Tyr1 and Ile7 of glucose-dependent insulinotropic polypeptide (GIP) confer differential ligand selectivity toward GIP and glucagon-like peptide-1 receptors

Molecules and Cells

Volumn 30, Issue 2, 2010, Pages 149-154

  Moon, Mi Jin ^a   Kim, Hee Young ^a,b   Kim, Sin Gon ^a,b   Park, Juri ^a,b   Choi, Dong Seop ^a,b   Hwang, Jong Ik ^a   Seong, Jae Young ^a  

^a Korea University College of Medicine   (South Korea)

^b Korea University   (South Korea)

Author keywords

GIP; GLP 1; GPCR; Insulin; Ligand selectivity; Pancreas

Indexed keywords

CYCLIC AMP; EXENDIN 4; GASTRIC INHIBITORY POLYPEPTIDE; GLUCAGON LIKE PEPTIDE 1 RECEPTOR; GASTRIC INHIBITORY POLYPEPTIDE RECEPTOR; GLUCAGON LIKE PEPTIDE RECEPTOR; GLUCAGON RECEPTOR; GLUCAGON-LIKE PEPTIDE RECEPTOR; HORMONE RECEPTOR; ISOLEUCINE; LIGAND; PEPTIDE; RECOMBINANT PROTEIN; TYROSINE; VENOM;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CELL STRAIN HEK293; GENETIC TRANSFECTION; PROTEIN EXPRESSION; ANIMAL; CHEMISTRY; HUMAN; METABOLISM; MOLECULAR GENETICS; RAT; SEQUENCE ALIGNMENT; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; ANIMALS; GASTRIC INHIBITORY POLYPEPTIDE; HUMANS; ISOLEUCINE; LIGANDS; MOLECULAR SEQUENCE DATA; PEPTIDES; RATS; RECEPTORS, GASTROINTESTINAL HORMONE; RECEPTORS, GLUCAGON; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; STRUCTURE-ACTIVITY RELATIONSHIP; TYROSINE; VENOMS;

EID: 78651485015     PISSN: 10168478     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10059-010-0100-5     Document Type: Article

References (22)

1. Adelhorst, K., Hedegaard, B. B., Knudsen, L. B., and Kirk, O. (1994). Structure-activity studies of glucagon-like peptide-1. J. Biol. Chem. 269, 6275-6278.
2. Al-Sabah, S., and Donnelly, D. (2003). A model for receptor-peptide binding at the glucagon-like peptide-1 (GLP-1) receptor through the analysis of truncated ligands and receptors. Br. J. Pharmacol. 140, 339-346.
3. Baggio, L. L., and Drucker, D. J. (2007). Biology of incretins: GLP-1 and GIP. Gastroenterology 132, 2131-2157.
4. Cho, H. J., Acharjee, S., Moon, M. J., Oh, D. Y., Vaudry, H., Kwon, H. B., and Seong, J. Y. (2007). Molecular evolution of neuropeptide receptors with regard to maintaining high affinity to their authentic ligands. Gen. Comp. Endocrinol. 153, 98-107.
5. Drucker, D. J., Philippe, J., Mojsov, S., Chick, W. L., and Habener, J. F. (1987). Glucagon-like peptide I stimulates insulin gene expression and increases cyclic AMP levels in a rat islet cell line. Proc. Natl. Acad. Sci. USA 84, 3434-3438.
6. Fehmann, H. C., Goke, R., and Goke, B. (1995). Cell and molecular biology of the incretin hormones glucagon-like peptide-I and glucose-dependent insulin releasing polypeptide. Endocr. Rev. 16, 390-410.
7. Gallwitz, B., Witt, M., Paetzold, G., Morys-Wortmann, C., Zimmermann, B., Eckart, K., Folsch, U. R., and Schmidt, W. E. (1994). Structure/activity characterization of glucagon-like peptide-1. Eur. J. Biochem. 225, 1151-1156.
8. Gallwitz, B., Witt, M., Morys-Wortmann, C., Folsch, U. R., and Schmidt, W. E. (1996). GLP-1/GIP chimeric peptides define the structural requirements for specific ligand-receptor interaction of GLP-1. Regul. Pept. 63, 17-22.
9. Göke, R., Fehmann, H. C., Linn, T., Schmidt, H., Krause, M., Eng, J., and Goke, B. (1993). Exendin-4 is a high potency agonist and truncated exendin-(9-39)-amide an antagonist at the glucagon-like peptide 1-(7-36)-amide receptor of insulin-secreting beta-cells. J. Biol. Chem. 268, 19650-19655.
10. Hinke, S. A., Manhart, S., Pamir, N., Demuth, H., W. Gelling, R., Pederson, R. A., and McIntosh, C. H. (2001). Identification of a bioactive domain in the amino-terminus of glucose-dependent insulinotropic polypeptide (GIP). Biochim. Biophys. Acta 1547, 143-155.
11. Hinke, S. A., Gelling, R. W., Pederson, R. A., Manhart, S., Nian, C., Demuth, H. U., and McIntosh, C. H. (2002). Dipeptidyl peptidase IV-resistant [D-Ala (2)]glucose-dependent insulinotropic polypeptide (GIP) improves glucose tolerance in normal and obese diabetic rats. Diabetes 51, 652-661.
12. Hinke, S. A., Manhart, S., Speck, M., Pederson, R. A., Demuth, H. U., and McIntosh, C. H. (2004). In depth analysis of the N-terminal bioactive domain of gastric inhibitory polypeptide. Life Sci. 75, 1857-1870.
13. Holtmann, M. H., Hadac, E. M., and Miller, L. J. (1995). Critical contributions of amino-terminal extracellular domains in agonist binding and activation of secretin and vasoactive intestinal polypeptide receptors. Studies of chimeric receptors. J. Biol. Chem. 270, 14394-14398.
14. Lee, Y. R., Tsunekawa, K., Moon, M. J., Um, H. N., Hwang, J. I., Osugi, T., Otaki, N., Sunakawa, Y., Kim, K., Vaudry, H., et al. (2009). Molecular evolution of multiple forms of kisspeptins and GPR54 receptors in vertebrates. Endocrinology 150, 2837-2846.
15. Maida, A., Hansotia, T., Longuet, C., Seino, Y., and Drucker, D. J. (2009). Differential importance of glucose-dependent insulinotropic polypeptide vs glucagon-like peptide 1 receptor signaling for beta cell survival in mice. Gastroenterology 137, 2146-2157.
16. Nauck, M. A., Bartels, E., Orskov, C., Ebert, R., and Creutzfeldt, W. (1993). Additive insulinotropic effects of exogenous synthetic human gastric inhibitory polypeptide and glucagon-like peptide-1-(7-36) amide infused at near-physiological insulinotropic hormone and glucose concentrations. J. Clin. Endocrinol. Metab. 76, 912-917.
17. Neidigh, J. W., Fesinmeyer, R. M., Prickett, K. S., and Andersen, N. H. (2001). Exendin-4 and glucagon-like-peptide-1: NMR structural comparisons in the solution and micelle-associated states. Biochemistry 40, 13188-13200.
18. Orskov, C., Holst, J. J., Knuhtsen, S., Baldissera, F. G., Poulsen, S. S., and Nielsen, O. V. (1986). Glucagon-like peptides GLP-1 and GLP-2, predicted products of the glucagon gene, are secreted separately from pig small intestine but not pancreas. Endocrinology 119, 1467-1475.
19. Parthier, C., Kleinschmidt, M., Neumann, P., Rudolph, R., Manhart, S., Schlenzig, D., Fanghanel, J., Rahfeld, J. U., Demuth, H. U., and Stubbs, M. T. (2007). Crystal structure of the incretin-bound extracellular domain of a G protein-coupled receptor. Proc. Natl. Acad. Sci. USA 104, 13942-13947.
20. Sherwood, N. M., Krueckl, S. L., and McRory, J. E. (2000). The origin and function of the pituitary adenylate cyclase-activating polypeptide (PACAP)/glucagon superfamily. Endocr. Rev. 21, 619-670.
21. Underwood, C. R., Garibay, P., Knudsen, L. B., Hastrup, S., Peters, G. H., Rudolph, R., and Reedtz-Runge, S. (2010). Crystal structure of glucagon-like peptide-1 in complex with the extracellular domain of the glucagon-like peptide-1 receptor. J. Biol. Chem. 285, 723-730.
22. Yaqub, T., Tikhonova, I. G., Lattig, J., Magnan, R., Laval, M., Escrieut, C., Boulegue, C., Hewage, C., and Fourmy, D. (2010). Identification of determinants of glucose-dependent insulinotropic polypeptide receptor that interact with N-terminal biologically active region of the natural ligand. Mol. Pharmacol. 77, 547-558.