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Volumn 136, Issue , 2017, Pages 99-108

Characterization of signal bias at the GLP-1 receptor induced by backbone modification of GLP-1

Author keywords

Biased agonism; Cell signaling; G protein coupled receptor; Glucagon like peptide 1 receptor; Peptides

Indexed keywords

ALPHA AMINO ACID; BETA AMINO ACID; BETA ARRESTIN 1; BETA ARRESTIN 2; CALCIUM; CYCLIC AMP; GLUCAGON LIKE PEPTIDE 1; GLUCAGON LIKE PEPTIDE 1 RECEPTOR; GUANINE NUCLEOTIDE BINDING PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; PEPTIDE FRAGMENT;

EID: 85017351662     PISSN: 00062952     EISSN: 18732968     Source Type: Journal    
DOI: 10.1016/j.bcp.2017.03.018     Document Type: Article
Times cited : (51)

References (46)
  • 1
    • 84955749058 scopus 로고    scopus 로고
    • Pathophysiology of type 1 and type 2 diabetes mellitus: a 90-year perspective
    • Zaccardi, F., Webb, D.R., Yates, T., Davies, M.J., Pathophysiology of type 1 and type 2 diabetes mellitus: a 90-year perspective. Postgrad. Med. J. 92 (2016), 63–69.
    • (2016) Postgrad. Med. J. , vol.92 , pp. 63-69
    • Zaccardi, F.1    Webb, D.R.2    Yates, T.3    Davies, M.J.4
  • 2
    • 0026572747 scopus 로고
    • Pathogensis of Type 2 (non-insulin dependent) diabetes mellitus: a balanced overview
    • DeFronzo, R.A., Pathogensis of Type 2 (non-insulin dependent) diabetes mellitus: a balanced overview. Diabetologia 35 (1992), 389–397.
    • (1992) Diabetologia , vol.35 , pp. 389-397
    • DeFronzo, R.A.1
  • 3
    • 0041736553 scopus 로고    scopus 로고
    • Metformin: new understandings, new uses
    • Hundal, R.S., Inzucchi, S.E., Metformin: new understandings, new uses. Drugs 63 (2003), 1879–1894.
    • (2003) Drugs , vol.63 , pp. 1879-1894
    • Hundal, R.S.1    Inzucchi, S.E.2
  • 5
    • 79959781838 scopus 로고    scopus 로고
    • Loss of incretin effect is a specific, important, and early characteristic of type 2 diabetes
    • Holst, J.J., Knop, F.K., Vilsboll, T., Krarup, T., Madsbad, S., Loss of incretin effect is a specific, important, and early characteristic of type 2 diabetes. Diabetes Care 34:Suppl 2 (2011), S251–257.
    • (2011) Diabetes Care , vol.34 , pp. S251-257
    • Holst, J.J.1    Knop, F.K.2    Vilsboll, T.3    Krarup, T.4    Madsbad, S.5
  • 6
    • 34248223285 scopus 로고    scopus 로고
    • (2007) Biology of incretins: GLP-1 and GIP
    • Baggio, L.L., Drucker, D.J., (2007) Biology of incretins: GLP-1 and GIP. Gastroenterology 132 (2007), 2131–2157.
    • (2007) Gastroenterology , vol.132 , pp. 2131-2157
    • Baggio, L.L.1    Drucker, D.J.2
  • 7
    • 0032941026 scopus 로고    scopus 로고
    • Pancreatic glucagon-like peptide-1 receptor couples to multiple G proteins and activates mitogen-activated protein kinase pathways in chinese hamster ovary cells
    • Montrose-Rafizadeh, C., Avdonin, P., Garant, M.J., Rodgers, B.D., Kole, S., Yang, H., et al. Pancreatic glucagon-like peptide-1 receptor couples to multiple G proteins and activates mitogen-activated protein kinase pathways in chinese hamster ovary cells. Endocrinology 140 (1999), 132–1140.
    • (1999) Endocrinology , vol.140 , pp. 132-1140
    • Montrose-Rafizadeh, C.1    Avdonin, P.2    Garant, M.J.3    Rodgers, B.D.4    Kole, S.5    Yang, H.6
  • 8
    • 0035831283 scopus 로고    scopus 로고
    • Different domains in the third intracellular loop of the GLP-1 receptor are responsible for Gas and Gai/Gao activation
    • Hallbrink, M., Homqvist, T., Olsson, M., Ostenson, C.-G., Efendic, S., Langel, U., Different domains in the third intracellular loop of the GLP-1 receptor are responsible for Gas and Gai/Gao activation. Bichim. Biophys. Acta 1546 (2001), 79–86.
    • (2001) Bichim. Biophys. Acta , vol.1546 , pp. 79-86
    • Hallbrink, M.1    Homqvist, T.2    Olsson, M.3    Ostenson, C.-G.4    Efendic, S.5    Langel, U.6
  • 9
    • 84975229526 scopus 로고    scopus 로고
    • The extracellular surface of the GLP-1 receptor is a molecular trigger for biased agonism
    • Wootten, D., Reynolds, C.A., Smith, K.J., Mobarec, J.C., Koole, C., Savage, E.E., et al. The extracellular surface of the GLP-1 receptor is a molecular trigger for biased agonism. Cell 165 (2016), 1632–1643.
    • (2016) Cell , vol.165 , pp. 1632-1643
    • Wootten, D.1    Reynolds, C.A.2    Smith, K.J.3    Mobarec, J.C.4    Koole, C.5    Savage, E.E.6
  • 10
    • 34250714898 scopus 로고    scopus 로고
    • Oxyntomodulin differentially affects glucagon-like peptide-1 receptor beta-arrestin recruitment and signaling through Galpha(s)
    • Jorgensen, R., Kubale, V., Vrecl, M., Schwartz, T.W., Elling, C.E., Oxyntomodulin differentially affects glucagon-like peptide-1 receptor beta-arrestin recruitment and signaling through Galpha(s). J. Pharmaocl. Exp. Ther. 322 (2007), 148–154.
    • (2007) J. Pharmaocl. Exp. Ther. , vol.322 , pp. 148-154
    • Jorgensen, R.1    Kubale, V.2    Vrecl, M.3    Schwartz, T.W.4    Elling, C.E.5
  • 11
    • 44349129654 scopus 로고    scopus 로고
    • Beta-Arrestin-1 mediates glucagon-like peptide-1 signaling to insulin secretion in cultured pancreatic beta cells
    • Sonoda, N., Imamura, T., Yoshizaki, T., Babendure, J.L., Lu, J.C., Olefsky, J.M., Beta-Arrestin-1 mediates glucagon-like peptide-1 signaling to insulin secretion in cultured pancreatic beta cells. Proc. Natl. Acad. Sci. U.S.A. 105 (2008), 6614–6619.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 6614-6619
    • Sonoda, N.1    Imamura, T.2    Yoshizaki, T.3    Babendure, J.L.4    Lu, J.C.5    Olefsky, J.M.6
  • 12
    • 76249122645 scopus 로고    scopus 로고
    • GLP-1 mediates antiapoptotic effect by phosphorylating Bad through a beta-arrestin 1-mediated ERK1/2 activation in pancreatic beta-cells
    • Quoyer, J., Longuet, C., Broca, C., Linck, N., Costes, S., Varin, E., et al. GLP-1 mediates antiapoptotic effect by phosphorylating Bad through a beta-arrestin 1-mediated ERK1/2 activation in pancreatic beta-cells. J. Biol. Chem. 285 (2010), 1989–2002.
    • (2010) J. Biol. Chem. , vol.285 , pp. 1989-2002
    • Quoyer, J.1    Longuet, C.2    Broca, C.3    Linck, N.4    Costes, S.5    Varin, E.6
  • 13
    • 77951844975 scopus 로고    scopus 로고
    • Teaching old receptors new tricks: biasing seven-transmembrane receptors
    • Rajagopal, S., Rajagopal, K., Lefkowitz, R.J., Teaching old receptors new tricks: biasing seven-transmembrane receptors. Nat. Rev. Drug Discov. 9 (2010), 373–386.
    • (2010) Nat. Rev. Drug Discov. , vol.9 , pp. 373-386
    • Rajagopal, S.1    Rajagopal, K.2    Lefkowitz, R.J.3
  • 14
    • 84855901533 scopus 로고    scopus 로고
    • Molecular mechanism of beta-arrestin-biased agonism at seven-transmembrane receptors
    • Reiter, E., Ahn, S., Shukla, A.K., Lefkowitz, R.J., Molecular mechanism of beta-arrestin-biased agonism at seven-transmembrane receptors. Annu. Rev. Pharmacol. Toxicol. 52 (2002), 179–197.
    • (2002) Annu. Rev. Pharmacol. Toxicol. , vol.52 , pp. 179-197
    • Reiter, E.1    Ahn, S.2    Shukla, A.K.3    Lefkowitz, R.J.4
  • 15
    • 84875227396 scopus 로고    scopus 로고
    • Signalling bias in new drug discovery: detection, quantification and therapeutic impact
    • Kenakin, T., Christopoulos, A., Signalling bias in new drug discovery: detection, quantification and therapeutic impact. Nat. Rev. Drug Discov. 12 (2013), 205–216.
    • (2013) Nat. Rev. Drug Discov. , vol.12 , pp. 205-216
    • Kenakin, T.1    Christopoulos, A.2
  • 16
    • 34447633368 scopus 로고    scopus 로고
    • Conformational complexity of G-protein-coupled receptors
    • Kobilka, B.K., Deupi, X., Conformational complexity of G-protein-coupled receptors. Trends Pharmacol. Sci. 28 (2007), 397–406.
    • (2007) Trends Pharmacol. Sci. , vol.28 , pp. 397-406
    • Kobilka, B.K.1    Deupi, X.2
  • 17
    • 0043235844 scopus 로고    scopus 로고
    • Ligand-selective receptor conformations revisited: the promise and the problem
    • Kenakin, T., Ligand-selective receptor conformations revisited: the promise and the problem. Trends Pharmacol. Sci. 24 (2003), 346–354.
    • (2003) Trends Pharmacol. Sci. , vol.24 , pp. 346-354
    • Kenakin, T.1
  • 18
    • 79952488185 scopus 로고    scopus 로고
    • Therapeutic potential of beta-arrestin- and G protein-biased agonists
    • Whalen, E.J., Rajagopal, S., Lefkowitz, R.J., Therapeutic potential of beta-arrestin- and G protein-biased agonists. Trends Mol. Med. 17 (2011), 126–139.
    • (2011) Trends Mol. Med. , vol.17 , pp. 126-139
    • Whalen, E.J.1    Rajagopal, S.2    Lefkowitz, R.J.3
  • 19
    • 84878543842 scopus 로고    scopus 로고
    • Emergent biological properties of arrestin pathway-selective biased agonism
    • Appleton, K.M., Luttrell, L.M., Emergent biological properties of arrestin pathway-selective biased agonism. J. Recept. Signal Transduct. Res. 33 (2013), 153–161.
    • (2013) J. Recept. Signal Transduct. Res. , vol.33 , pp. 153-161
    • Appleton, K.M.1    Luttrell, L.M.2
  • 20
    • 77956249652 scopus 로고    scopus 로고
    • Allosteric ligands of the glucagon-like peptide 1 receptor (GLP-1R) differentially modulate endogenous and exogenous peptide responses in a pathway-selective manner: implications for drug screening
    • Koole, C., Wootten, D., Simms, J., Valant, C., Sridhar, R., Woodman, O.L., et al. Allosteric ligands of the glucagon-like peptide 1 receptor (GLP-1R) differentially modulate endogenous and exogenous peptide responses in a pathway-selective manner: implications for drug screening. Mol. Pharmacol. 78 (2010), 456–465.
    • (2010) Mol. Pharmacol. , vol.78 , pp. 456-465
    • Koole, C.1    Wootten, D.2    Simms, J.3    Valant, C.4    Sridhar, R.5    Woodman, O.L.6
  • 21
    • 84875426039 scopus 로고    scopus 로고
    • Differential activation and modulation of the glucagon-like peptide-1 receptor by small molecule ligands
    • Wootten, D., Savage, E.E., Willard, F.S., Bueno, A.B., Sloop, K.W., Christopoulos, A., et al. Differential activation and modulation of the glucagon-like peptide-1 receptor by small molecule ligands. Mol. Pharmacol. 83 (2013), 822–834.
    • (2013) Mol. Pharmacol. , vol.83 , pp. 822-834
    • Wootten, D.1    Savage, E.E.2    Willard, F.S.3    Bueno, A.B.4    Sloop, K.W.5    Christopoulos, A.6
  • 23
    • 84948843969 scopus 로고    scopus 로고
    • Autocrine selection of a GLP-1R G-protein biased agonist with potent antidiabetic effects
    • Zhang, H., Sturchler, E., Zhu, J., Nieto, A., Cistrone, P.A., Xie, J., et al. Autocrine selection of a GLP-1R G-protein biased agonist with potent antidiabetic effects. Nat. Commun., 6, 2015, 8918.
    • (2015) Nat. Commun. , vol.6 , pp. 8918
    • Zhang, H.1    Sturchler, E.2    Zhu, J.3    Nieto, A.4    Cistrone, P.A.5    Xie, J.6
  • 24
    • 84996490641 scopus 로고    scopus 로고
    • Beta-arrestin-biased agonists of the GLP-1 receptor from beta-amino acid residue incorporation into GLP-1 analogues
    • Hager, M.V., Johnson, L.M., Wootten, D., Sexton, P.M., Gellman, S.H., Beta-arrestin-biased agonists of the GLP-1 receptor from beta-amino acid residue incorporation into GLP-1 analogues. J. Am. Chem. Soc. 138 (2016), 14970–14979.
    • (2016) J. Am. Chem. Soc. , vol.138 , pp. 14970-14979
    • Hager, M.V.1    Johnson, L.M.2    Wootten, D.3    Sexton, P.M.4    Gellman, S.H.5
  • 25
    • 84875533946 scopus 로고    scopus 로고
    • Polar transmembrane interactions drive formation of ligand-specific and signal pathway-biased family B G protein-coupled receptor conformations
    • Wootten, D., Simms, J., Miller, L.J., Christopoulos, A., Sexton, P.M., Polar transmembrane interactions drive formation of ligand-specific and signal pathway-biased family B G protein-coupled receptor conformations. Proc. Natl. Acad. Sci. U.S.A. 110 (2013), 5211–5216.
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 5211-5216
    • Wootten, D.1    Simms, J.2    Miller, L.J.3    Christopoulos, A.4    Sexton, P.M.5
  • 28
    • 84959036712 scopus 로고    scopus 로고
    • A new GLP-1 analogue with prolonged glucose-lowering activity in vivo via backbone-based modification at the N-terminus
    • Bai, X., Niu, Y., Zhu, J., Yang, A.Q., Wu, Y.F., Ye, X.S., A new GLP-1 analogue with prolonged glucose-lowering activity in vivo via backbone-based modification at the N-terminus. Bioorg. Med. Chem. 24 (2016), 1163–1170.
    • (2016) Bioorg. Med. Chem. , vol.24 , pp. 1163-1170
    • Bai, X.1    Niu, Y.2    Zhu, J.3    Yang, A.Q.4    Wu, Y.F.5    Ye, X.S.6
  • 29
    • 0037172821 scopus 로고    scopus 로고
    • Structure-function studies of analogues of parathyroid hormone (PTH)-1-34 containing beta-amino acid residues in positions 11–13
    • Peggion, E., Mammi, S., Schievano, E., Silvestri, L., Schiebler, L., Bisello, A., et al. Structure-function studies of analogues of parathyroid hormone (PTH)-1-34 containing beta-amino acid residues in positions 11–13. Biochemistry 41 (2002), 8162–8175.
    • (2002) Biochemistry , vol.41 , pp. 8162-8175
    • Peggion, E.1    Mammi, S.2    Schievano, E.3    Silvestri, L.4    Schiebler, L.5    Bisello, A.6
  • 30
    • 0348111261 scopus 로고    scopus 로고
    • Conformational and biological characterization of human parathyroid hormone hPTH(1–34) analogues containing beta-amino acid residues in positions 17–19
    • Schievano, E., Mammi, S., Carretta, E., Fiori, N., Corich, M., Bisello, A., et al. Conformational and biological characterization of human parathyroid hormone hPTH(1–34) analogues containing beta-amino acid residues in positions 17–19. Biopolymers 70 (2003), 534–547.
    • (2003) Biopolymers , vol.70 , pp. 534-547
    • Schievano, E.1    Mammi, S.2    Carretta, E.3    Fiori, N.4    Corich, M.5    Bisello, A.6
  • 31
    • 84903964236 scopus 로고    scopus 로고
    • Backbone modification of a polypeptide drug alters duration of action in vivo
    • Cheloha, R.W., Maeda, A., Dean, T., Gardella, T.J., Gellman, S.H., Backbone modification of a polypeptide drug alters duration of action in vivo. Nat. Biotechnol. 32 (2014), 653–655.
    • (2014) Nat. Biotechnol. , vol.32 , pp. 653-655
    • Cheloha, R.W.1    Maeda, A.2    Dean, T.3    Gardella, T.J.4    Gellman, S.H.5
  • 32
    • 84949949615 scopus 로고    scopus 로고
    • Selective VIP receptor agonists facilitate immune transformation for dopaminergic neuroprotection in MPTP-intoxicated mice
    • Olson, K.E., Kosloski-Bilek, L.M., Anderson, K.M., Diggs, B.J., Clark, B.E., Gledhill, J.M. Jr, et al. Selective VIP receptor agonists facilitate immune transformation for dopaminergic neuroprotection in MPTP-intoxicated mice. J. Neurosci. 35 (2015), 16463–16478.
    • (2015) J. Neurosci. , vol.35 , pp. 16463-16478
    • Olson, K.E.1    Kosloski-Bilek, L.M.2    Anderson, K.M.3    Diggs, B.J.4    Clark, B.E.5    Gledhill, J.M.6
  • 33
    • 84992189589 scopus 로고    scopus 로고
    • Backbone modification of a parathyroid hormone receptor-1 antagonist/inverse agonist
    • Cheloha, R.W., Watanabe, T., Dean, T., Gellman, S.H., Gardella, T.J., Backbone modification of a parathyroid hormone receptor-1 antagonist/inverse agonist. ACS Chem. Biol. 11 (2016), 2752–2762.
    • (2016) ACS Chem. Biol. , vol.11 , pp. 2752-2762
    • Cheloha, R.W.1    Watanabe, T.2    Dean, T.3    Gellman, S.H.4    Gardella, T.J.5
  • 34
  • 36
    • 84856731249 scopus 로고    scopus 로고
    • Second extracellular loop of human glucagon-like peptide-1 receptor (GLP-1R) has a critical role in GLP-1 peptide binding and receptor activation
    • Koole, C., Wootten, D., Simms, J., Miller, L.J., Christopoulos, A., Sexton, P.M., Second extracellular loop of human glucagon-like peptide-1 receptor (GLP-1R) has a critical role in GLP-1 peptide binding and receptor activation. J. Biol. Chem. 287 (2012), 3642–3658.
    • (2012) J. Biol. Chem. , vol.287 , pp. 3642-3658
    • Koole, C.1    Wootten, D.2    Simms, J.3    Miller, L.J.4    Christopoulos, A.5    Sexton, P.M.6
  • 37
    • 80051958802 scopus 로고    scopus 로고
    • Polymorphism and ligand dependent changes in human glucagon-like peptide-1 receptor (GLP-1R) function: allosteric rescue of loss of function mutation
    • Koole, C., Wootten, D., Simms, J., Valant, C., Miller, L.J., Christopoulos, A., et al. Polymorphism and ligand dependent changes in human glucagon-like peptide-1 receptor (GLP-1R) function: allosteric rescue of loss of function mutation. Mol. Pharmacol. 80 (2011), 486–497.
    • (2011) Mol. Pharmacol. , vol.80 , pp. 486-497
    • Koole, C.1    Wootten, D.2    Simms, J.3    Valant, C.4    Miller, L.J.5    Christopoulos, A.6
  • 38
    • 34547187191 scopus 로고    scopus 로고
    • Structure-function studies of allosteric agonism at M2 muscarinic acetylcholine receptors
    • May, L.T., Avlani, V.A., Langmead, C.J., Herdon, H.J., Wood, M.D., Sexton, P.M., et al. Structure-function studies of allosteric agonism at M2 muscarinic acetylcholine receptors. Mol. Pharmacol. 72 (2007), 463–476.
    • (2007) Mol. Pharmacol. , vol.72 , pp. 463-476
    • May, L.T.1    Avlani, V.A.2    Langmead, C.J.3    Herdon, H.J.4    Wood, M.D.5    Sexton, P.M.6
  • 39
    • 84876494666 scopus 로고    scopus 로고
    • A simple method to generate stable cell lines for the analysis of transient protein-protein interactions
    • Savage, E.E., Wootten, D., Christopoulos, A., Sexton, P.M., Furness, S.G., A simple method to generate stable cell lines for the analysis of transient protein-protein interactions. Biotechniques 54 (2013), 217–221.
    • (2013) Biotechniques , vol.54 , pp. 217-221
    • Savage, E.E.1    Wootten, D.2    Christopoulos, A.3    Sexton, P.M.4    Furness, S.G.5
  • 41
    • 14844321939 scopus 로고    scopus 로고
    • Characterization of glucagon-like peptide-1 receptor beta-arrestin 2 interaction: a high-affinity receptor phenotype
    • Jorgensen, R., Martini, L., Schwartz, T.W., Elling, C.E., Characterization of glucagon-like peptide-1 receptor beta-arrestin 2 interaction: a high-affinity receptor phenotype. Mol. Endocrinol. 19 (2005), 812–823.
    • (2005) Mol. Endocrinol. , vol.19 , pp. 812-823
    • Jorgensen, R.1    Martini, L.2    Schwartz, T.W.3    Elling, C.E.4
  • 42
    • 0027164996 scopus 로고
    • Functional expression of the rat glucagon-like peptide-1 receptor, and evidence for coupling to both adenylyl cyclase, and phospholipase-C
    • Wheeler, M.B., Lu, M., Dillon, J.S., Leng, X.-H., Chen, C., Boyd, A.E., Functional expression of the rat glucagon-like peptide-1 receptor, and evidence for coupling to both adenylyl cyclase, and phospholipase-C. Endocrinology 133 (1993), 57–62.
    • (1993) Endocrinology , vol.133 , pp. 57-62
    • Wheeler, M.B.1    Lu, M.2    Dillon, J.S.3    Leng, X.-H.4    Chen, C.5    Boyd, A.E.6
  • 43
    • 0347990624 scopus 로고    scopus 로고
    • Epac: a new cAMP-binding protein in support of glucagon-like peptide-1 receptor-mediated signal transduction in the pancreatic beta-cell
    • Holz, G.G., Epac: a new cAMP-binding protein in support of glucagon-like peptide-1 receptor-mediated signal transduction in the pancreatic beta-cell. Diabetes 53 (2004), 5–13.
    • (2004) Diabetes , vol.53 , pp. 5-13
    • Holz, G.G.1
  • 44
    • 84919740425 scopus 로고    scopus 로고
    • Agonist-induced internalisation of the glucagon-like peptide-1 receptor is mediated by the Galphaq pathway
    • Thompson, A., Kanamarlapudi, V., Agonist-induced internalisation of the glucagon-like peptide-1 receptor is mediated by the Galphaq pathway. Biochem. Pharmacol. 93 (2015), 72–84.
    • (2015) Biochem. Pharmacol. , vol.93 , pp. 72-84
    • Thompson, A.1    Kanamarlapudi, V.2
  • 45
    • 0021058380 scopus 로고
    • Operational models of pharmacological agonism
    • Black, J.W., Leff, P., Operational models of pharmacological agonism. Proc. R. Soc. Lond. B Biol. Sci. 220 (1983), 141–162.
    • (1983) Proc. R. Soc. Lond. B Biol. Sci. , vol.220 , pp. 141-162
    • Black, J.W.1    Leff, P.2


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