On the mechanism of hormone recognition and binding by the CCK-B/gastrin receptor

Journal of Peptide Science

Volumn 3, Issue 1, 1997, Pages 1-14

  Moroder, Luis ^a  

^a MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

Author keywords

Conformation; Ligand receptor docking; Lipid interaction; Peptide lipidation; Receptor binding; Vesicles

Indexed keywords

CHOLECYSTOKININ B RECEPTOR; CHOLECYSTOKININ RECEPTOR; HORMONE;

ANIMAL; ARTICLE; CHEMISTRY; ENTROPY; HUMAN; METABOLISM; PROTEIN BINDING;

ANIMALS; ENTROPY; HORMONES; HUMANS; PROTEIN BINDING; RECEPTOR, CHOLECYSTOKININ B; RECEPTORS, CHOLECYSTOKININ;

EID: 0030629416     PISSN: 10752617     EISSN: None     Source Type: Journal    
DOI: 10.1002/(sici)1099-1387(199701)3:1<1::aid-psc85>3.0.co;2-l     Document Type: Review

References (95)

1. G. A. Weiland, K. P. Minneman and P. B. Molinoff, (1979). Differences between the molecular interaction of agonists and antagonists with the β-adrenergic receptor. Nature 281, 114-117.
2. A. Miklavc, D. Kocjan, J. Mavri, J. Koller and D. Hadzi, (1990). On the fundamental difference in the thermodynamics of agonist and antagonist interactions with β-adrenergic receptors and the mechanism of entropy-driven binding. Biochem. Pharmacol. 40, 663-669.
3. M. S. Searle and D. H. Williams, (1992). The cost of conformational order: entropy changes in molecular associations. J. Am. Chem. Soc. 114, 10690-10697.
4. R. Schwyzer, in: Natural Products and Biological Activity, H. Imura, T. Goto, T. Murachi and T. Nakajima, Eds., p. 197-207, Tokyo Press, Elsevier, Tokyo, 1986.
5. R. Schwyzer, (1991). Peptide-membrane interactions and a new principle in quantitative structure-activity relationships. Biopolymers 31, 785-792.
6. R. Schwyzer, (1995). In search of the 'bioactive conformation' - Is it induced by the target cell membrane? J. Mol. Recogn. 8, 3-8.
7. A. Seelig and J. Seelig, (1977). Structure of phospholipid bilayers. Biochemistry 16, 45-50.
8. G. Büldt, H. U. Gally, A. Seelig, J. Seelig and G. Zaccai, (1978). Studies on selectively deuterated phospholipid bilayers. Nature 271, 182-184.
9. M. C. Wiener and S. H. White, (1992). Dioleoylphosphatidylethanolamine bilayer determined by joint refinement of X-ray and neutron diffraction data. 2. Distribution and packing of terminal methyl groups. Biophys. J. 61, 434-447.
10. C. Tanford: The Hydrophobic Effect: Formation of Micelles and Biological Membranes, 2nd edn, Wiley-Interscience, New York, 1980.
11. C.-H. Huang and J. P. Charlton, (1972). Interaction of phosphatidylcholine vesicles with 2-p-toluidinylnaphthalene-6-sulfonate. Biochemistry 11, 735-740.
12. J. Seelig and P. Glanz, (1991). Nonclassical hydrophobic effect in membrane-binding equilibria. Biochemistry 30, 9354-9359.
13. W. C. Wimley and S. H. White (1993). Membrane partitioning: Distinguishing bilayer effects from the hydrophobic effect. Biochemistry 32, 6307-6312.
14. G. Beschiaschvili and J. Seelig, (1992). Peptide binding to lipid bilayers, Nonclassical hydrophobic effect and membrane-induced pK shifts. Biochemistry 31, 10044-10053.
15. L. Leder, Ch. Berger, S. Bornhauser, H. Wendt, F. Ackermann, I. Jelesarov and H. R. Bosshard, (1995). Spectroscopic, calorimetric and kinetic demonstration of conformational adaptation in peptide-antibody recognition. Biochemistry 34, 16509-16518.
16. D. E. Koshland Jr, G. Nemethy and D. Filmer, (1966). Comparison of experimental binding data and theoretical models in proteins containing subunits. Biochemistry 5, 365-385.
17. P. J. Casey (1995). Protein lipidation in cell signaling. Science 268, 221-225.
18. R. M. Peitzsch and S. McLaughlin, (1993). Binding of acylated peptides and fatty-acids to phospholipid vesicles - Pertinence to myristoylated proteins. Biochemistry 32, 10436-10443.
19. R. F. Epand, C. B. Kue, S.-H. Wang, F. Naider, J. M. Becker and R. M. Epand, (1993). Role of prenylation in the interaction of the α-factor mating pheromone with phospholipid bilayers. Biochemistry 32, 8368-8373
20. J. R. Silvius and F. L'Heureux, (1994). Fluorometric evaluation of the affinities of isoprenylated peptides for lipid bilayers. Biochemistry 33, 3014-3022.
21. 2-terminus of SRC. Biochemistry 33, 13093-13101.
22. J. Kim, T. Shishido, X. Jiang, A. Aderem and S. McLaughlin, (1994). Phosphorylation, high ionic strength, and calmodulin reverse the binding of MARCKS to phospholipid vesicles. J. Biol. Chem. 269, 28214-28219.
23. C. T. Sigal, W. J. Zhou, C. A. Buser, S. McLaughlin and M. D. Resh, (1994). Amino-terminal basic residues of SRC mediate membrane-binding through electrostatic interaction with acidic phospholipids. Proc. Acad. Sci. USA 91, 12253-12257.
24. S. McLaughlin and A. Aderem, (1995). The myristoylelectrostatic switch: A modulation of reversible protein-membrane interactions. Trends Biochem. Sci. 20, 272-276.
25. S. Shahinian and J. R. Silvius, (1995). Double-lipid-modified protein sequence motifs exhibit long-lived anchorage to lipid bilayer membranes. Biochemistry 34, 3813-3822.
26. M. A. J. Ferguson and A. F. Williams, (1988). Cell-surface anchoring of proteins via glyceryl-phosphatidylinositol structures. Annu. Rev. Biochem. 57, 285-320.
27. G. A. M. Cross, (1990). Glycolipid anchoring of plasma-membrane proteins. Annu. Rev. Cell. Biol. 6, 1-39.
28. L. Moroder, H.-J. Musiol and G. Siglmüller, (1990). Synthesis of 1,2-diacyl-3-thioglycerols. Synthesis, 889-892.
29. B. G. Tenchov, A. I. Boyanov and R. D. Koynova, (1984). Lyotropic polymorphism of racemic dipalmitoylphosphatidylethanolamine: A differential scanning calorimetry study. Biochemistry 23, 3553-3558.
30. F. Macquaire, F. Baleux, E. Giaccobi, T. Huynh-Dinh, J.-M. Neuman and A. Sanson, (1992). Peptide secondary structure induced by a micellar phospholipid interface. Proton NMR conformational study of a lipopeptide. Biochemistry 31, 2576-2582.
31. F. Delie, P. Couvreur, D. Nisato, J.-B. Michel, F. Puisieux and Y. Letourneux, (1994). Synthesis and in vitro study of a diglyceride prodrug of a peptide. Pharm. Res. 11, 1082-1087.
32. Y. Murakami, A. Nakano and H. Ikeda, (1982). Preparation of stable single-compartment vesicles with cationic and zwitterionic amphiphiles involving amino acid residues. J. Org. Chem. 47, 2137-2144.
33. K. Yamada, H. Ihara, T. Ide, T. Fukumoto and C. Hirayama, (1984). Formation of helical super-structure from single-walled bilayers by amphiphiles with oligo-L-glutamic acid-head group. Chem. Lett., 1713-1716.
34. T. Shimizu and M. Hato, (1993). Self-assembling properties of synthetic peptidic lipids. Biochim. Biophys. Acta 1147, 50-58.
35. J. Martinez, in: Comprehensive Medicinal Chemistry, Vol. 3, C. Hansch, P. G. Sammer and J. B. Taylor, Eds. P. 925-959, Pergamon Press, New York, 1990.
36. R. Romano, H.-J. Musiol, E. Weyher, M. Dufresne and L. Moroder, (1992). Peptide hormone membrane interactions: the aggregational and conformational state of lipo-gastrin derivatives and their receptor binding affinity. Biopolymers 32, 1545-1558.
37. R. Roman, T. M. Bayerl and L. Moroder, (1993). Lipophilic derivatization and its effect on the interaction of cholecystokinin (CCK) nonapeptide with phospholipids. Biochim. Biophys. Acta 1151, 111-119.
38. J. Lutz, R. Romano-Götsch, C. Escrieut, D. Fourmy, B Mathā, G. Müller, H. Kessler and L. Moroder, (1996). Mapping of the ligand binding site of cholecystokinin-B/gastrin receptor using lipo-gastrin peptides and molecular modelling. Biopolymers, in press
39. G. H. de Haas, P. P. M. Bonsen, W. A. Pieterson and L.L. M. van Deenen, (1971). Studies on phospholipase A and its zymogen from porcine pancreas. Biochim. Biophys. Acta 239, 252-266.
40. D. A. Mannock, R. N. A. H. Lewis, A. Sen and R. N. Mcelhaney, (1988). The physical properties of glycosidyl-diacylglycerols. I. Calorimetric studies of a homologous series of 1,2-di-O-acyl-3-O-(β-D-glucopyranosyl)-S,N-glycerols. Biochemistry 27, 6852-6859.
41. H. J. Hinz, H. Kuttenreich, R. Meyer, M. Renner and R. Fruend, (1991). Stereochemistry and size of sugar headgroups determine structure and phase behaviour of glycolipid membranes. Biochemistry 30, 5125-5138.
42. J. R. Silvius and M. J. Zuckermann (1993). Interbilayer transfer of phospholipid-anchored macromolecules via monomer diffusion. Biochemistry 32, 3153-3161.
43. H. Ihara, T. Fukumoto, C. Hirayama and K. Yamada, (1986). Exceptional morphologies and metamorphosis of bilayer-membranes formed from amphiphiles with poly-(L-aspartic acid)-head groups. Polym. Commun. 27, 282-285.
44. R. Romano, M. Dufresne, M.-C. Prost, J.-P. Bali, T. M. Bayerl and L. Moroder, (1993). Peptide hormone membrane interactions. Intervesicular transfer of lipophilic gastrin derivatives to artificial membranes and their bioactivities. Biochim. Biophys. Acta 1145, 235-242.
45. J. W. Nichols and R. E. Pagano, (1981). Kinetics of soluble lipid monomer diffusion between vesicles. Biochemistry 20, 2783-2789.
46. M. De Cuyper, M. Joniau and H. Dangreau. (1983). Intervesicular phospholipid transfer. A free-flow electrophoresis study. Biochemistry 26, 5389-5397.
47. L. Thilo, (1977). Kinetics of phospholipid exchange in bilayer membranes. Biochim. Biophys. Acta 469, 326-334.
48. J. W. Nichols, (1985). Thermodynamics and kinetics of phospholipid monomer-vesicular interaction. Biochemistry 24, 6390-6398.
49. B. R. Lentz, T. J. Carpenter and D. R. Alford, (1983). Spontaneous fusion of phosphatidylcholine small unilamellar vesicles in the fluid phase. Biochemistry 26, 5389-5397.
50. R. F. Irvine, (1992). Inositol lipids in cell signalling. Curr. Opin. Cell Biol. 4, 212-219.
51. S. Muallem, (1989). Calcium transport pathways of pancreatic acinar cells. Annu. Rev. Physiol. 51, 83-105.
52. - current recording in single pancreatic acinar cells. EMBO J. 9, 697-704.
53. M. Korc, B. Chandrasekar and S. A. Siwik, (1991). Cholecystokinin-induced phosphatidylinositol hydrolysis in rat pancreatic acinar cells: modulation by extracellular calcium and manganese. Endocrinology 129, 39-46.
54. L. Moroder and R. Romano, (1994). Synthesis, conformation and biological properties of lipophilic derivatives of gastrin and cholecystokinin peptides. Pure Appl. Chem. 66, 2111-2114.
55. E. Peggion, S. Mammi, M. Palumbo, L. Moroder and E. Wünsch, (1983). Interaction of calcium ions with peptide hormones of the gastrin family. Biopolymers 22, 2443-2457.
56. 2+ to biologically active analogs of little gastrin and minigastrin. Biopolymers 23, 1225-1240.
57. J. Lutz, E. Weyher and L. Moroder. (1995). Metal ion binding affinities of gastrin and CCK in membrane mimetic conditions. J. Peptide Sci. 1, 360-370.
58. R. Romano-Götsch, 'Interaction of peptide hormones with lipids', Dissertation, TU-München 1993.
59. L. Moroder, R. Romano, W. Guba, D. F. Mierke, H. Kessler, C. Delporte, J. Winand and J. Christophe, (1993). New evidence for a membrane-bound pathway in hormone receptor binding. Biochemistry 32, 13551-12559.
60. V. S. Ananthanarayanan, in: Peptides, Design, Synthesis and Biological Activity, C. Basava and G. M. Anantharamaiah, Eds., p. 223-234, Birkhäuser, Boston, 1994.
61. E. Fattal, S. Nir, R. A. Parente and F. C. Szoka Jr, (1994). Pore-forming peptides induce rapid phospholipid flip-flop in membranes. Biochemistry 33, 6721-6731.
62. 2+ ionophores: implications for signal transduction. Biochem. Cell Biol. 69, 93-95.
63. 2+-induced aggregation of oligopeptides having a carboxyl group in phospholipid bilayer membrane. Bull. Chem. Soc. Jpn. 66, 1466-1471.
64. L.-P. Choo, M. Jackson and H. Mantsch, (1994). Conformation and self-association of the peptide hormone substance P. Fourier-transform infrared spectroscopic study. Biochem. J. 301, 667-670.
65. J. R. Silvius and R. Leventis, (1993). Spontaneous interbilayer transfer of phospholipids: Dependence on acyl chain composition. Biochemistry 32, 13318-13326.
66. H. J. Tracy and R. A. Gregory (1964). Physiological properties of a series of synthetic peptides structurally related to gastrin. Nature 204, 935-938.
67. M. Dufresne, C. Escrieut, P. Clerc, C. Saillan, K. Kennedy, M. Fanjul, G. Mengod, F. Real, L. Moroder, N Vaysse and D. Fourmy, (1995). Predominant expression of CCK-B/gastrin receptor in the human pancreas. Digestion 56, 280.
68. K. Takeuchi, G. R. Speir and L. R. Johnson, (1980). Mucosal gastrin receptor. IV. Binding specificity. Am J. Physiol. 239, G395-G399.
69. J. E. Ferrell Jr, K.-J. Lee and W. Huestis, (1985). Lipid transfer between phasphatidylcholine vesicles and human erythrocytes: Exponential decrease in rate with increasing acyl chain length. Biochemistry 24, 2857-2864.
70. M. Beinborn, Y.-M. Lee, E. W. McBride, S. M. Quinn and A. S. Kopin, (1993). A single amino acid of the cholecystokinin-B/gastrin receptor determines specificity for non-peptide antagonists. Nature 362, 348-350.
71. T. Mantamadiotis and G. S. Baldwin, (1994). The seventh transmembrane domain of gastrin/CCK-B receptors contributes to non-peptide antagonist binding. Biochem. Biophys. Res. Commun. 201, 1382-1389.
72. A. S. Kopin, E. W. McBride, S. M. Quinn, L. F. Kolakowski and M. Beinborn, (1995). The role of the cholecystokinin-B/gastrin receptor transmembrane domains in determining affinity for subtype-selective ligands. J. Biol. Chem. 270, 5019-5023.
73. K. Kennedy, C. Escrieut, M. Dufresne, P. Clerc, N. Vaysse and D. Fourmy, (1995). Identification of a region of the N-terminal of the human CCK-A receptor essential for the high affinity interaction with agonist CCK. Biochem. Biophys. Res. Commun. 213, 845-852.
74. F. Schmitz, M.-J. Wu, D. S. Pratt, M. Beinborn and A. S. Kopin, (1995). Identification of cholecystokinin-B/ gastrin receptor domains which confer high affinity for gastrin. Gastroenterology 108, A1004.
75. J. Ren, D. Avedian, J. H. Walsh and S. V. Wu, (1995). Binding and cellular responses exhibited by a chimeric human CCK-A/CCK-B receptor indicate separate ligand binding, inhibitor binding and signal transduction domains. Gastroenterology 108, A1202.
76. S. S. Poirot and S. A. Wank, (1995). Identification of the amino acids responsible for cholecystokinin receptor subtype selectivity for gastrin. Gastroenterology 108, A845.
77. 100 in the second transmembrane domain of the cholecystokinin B receptor increases antagonist binding and reduces signal transduction. Mol. Pharmacol. 48, 783-789.
78. R. Henderson, J. M. Baldwin, T. A. Ceska, F. Zemlin, L. Beckman and K. H. Downing, (1990). Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J. Mol. Biol. 213, 899-929.
79. G. F. X. Schertler, C. Villa and R. Henderson, (1993). Projection structure of rhodopsin. Nature 362, 770-772.
80. J. M. Baldwin, (1993). The probable arrangement of the helices in G protein-coupled receptors. EMBO J. 12, 1693-1703.
81. 1H-NMR. Int. J. Peptide Protein Res. 27, 145-152.
82. 1H-NMR and circular dichroism. Biochemistry 27, 1374-1379.
83. L. Moroder, A. D'Ursi, D. Picone, P. Amodeo and P. A. Temussi, (1993). Solution conformation of CCK-9, a cholecystokinin analog. Biochem. Biophys. Res. Commun. 190, 741-746.
84. L. Moroder, R. Romano, E. Weyher, M. Svoboda and J. Christophe, (1993). Circular dichroism study on fully bioactive CCK-peptides. Z. Naturforsch. 48b, 1419-1430.
85. E. Wünsch, L. Moroder, W. Göhring, G. Borin, A. Calderan and J.-P. Bali, (1986). Synthesis of human des-tryptophan-1, norleucine-12-minigastrin-II and its biological activities. FEBS Lett. 206, 203-207.
86. S. C. Huang, D.-H. Yu, S. A. Wank, S. Mantley, J. D. Gardner and R. T. Jensen, (1989). Importance of sulfation of gastrin or cholecystokinin (CCK) on affinity forgastrin and CCK receptors. Peptides 10, 785-789.
87. R. Magous and J.-P. Bali, (1982). High-affinity binding sites for gastrin on isolated rabbit gastric mucosal cells. Eur. J. Pharmacol. 82, 47-54.
88. W. Göhring, L. Moroder, G. Borin, A. Lobbia, J.-P. Bali and E. Wünsch, (1984). Synthese von gastrin-aktiven Peptiden. Untersuchungen zur Struktur-Wirkungsbeziehung des natürlichen Hormones Human-Little-Gastrin-I. Hoppe Seyler's Z. Physiol. Chem. 365, 83-94.
89. L. Moroder and E. Wünsch, in: Gastrin and Cholecystokinin: Chemistry, Physiology and Pharmacology, J.-P. Bali and J. Martinez, Eds., p. 21-32, Elsevier, Amsterdam 1987.
90. S. S. Poirot and S. A. Wank, (1996). J. Biol. Chem. 271, 14698-14706.
91. M. Jackson and H. H. Mantsch. (1992). Halogenated alcohols as solvents for proteins: FTIR spectroscopic studies. Biochim. Biophys. Acta 1118, 139-143.
92. F. D. Sönnichsen, J. E. Van Eyk, R. S. Hodges and B. D. Sykes, (1992). Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using a synthetic actin peptide. Biochemistry 31, 8790-8798.
93. L. Moroder and J. Lutz, in: Studies in Natural Products Chemistry, Atta-ur-Rahman, Ed., p. 819-873, Elsevier Science, Amsterdam 1996.
94. M. R. Pincus, R. P. Carry, J. Chen, J. Lubowsky, M. Avitable, D. Shah, H. A. Scheraga and R. B. Murphy, (1987). On the biologically active structures of cholecystokinin, little gastrin, and enkephalin in the gastrointestinal system. Proc. Natl. Acad. Sci. USA 84, 4821-4825.
95. B. E. Evans, M. G. Bock, K. E. Rittle, R. M. DiPardo, W. L. Whitter, D. F. Veber, P. S. Anderson and R. M. Freidinger, (1986). Design of potent orally effective nonpeptidal antagonists of the peptide-hormone cholecystokinin. Proc. Natl. Acad. Sci. USA 74, 414-418.