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Volumn 6, Issue 2, 2011, Pages 135-145

A novel human-based receptor antagonist of sustained action reveals body weight control by endogenous GLP-1

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; ARGININE; EXENDIN 4; GLUCAGON LIKE PEPTIDE 1; GLUCAGON LIKE PEPTIDE 1 RECEPTOR; GLUTAMIC ACID; GLYCINE; LYSINE; PEPTIDE JANT 4; UNCLASSIFIED DRUG; VALINE;

EID: 79951879369     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb1002015     Document Type: Article
Times cited : (46)

References (37)
  • 1
    • 1842855423 scopus 로고    scopus 로고
    • Incretins, insulin secretion and Type 2 diabetes mellitus
    • Vilsboll, T. and Holst, J. J. (2004) Incretins, insulin secretion and Type 2 diabetes mellitus Diabetologia 47, 357-366
    • (2004) Diabetologia , vol.47 , pp. 357
    • Vilsboll, T.1    Holst, J.J.2
  • 2
    • 0026648961 scopus 로고
    • Isolation and characterization of exendin-4, an exendin-3 analogue, from Heloderma suspectum venom. Further evidence for an exendin receptor on dispersed acini from guinea pig pancreas
    • Eng, J., Kleinman, W. A., Singh, L., Singh, G., and Raufman, J. P. (1992) Isolation and characterization of exendin-4, an exendin-3 analogue, from Heloderma suspectum venom. Further evidence for an exendin receptor on dispersed acini from guinea pig pancreas J. Biol. Chem. 267, 7402-7405
    • (1992) J. Biol. Chem. , vol.267 , pp. 7402
    • Eng, J.1    Kleinman, W.A.2    Singh, L.3    Singh, G.4    Raufman, J.P.5
  • 3
    • 0035818410 scopus 로고    scopus 로고
    • Exendin-4 and glucagon-like-peptide-1: NMR structural comparisons in the solution and micelle-associated states
    • 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
    • (2001) Biochemistry , vol.40 , pp. 13188
    • Neidigh, J.W.1    Fesinmeyer, R.M.2    Prickett, K.S.3    Andersen, N.H.4
  • 4
    • 0028207562 scopus 로고
    • Structure of glucagon-like peptide (7-36) amide in a dodecylphosphocholine micelle as determined by 2D NMR
    • Thornton, K. and Gorenstein, D. G. (1994) Structure of glucagon-like peptide (7-36) amide in a dodecylphosphocholine micelle as determined by 2D NMR Biochemistry 33, 3532-3539
    • (1994) Biochemistry , vol.33 , pp. 3532
    • Thornton, K.1    Gorenstein, D.G.2
  • 5
    • 0027184119 scopus 로고
    • 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
    • Goke, 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
    • (1993) J. Biol. Chem. , vol.268 , pp. 19650
    • Goke, R.1    Fehmann, H.C.2    Linn, T.3    Schmidt, H.4    Krause, M.5    Eng, J.6    Goke, B.7
  • 6
    • 0028171996 scopus 로고
    • Exendin-4 and exendin-(9-39)NH2: Agonist and antagonist, respectively, at the rat parietal cell receptor for glucagon-like peptide-1-(7-36)NH2
    • Schepp, W., Schmidtler, J., Riedel, T., Dehne, K., Schusdziarra, V., Holst, J. J., Eng, J., Raufman, J. P., and Classen, M. (1994) Exendin-4 and exendin-(9-39)NH2: agonist and antagonist, respectively, at the rat parietal cell receptor for glucagon-like peptide-1-(7-36)NH2 Eur. J. Pharmacol. 269, 183-191
    • (1994) Eur. J. Pharmacol. , vol.269 , pp. 183
    • Schepp, W.1    Schmidtler, J.2    Riedel, T.3    Dehne, K.4    Schusdziarra, V.5    Holst, J.J.6    Eng, J.7    Raufman, J.P.8    Classen, M.9
  • 8
    • 0029958404 scopus 로고    scopus 로고
    • Glucose intolerance but normal satiety in mice with a null mutation in the glucagon-like peptide 1 receptor gene
    • Scrocchi, L. A., Brown, T. J., MaClusky, N., Brubaker, P. L., Auerbach, A. B., Joyner, A. L., and Drucker, D. J. (1996) Glucose intolerance but normal satiety in mice with a null mutation in the glucagon-like peptide 1 receptor gene Nat. Med. 2, 1254-1258
    • (1996) Nat. Med. , vol.2 , pp. 1254
    • Scrocchi, L.A.1    Brown, T.J.2    MacLusky, N.3    Brubaker, P.L.4    Auerbach, A.B.5    Joyner, A.L.6    Drucker, D.J.7
  • 10
    • 33748319404 scopus 로고    scopus 로고
    • Lymphocytic infiltration and immune activation in metallothionein promoter-exendin-4 (MT-Exendin) transgenic mice
    • Baggio, L. L., Holland, D., Wither, J., and Drucker, D. J. (2006) Lymphocytic infiltration and immune activation in metallothionein promoter-exendin-4 (MT-Exendin) transgenic mice Diabetes 55, 1562-1570
    • (2006) Diabetes , vol.55 , pp. 1562
    • Baggio, L.L.1    Holland, D.2    Wither, J.3    Drucker, D.J.4
  • 11
    • 54449098531 scopus 로고    scopus 로고
    • Exendin-(9-39) corrects fasting hypoglycemia in SUR-1-/- mice by lowering cAMP in pancreatic beta-cells and inhibiting insulin secretion
    • De Leon, D. D., Li, C., Delson, M. I., Matschinsky, F. M., Stanley, C. A., and Stoffers, D. A. (2008) Exendin-(9-39) corrects fasting hypoglycemia in SUR-1-/- mice by lowering cAMP in pancreatic beta-cells and inhibiting insulin secretion J. Biol. Chem. 283, 25786-25793
    • (2008) J. Biol. Chem. , vol.283 , pp. 25786
    • De Leon, D.D.1    Li, C.2    Delson, M.I.3    Matschinsky, F.M.4    Stanley, C.A.5    Stoffers, D.A.6
  • 13
    • 18844412634 scopus 로고    scopus 로고
    • Chronic treatment with exendin(9-39)amide indicates a minor role for endogenous glucagon-like peptide-1 in metabolic abnormalities of obesity-related diabetes in ob/ob mice
    • Green, B. D., Irwin, N., Gault, V. A., Bailey, C. J., O'Harte, F. P., and Flatt, P. R. (2005) Chronic treatment with exendin(9-39)amide indicates a minor role for endogenous glucagon-like peptide-1 in metabolic abnormalities of obesity-related diabetes in ob/ob mice J. Endocrinol. 185, 307-317
    • (2005) J. Endocrinol. , vol.185 , pp. 307
    • Green, B.D.1    Irwin, N.2    Gault, V.A.3    Bailey, C.J.4    O'Harte, F.P.5    Flatt, P.R.6
  • 14
    • 58149330670 scopus 로고    scopus 로고
    • Mary, Mary, quite contrary, how do your beta-cells fail
    • 2564
    • Leahy, J. L. (2008) Mary, Mary, quite contrary, how do your beta-cells fail Diabetes 57, 2563-2564
    • (2008) Diabetes , vol.57 , pp. 2563
    • Leahy, J.L.1
  • 15
    • 45549086826 scopus 로고    scopus 로고
    • Crystal structure of the ligand-bound glucagon-like peptide-1 receptor extracellular domain
    • Runge, S., Thogersen, H., Madsen, K., Lau, J., and Rudolph, R. (2008) Crystal structure of the ligand-bound glucagon-like peptide-1 receptor extracellular domain J. Biol. Chem. 283, 11340-11347
    • (2008) J. Biol. Chem. , vol.283 , pp. 11340
    • Runge, S.1    Thogersen, H.2    Madsen, K.3    Lau, J.4    Rudolph, R.5
  • 16
    • 73649107900 scopus 로고    scopus 로고
    • Crystal structure of glucagon-like peptide-1 in complex with the extracellular domain of the glucagon-like peptide-1 receptor
    • 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
    • (2010) J. Biol. Chem. , vol.285 , pp. 723
    • Underwood, C.R.1    Garibay, P.2    Knudsen, L.B.3    Hastrup, S.4    Peters, G.H.5    Rudolph, R.6    Reedtz-Runge, S.7
  • 17
    • 56949096744 scopus 로고    scopus 로고
    • Molecular modeling of the three-dimensional structure of GLP-1R and its interactions with several agonists
    • Lin, F. and Wang, R. (2009) Molecular modeling of the three-dimensional structure of GLP-1R and its interactions with several agonists J. Mol. Model. 15, 53-65
    • (2009) J. Mol. Model. , vol.15 , pp. 53
    • Lin, F.1    Wang, R.2
  • 19
    • 0037349103 scopus 로고    scopus 로고
    • Different domains of the glucagon and glucagon-like peptide-1 receptors provide the critical determinants of ligand selectivity
    • Runge, S., Wulff, B. S., Madsen, K., Brauner-Osborne, H., and Knudsen, L. B. (2003) Different domains of the glucagon and glucagon-like peptide-1 receptors provide the critical determinants of ligand selectivity Br. J. Pharmacol. 138, 787-794
    • (2003) Br. J. Pharmacol. , vol.138 , pp. 787
    • Runge, S.1    Wulff, B.S.2    Madsen, K.3    Brauner-Osborne, H.4    Knudsen, L.B.5
  • 20
    • 34248563781 scopus 로고    scopus 로고
    • Differential structural properties of GLP-1 and exendin-4 determine their relative affinity for the GLP-1 receptor N-terminal extracellular domain
    • Runge, S., Schimmer, S., Oschmann, J., Schiodt, C. B., Knudsen, S. M., Jeppesen, C. B., Madsen, K., Lau, J., Thogersen, H., and Rudolph, R. (2007) Differential structural properties of GLP-1 and exendin-4 determine their relative affinity for the GLP-1 receptor N-terminal extracellular domain Biochemistry 46, 5830-5840
    • (2007) Biochemistry , vol.46 , pp. 5830
    • Runge, S.1    Schimmer, S.2    Oschmann, J.3    Schiodt, C.B.4    Knudsen, S.M.5    Jeppesen, C.B.6    Madsen, K.7    Lau, J.8    Thogersen, H.9    Rudolph, R.10
  • 21
    • 0037518197 scopus 로고    scopus 로고
    • The isolated N-terminal domain of the glucagon-like peptide-1 (GLP-1) receptor binds exendin peptides with much higher affinity than GLP-1
    • Lopez de Maturana, R., Willshaw, A., Kuntzsch, A., Rudolph, R., and Donnelly, D. (2003) The isolated N-terminal domain of the glucagon-like peptide-1 (GLP-1) receptor binds exendin peptides with much higher affinity than GLP-1 J. Biol. Chem. 278, 10195-10200
    • (2003) J. Biol. Chem. , vol.278 , pp. 10195
    • Lopez De Maturana, R.1    Willshaw, A.2    Kuntzsch, A.3    Rudolph, R.4    Donnelly, D.5
  • 22
    • 0030602177 scopus 로고    scopus 로고
    • The isolated N-terminal extracellular domain of the glucagon-like peptide-1 (GLP)-1 receptor has intrinsic binding activity
    • Wilmen, A., Goke, B., and Goke, R. (1996) The isolated N-terminal extracellular domain of the glucagon-like peptide-1 (GLP)-1 receptor has intrinsic binding activity FEBS Lett. 398, 43-47
    • (1996) FEBS Lett. , vol.398 , pp. 43
    • Wilmen, A.1    Goke, B.2    Goke, R.3
  • 23
    • 0030607672 scopus 로고    scopus 로고
    • Glucagon-like peptide-1-(9-36) amide is a major metabolite of glucagon-like peptide-1-(7-36) amide after in vivo administration to dogs, and it acts as an antagonist on the pancreatic receptor
    • Knudsen, L. B. and Pridal, L. (1996) Glucagon-like peptide-1-(9-36) amide is a major metabolite of glucagon-like peptide-1-(7-36) amide after in vivo administration to dogs, and it acts as an antagonist on the pancreatic receptor Eur. J. Pharmacol. 318, 429-435
    • (1996) Eur. J. Pharmacol. , vol.318 , pp. 429
    • Knudsen, L.B.1    Pridal, L.2
  • 24
    • 0038359686 scopus 로고    scopus 로고
    • Effects of GLP-1-(7-36)NH2, GLP-1-(7-37), and GLP-1-(9-36)NH2 on intravenous glucose tolerance and glucose-induced insulin secretion in healthy humans
    • Vahl, T. P., Paty, B. W., Fuller, B. D., Prigeon, R. L., and D'Alessio, D. A. (2003) Effects of GLP-1-(7-36)NH2, GLP-1-(7-37), and GLP-1-(9-36)NH2 on intravenous glucose tolerance and glucose-induced insulin secretion in healthy humans J. Clin. Endocrinol. Metab. 88, 1772-1779
    • (2003) J. Clin. Endocrinol. Metab. , vol.88 , pp. 1772
    • Vahl, T.P.1    Paty, B.W.2    Fuller, B.D.3    Prigeon, R.L.4    D'Alessio, D.A.5
  • 25
    • 37849026464 scopus 로고    scopus 로고
    • Structure-activity and protraction relationship of long-acting glucagon-like peptide-1 derivatives: Importance of fatty acid length, polarity, and bulkiness
    • Madsen, K., Knudsen, L. B., Agersoe, H., Nielsen, P. F., Thogersen, H., Wilken, M., and Johansen, N. L. (2007) Structure-activity and protraction relationship of long-acting glucagon-like peptide-1 derivatives: importance of fatty acid length, polarity, and bulkiness J. Med. Chem. 50, 6126-6132
    • (2007) J. Med. Chem. , vol.50 , pp. 6126
    • Madsen, K.1    Knudsen, L.B.2    Agersoe, H.3    Nielsen, P.F.4    Thogersen, H.5    Wilken, M.6    Johansen, N.L.7
  • 26
    • 0037299115 scopus 로고    scopus 로고
    • Effects of the novel (Pro3)GIP antagonist and exendin(9-39)amide on GIP- and GLP-1-induced cyclic AMP generation, insulin secretion and postprandial insulin release in obese diabetic (ob/ob) mice: Evidence that GIP is the major physiological incretin
    • Gault, V. A., O'Harte, F. P., Harriott, P., Mooney, M. H., Green, B. D., and Flatt, P. R. (2003) Effects of the novel (Pro3)GIP antagonist and exendin(9-39)amide on GIP- and GLP-1-induced cyclic AMP generation, insulin secretion and postprandial insulin release in obese diabetic (ob/ob) mice: evidence that GIP is the major physiological incretin Diabetologia 46, 222-230
    • (2003) Diabetologia , vol.46 , pp. 222
    • Gault, V.A.1    O'Harte, F.P.2    Harriott, P.3    Mooney, M.H.4    Green, B.D.5    Flatt, P.R.6
  • 27
    • 0036132087 scopus 로고    scopus 로고
    • Medium-dependence of the secondary structure of exendin-4 and glucagon-like-peptide-1
    • Andersen, N. H., Brodsky, Y., Neidigh, J. W., and Prickett, K. S. (2002) Medium-dependence of the secondary structure of exendin-4 and glucagon-like-peptide-1 Bioorg. Med. Chem. 10, 79-85
    • (2002) Bioorg. Med. Chem. , vol.10 , pp. 79
    • Andersen, N.H.1    Brodsky, Y.2    Neidigh, J.W.3    Prickett, K.S.4
  • 28
    • 0028883257 scopus 로고
    • Reduction of the incretin effect in rats by the glucagon-like peptide 1 receptor antagonist exendin (9-39) amide
    • Kolligs, F., Fehmann, H. C., Goke, R., and Goke, B. (1995) Reduction of the incretin effect in rats by the glucagon-like peptide 1 receptor antagonist exendin (9-39) amide Diabetes 44, 16-19
    • (1995) Diabetes , vol.44 , pp. 16
    • Kolligs, F.1    Fehmann, H.C.2    Goke, R.3    Goke, B.4
  • 31
    • 0000385121 scopus 로고    scopus 로고
    • Exendin(9-39)amide is an antagonist of glucagon-like peptide-1(7-36)amide in humans
    • Schirra, J., Sturm, K., Leicht, P., Arnold, R., Goke, B., and Katschinski, M. (1998) Exendin(9-39)amide is an antagonist of glucagon-like peptide-1(7-36)amide in humans J. Clin. Invest. 101, 1421-1430
    • (1998) J. Clin. Invest. , vol.101 , pp. 1421
    • Schirra, J.1    Sturm, K.2    Leicht, P.3    Arnold, R.4    Goke, B.5    Katschinski, M.6
  • 35
    • 79751495037 scopus 로고    scopus 로고
    • Charge inversion at position 68 of the glucagon and glucagon-like peptide-1 receptors supports selectivity in hormone action
    • In press.
    • Day, J. W., Li, P., Patterson, J. T., Chabenne, J., DiMarchi Chabenne, M., Gelfanov, V., and DiMarchi, R. Charge inversion at position 68 of the glucagon and glucagon-like peptide-1 receptors supports selectivity in hormone action, J. Pept. Sci. In press.
    • J. Pept. Sci.
    • Day, J.W.1    Li, P.2    Patterson, J.T.3    Chabenne, J.4    Dimarchi Chabenne, M.5    Gelfanov, V.6    Dimarchi, R.7
  • 36
    • 0026486811 scopus 로고
    • In situ neutralization in Boc-chemistry solid phase peptide synthesis. Rapid, high yield assembly of difficult sequences
    • Schnolzer, M., Alewood, P., Jones, A., Alewood, D., and Kent, S. B. (1992) In situ neutralization in Boc-chemistry solid phase peptide synthesis. Rapid, high yield assembly of difficult sequences Int. J. Pept. Protein Res. 40, 180-193
    • (1992) Int. J. Pept. Protein Res. , vol.40 , pp. 180
    • Schnolzer, M.1    Alewood, P.2    Jones, A.3    Alewood, D.4    Kent, S.B.5
  • 37
    • 1542470485 scopus 로고    scopus 로고
    • Quantitative magnetic resonance (QMR) method for bone and whole-body-composition analysis
    • Taicher, G. Z., Tinsley, F. C., Reiderman, A., and Heiman, M. L. (2003) Quantitative magnetic resonance (QMR) method for bone and whole-body-composition analysis Anal. Bioanal. Chem. 377, 990-1002
    • (2003) Anal. Bioanal. Chem. , vol.377 , pp. 990
    • Taicher, G.Z.1    Tinsley, F.C.2    Reiderman, A.3    Heiman, M.L.4


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