.K., Hudson E.A., Czerwinski G., Miller J.L., Pavlakis G.N., Michejda C.J., Wank S.A. Visualization of G protein-coupled receptor trafficking with the aid of the green fluorescent proteinendocytosis and recycling of cholecystokinin receptor type A. J. Biol. Chem. 272:1997;14817-14824.
25. Topham C.M., Mouledous L., Poda G., Maigret B., Meunier J.C. Molecular modelling of the ORL1 receptor and its complex with nociceptin. Protein Eng. 11:1998;1163-1179.
26. Walker P., Munoz M., Martinez R., Peitsch M.C. Acidic residues in extracellular loops of the human Y1 neuropeptide Y receptor are essential for ligand binding. J. Biol. Chem. 269:1994;2863-2869.
27. Wank S.A. Cholecystokinin receptors. Am. J. Physiol. 32:1995;G628-G646.
28. Wank S.A. G protein-coupled receptors in gastrointestinal physiology iCCK receptorsan exemplary family. Am. J. Physiol. 37:1998;G607-G613.
29. Wank S.A., Harkins R.T., Jensen R.T., Shapira H., De Weerth A., Slattery T. Purification, molecular cloning, and functional expression of the cholecystokinin receptor from rat pancreas. Proc. Natl. Acad. Sci. U.S.A. 89:1992;3125-3129.
30. Wank S.A., Pisegna J.R., De Weerth A. Brain and gastrointestinal cholecystokinin receptor family: structure and functional expression. Proc. Natl. Acad. Sci. U.S.A. 89:1992;8691-8695.
31. Wu V., Yang M., McRoberts J.A., Ren J., Seensalu R., Zeng N.X., Dagrag M., Birnbaumer M., Walsh J.H. First intracellular loop of the human cholecystokinin-A receptor is essential for cyclic AMP signaling in transfected HEK-293 cells. J. Biol. Chem. 272:1997;9037-9042.