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Volumn 17, Issue 11, 2003, Pages 2201-2210

High Constitutive Signaling of the Ghrelin Receptor - Identification of a Potent Inverse Agonist

Author keywords

[No Author keywords available]

Indexed keywords

APPETITE STIMULANT; GHRELIN; GHRELIN RECEPTOR; GHRELIN RECEPTOR STIMULATING AGENT; HORMONE ANTAGONIST; HORMONE RECEPTOR; HORMONE RECEPTOR STIMULATING AGENT; INOSITOL PHOSPHATE; MOTILIN; MOTILIN RECEPTOR; SUBSTANCE P [1 DEXTRO ARGININE 5 DEXTRO PHENYLALANINE 7,9 DEXTRO TRYPTOPHAN 11 LEUCINE]; SUBSTANCE P DERIVATIVE; UNCLASSIFIED DRUG;

EID: 0242330291     PISSN: 08888809     EISSN: None     Source Type: Journal    
DOI: 10.1210/me.2003-0069     Document Type: Article
Times cited : (437)

References (47)
  • 1
    • 0018899801 scopus 로고
    • Structure-activity relationships of a synthetic pentapeptide that specifically releases growth hormone in vitro
    • Bowers CY, Momany F, Reynolds GA, Chang D, Hong A, Chang K 1980 Structure-activity relationships of a synthetic pentapeptide that specifically releases growth hormone in vitro. Endocrinology 106:663-667
    • (1980) Endocrinology , vol.106 , pp. 663-667
    • Bowers, C.Y.1    Momany, F.2    Reynolds, G.A.3    Chang, D.4    Hong, A.5    Chang, K.6
  • 2
    • 0021322884 scopus 로고
    • On the in vitro and in vivo activity of a new synthetic hexapeptide that acts on the pituitary to specifically release growth hormone
    • Bowers CY, Momany FA, Reynolds GA, Hong A 1984 On the in vitro and in vivo activity of a new synthetic hexapeptide that acts on the pituitary to specifically release growth hormone. Endocrinology 114:1537-1545
    • (1984) Endocrinology , vol.114 , pp. 1537-1545
    • Bowers, C.Y.1    Momany, F.A.2    Reynolds, G.A.3    Hong, A.4
  • 7
    • 0033540056 scopus 로고    scopus 로고
    • Ghrelin is a growth-hormone-releasing acylated peptide from stomach
    • Kojima M, Hosoda H, Date Y, Nakazato M, Matsuo H, Kangawa K 1999 Ghrelin is a growth-hormone-releasing acylated peptide from stomach. Nature 402:656-660
    • (1999) Nature , vol.402 , pp. 656-660
    • Kojima, M.1    Hosoda, H.2    Date, Y.3    Nakazato, M.4    Matsuo, H.5    Kangawa, K.6
  • 8
    • 0346949031 scopus 로고    scopus 로고
    • Structural divergence of human ghrelin; identification of multiple ghrelin-derived molecules produced by post-translational processing
    • Hosoda H, Kojima M, Mizushima T, Shimizu S, Kangawa K 2002 Structural divergence of human ghrelin; identification of multiple ghrelin-derived molecules produced by post-translational processing. J Biol Chem 278:64-70
    • (2002) J Biol Chem , vol.278 , pp. 64-70
    • Hosoda, H.1    Kojima, M.2    Mizushima, T.3    Shimizu, S.4    Kangawa, K.5
  • 9
    • 0034676324 scopus 로고    scopus 로고
    • Structure-function studies on the new growth hormone-releasing peptide, ghrelin: Minimal sequence of ghrelin necessary for activation of growth hormone secretagogue receptor 1a
    • Bednarek MA, Feighner SD, Pong SS, McKee KK, Hreniuk DL, Silva MV, Warren VA, Howard AD, Van Der Ploeg LH, Heck JV 2000 Structure-function studies on the new growth hormone-releasing peptide, ghrelin: minimal sequence of ghrelin necessary for activation of growth hormone secretagogue receptor 1a. J Med Chem 43:4370-4376
    • (2000) J Med Chem , vol.43 , pp. 4370-4376
    • Bednarek, M.A.1    Feighner, S.D.2    Pong, S.S.3    McKee, K.K.4    Hreniuk, D.L.5    Silva, M.V.6    Warren, V.A.7    Howard, A.D.8    Van Der Ploeg, L.H.9    Heck, J.V.10
  • 11
    • 0034687376 scopus 로고    scopus 로고
    • Ghrelin induces adiposity in rodents
    • Tschop M, Smiley DL, Heiman ML 2000 Ghrelin induces adiposity in rodents. Nature 407:908-913
    • (2000) Nature , vol.407 , pp. 908-913
    • Tschop, M.1    Smiley, D.L.2    Heiman, M.L.3
  • 15
    • 0034802108 scopus 로고    scopus 로고
    • Minireview: Ghrelin and the regulation of energy balance - A hypothalamic perspective
    • Horvath TL, Diano S, Sotonyi P, Heiman M, Tschop M 2001 Minireview: ghrelin and the regulation of energy balance - a hypothalamic perspective. Endocrinology 142:4163-4169
    • (2001) Endocrinology , vol.142 , pp. 4163-4169
    • Horvath, T.L.1    Diano, S.2    Sotonyi, P.3    Heiman, M.4    Tschop, M.5
  • 16
    • 0035320623 scopus 로고    scopus 로고
    • Ghrelin: Discovery of the natural endogenous ligand for the growth hormone secretagogue receptor
    • Kojima M, Hosoda H, Matsuo H, Kangawa K 2001 Ghrelin: discovery of the natural endogenous ligand for the growth hormone secretagogue receptor. Trends Endocrinol Metab 12:118-122
    • (2001) Trends Endocrinol Metab , vol.12 , pp. 118-122
    • Kojima, M.1    Hosoda, H.2    Matsuo, H.3    Kangawa, K.4
  • 20
    • 0030966439 scopus 로고    scopus 로고
    • Motilin and clinical application
    • Itoh Z 1997 Motilin and clinical application. Peptides 18:593-608
    • (1997) Peptides , vol.18 , pp. 593-608
    • Itoh, Z.1
  • 21
    • 0033534718 scopus 로고    scopus 로고
    • Agonists and inverse agonists for the herpesvirus 8-encoded constitutively active seven-transmembrane oncogene product, ORF-74
    • Rosenkilde MM, Kledal TN, Brauner-Osborne H, Schwartz TW 1999 Agonists and inverse agonists for the herpesvirus 8-encoded constitutively active seven-transmembrane oncogene product, ORF-74. J Biol Chem 274:956-961
    • (1999) J Biol Chem , vol.274 , pp. 956-961
    • Rosenkilde, M.M.1    Kledal, T.N.2    Brauner-Osborne, H.3    Schwartz, T.W.4
  • 25
    • 0030598845 scopus 로고    scopus 로고
    • Solubilization and characterization of a growth hormone secretagogue receptor from porcine anterior pituitary membranes
    • Pomes A, Pong SS, Schaeffer JM 1996 Solubilization and characterization of a growth hormone secretagogue receptor from porcine anterior pituitary membranes. Biochem Biophys Res Commun 225:939-945
    • (1996) Biochem Biophys Res Commun , vol.225 , pp. 939-945
    • Pomes, A.1    Pong, S.S.2    Schaeffer, J.M.3
  • 26
    • 0035827631 scopus 로고    scopus 로고
    • Two active molecular phenotypes of the tachykinin NK1 receptor revealed by G-protein fusions and mutagenesis
    • Holst B, Hastrup H, Raffetseder U, Martini L, Schwartz TW 2001 Two active molecular phenotypes of the tachykinin NK1 receptor revealed by G-protein fusions and mutagenesis. J Biol Chem 276:19793-19799
    • (2001) J Biol Chem , vol.276 , pp. 19793-19799
    • Holst, B.1    Hastrup, H.2    Raffetseder, U.3    Martini, L.4    Schwartz, T.W.5
  • 27
    • 0028043957 scopus 로고
    • Mutations along transmembrane segment II of the NK-1 receptor affect substance P competition with non-peptide antagonists but not substance P binding
    • Rosenkilde MM, Cahir M, Gether U, Hjorth SA, Schwartz TW 1994 Mutations along transmembrane segment II of the NK-1 receptor affect substance P competition with non-peptide antagonists but not substance P binding. J Biol Chem 269:28160-28164
    • (1994) J Biol Chem , vol.269 , pp. 28160-28164
    • Rosenkilde, M.M.1    Cahir, M.2    Gether, U.3    Hjorth, S.A.4    Schwartz, T.W.5
  • 28
    • 9444267059 scopus 로고    scopus 로고
    • The CXC chemokines growth-regulated oncogene (GRO) α, GROβ, GROγ, neutrophil-activating peptide-2, and epithelial cell-derived neutrophil-activating peptide-78 are potent agonists for the type B, but not the type A, human interleukin-8 receptor
    • Ahuja SK, Murphy PM 1996 The CXC chemokines growth-regulated oncogene (GRO) α, GROβ, GROγ, neutrophil-activating peptide-2, and epithelial cell-derived neutrophil-activating peptide-78 are potent agonists for the type B, but not the type A, human interleukin-8 receptor. J Biol Chem 271:30545-20550
    • (1996) J Biol Chem , vol.271 , pp. 30545-20550
    • Ahuja, S.K.1    Murphy, P.M.2
  • 30
    • 0028800729 scopus 로고
    • Conversion of antagonist-binding site to metal-ion site in the tachykinin Nk-1 receptor
    • Elling CE, Nielsen SM, Schwartz TW 1995 Conversion of antagonist-binding site to metal-ion site in the tachykinin Nk-1 receptor. Nature 374:74-77
    • (1995) Nature , vol.374 , pp. 74-77
    • Elling, C.E.1    Nielsen, S.M.2    Schwartz, T.W.3
  • 31
    • 0033607270 scopus 로고    scopus 로고
    • Conversion of agonist site to metal-ion chelator site in the β(2)-adrenergic receptor
    • Elling CE, Thirstrup K, Holst B, Schwartz TW 1999 Conversion of agonist site to metal-ion chelator site in the β(2)-adrenergic receptor. Proc Natl Acad Sci USA 96:12322-12327
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 12322-12327
    • Elling, C.E.1    Thirstrup, K.2    Holst, B.3    Schwartz, T.W.4
  • 32
    • 0028947365 scopus 로고
    • A colorimetric assay for measuring activation of Gs- And Gq-coupled signaling pathways
    • Chen W, Shields TS, Stork PJ, Cone RD 1995 A colorimetric assay for measuring activation of Gs-and Gq-coupled signaling pathways. Anal Biochem 226:349-354
    • (1995) Anal Biochem , vol.226 , pp. 349-354
    • Chen, W.1    Shields, T.S.2    Stork, P.J.3    Cone, R.D.4
  • 33
    • 0027981633 scopus 로고
    • Calcium/calmodulin-dependent protein kinase types II and IV differentially regulate CREB-dependent gene expression
    • Matthews RP, Guthrie CR, Wailes LM, Zhao X, Means AR, McKnight GS 1994 Calcium/calmodulin-dependent protein kinase types II and IV differentially regulate CREB-dependent gene expression. Mol Cell Biol 14:6107-6116
    • (1994) Mol Cell Biol , vol.14 , pp. 6107-6116
    • Matthews, R.P.1    Guthrie, C.R.2    Wailes, L.M.3    Zhao, X.4    Means, A.R.5    McKnight, G.S.6
  • 34
    • 0036055478 scopus 로고    scopus 로고
    • Inhibitory control of growth hormone secretion by somatostatin in rat pituitary GC cells: sst(2) but not sst(1) receptors are coupled to inhibition of single-cell intracellular free calcium concentrations
    • Cervia D, Petrucci C, Bluet-Pajot MT, Epelbaum J, Bagnoli P 2002 Inhibitory control of growth hormone secretion by somatostatin in rat pituitary GC cells: sst(2) but not sst(1) receptors are coupled to inhibition of single-cell intracellular free calcium concentrations. Neuroendocrinology 76:99-110
    • (2002) Neuroendocrinology , vol.76 , pp. 99-110
    • Cervia, D.1    Petrucci, C.2    Bluet-Pajot, M.T.3    Epelbaum, J.4    Bagnoli, P.5
  • 35
    • 0035143816 scopus 로고    scopus 로고
    • Ghrelin, an endogenous growth hormone secretagogue, is a novel orexigenic peptide that antagonizes leptin action through the activation of hypothalamic neuropeptide Y/Y1 receptor pathway
    • Shintani M, Ogawa Y, Ebihara K, Aizawa-Abe M, Miyanaga F, Takaya K, Hayashi T, Inoue G, Hosoda K, Kojima M, Kangawa K, Nakao K 2001 Ghrelin, an endogenous growth hormone secretagogue, is a novel orexigenic peptide that antagonizes leptin action through the activation of hypothalamic neuropeptide Y/Y1 receptor pathway. Diabetes 50:227-232
    • (2001) Diabetes , vol.50 , pp. 227-232
    • Shintani, M.1    Ogawa, Y.2    Ebihara, K.3    Aizawa-Abe, M.4    Miyanaga, F.5    Takaya, K.6    Hayashi, T.7    Inoue, G.8    Hosoda, K.9    Kojima, M.10    Kangawa, K.11    Nakao, K.12
  • 36
    • 0035866077 scopus 로고    scopus 로고
    • Down-regulation of fasting-induced cAMP response element-mediated gene induction by leptin in neuropeptide Y neurons of the arcuate nucleus
    • Shimizu-Albergine M, Ippolito DL, Beavo JA 2001 Down-regulation of fasting-induced cAMP response element-mediated gene induction by leptin in neuropeptide Y neurons of the arcuate nucleus. J Neurosci 21:1238-1246
    • (2001) J Neurosci , vol.21 , pp. 1238-1246
    • Shimizu-Albergine, M.1    Ippolito, D.L.2    Beavo, J.A.3
  • 37
    • 0035130843 scopus 로고    scopus 로고
    • AgRP(83-132) acts as an inverse agonist on the human-melanocortin-4 receptor
    • Nijenhuis WA, Oosterom J, Adan RA 2001 AgRP(83-132) acts as an inverse agonist on the human-melanocortin-4 receptor. Mol Endocrinol 15:164-171
    • (2001) Mol Endocrinol , vol.15 , pp. 164-171
    • Nijenhuis, W.A.1    Oosterom, J.2    Adan, R.A.3
  • 38
    • 0030764741 scopus 로고    scopus 로고
    • Antagonism of central melanocortin receptors in vitro and in vivo by agouti-related protein
    • Ollmann MM, Wilson BD, Yang YK, Kerns JA, Chen Y, Gantz I, Barsh GS 1997 Antagonism of central melanocortin receptors in vitro and in vivo by agouti-related protein. Science 278:135-138
    • (1997) Science , vol.278 , pp. 135-138
    • Ollmann, M.M.1    Wilson, B.D.2    Yang, Y.K.3    Kerns, J.A.4    Chen, Y.5    Gantz, I.6    Barsh, G.S.7
  • 39
    • 0033056858 scopus 로고    scopus 로고
    • Down-regulation of melanocortin receptor signaling mediated by the amino terminus of Agouti protein in Xenopus melanophores
    • Ollmann MM, Barsh GS 1999 Down-regulation of melanocortin receptor signaling mediated by the amino terminus of Agouti protein in Xenopus melanophores. J Biol Chem 274:15837-15846
    • (1999) J Biol Chem , vol.274 , pp. 15837-15846
    • Ollmann, M.M.1    Barsh, G.S.2
  • 40
    • 0024163078 scopus 로고
    • [D-Arg1,D-Phe5,D-Trp7,9,Leu11] substance P, a potent bombesin antagonist in murine Swiss 3T3 cells, inhibits the growth of human small cell lung cancer cells in vitro
    • Woll PJ, Rozengurt E 1988 [D-Arg1,D-Phe5,D-Trp7,9,Leu11] substance P, a potent bombesin antagonist in murine Swiss 3T3 cells, inhibits the growth of human small cell lung cancer cells in vitro. Proc Natl Acad Sci USA 85:1859-1863
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 1859-1863
    • Woll, P.J.1    Rozengurt, E.2
  • 42
    • 0030273630 scopus 로고    scopus 로고
    • Use of the chemical structure of peptides as the starting point to design nonpeptide agonists and antagonists at peptide receptors: Examples with cholecystokinin and tachykinins
    • Horwell DC 1996 Use of the chemical structure of peptides as the starting point to design nonpeptide agonists and antagonists at peptide receptors: examples with cholecystokinin and tachykinins. Bioorg Med Chem 4:1573-1576
    • (1996) Bioorg Med Chem , vol.4 , pp. 1573-1576
    • Horwell, D.C.1
  • 43
    • 0037043534 scopus 로고    scopus 로고
    • Obesity: Keeping hunger at bay
    • Schwartz MW, Morton GJ 2002 Obesity: keeping hunger at bay. Nature 418:595-597
    • (2002) Nature , vol.418 , pp. 595-597
    • Schwartz, M.W.1    Morton, G.J.2
  • 45
    • 0035214464 scopus 로고    scopus 로고
    • Agonism, inverse agonism, and neutral antagonism at the constitutively active human neurotensin receptor 2
    • Richard F, Barroso S, Martinez J, Labbe-Jullie C, Kitabgi P 2001 Agonism, inverse agonism, and neutral antagonism at the constitutively active human neurotensin receptor 2. Mol Pharmacol 60:1392-1398
    • (2001) Mol Pharmacol , vol.60 , pp. 1392-1398
    • Richard, F.1    Barroso, S.2    Martinez, J.3    Labbe-Jullie, C.4    Kitabgi, P.5
  • 46
    • 0024556150 scopus 로고
    • Engineering hybrid genes without the use of restriction enzymes: Gene splicing by overlap extension
    • Horton RM, Hunt HD, Ho SN, Pullen JK, Pease LR 1989 Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension. Gene 77:61-68
    • (1989) Gene , vol.77 , pp. 61-68
    • Horton, R.M.1    Hunt, H.D.2    Ho, S.N.3    Pullen, J.K.4    Pease, L.R.5
  • 47
    • 0027340010 scopus 로고
    • Chimeric NK1 (substance P) NK3 (neurokinin B) Receptors
    • Gether U, Johansen TE, Schwartz TW 1993 Chimeric NK1 (substance P) NK3 (neurokinin B) Receptors. J Biol Chem 268:7893-7898
    • (1993) J Biol Chem , vol.268 , pp. 7893-7898
    • Gether, U.1    Johansen, T.E.2    Schwartz, T.W.3


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