메뉴 건너뛰기




Volumn 55, Issue 1, 2003, Pages 167-194

International Union of Pharmacology. XXXV. The glucagon receptor family

Author keywords

[No Author keywords available]

Indexed keywords

GLUCAGON LIKE PEPTIDE 1; GLUCAGON LIKE PEPTIDE 2; GLUCAGON RECEPTOR; SECRETIN;

EID: 0037373183     PISSN: 00316997     EISSN: None     Source Type: Journal    
DOI: 10.1124/pr.55.1.6     Document Type: Review
Times cited : (421)

References (412)
  • 1
    • 0029019227 scopus 로고
    • Regulation of glucagon receptor mRNA in cultured primary rat hepatocytes by glucose and cAMP
    • Abrahamsen N, Lundgren K, and Nishimura E (1995) Regulation of glucagon receptor mRNA in cultured primary rat hepatocytes by glucose and cAMP. J Biol Chem 270:15853-15857.
    • (1995) J Biol Chem , vol.270 , pp. 15853-15857
    • Abrahamsen, N.1    Lundgren, K.2    Nishimura, E.3
  • 2
    • 0028933090 scopus 로고
    • Regulation of glucagon and glucagon-like peptide-1 receptor messenger ribonucleic acid expression in cultured rat pancreatic islets by glucose, cyclic adenosine 3′,5′-monophosphate and glucocorticoids
    • Abrahamsen N and Nishimura E (1995) Regulation of glucagon and glucagon-like peptide-1 receptor messenger ribonucleic acid expression in cultured rat pancreatic islets by glucose, cyclic adenosine 3′,5′-monophosphate and glucocorticoids. Endocrinology 136:1572-1578
    • (1995) Endocrinology , vol.136 , pp. 1572-1578
    • Abrahamsen, N.1    Nishimura, E.2
  • 3
    • 0025196548 scopus 로고
    • Characterization of [125ITyr10]human growth hormone-releasing factor (1-44) amide binding to rat pituitary: Evidence for high and low affinity classes of sites
    • Abribat T, Boulanger L, and Gaudreau P (1990) Characterization of [125ITyr10]human growth hormone-releasing factor (1-44) amide binding to rat pituitary: evidence for high and low affinity classes of sites. Brain Res 528:291-299.
    • (1990) Brain Res , vol.528 , pp. 291-299
    • Abribat, T.1    Boulanger, L.2    Gaudreau, P.3
  • 4
    • 0036189831 scopus 로고    scopus 로고
    • The pharmacokinetics, pharmacodymamics, safety and tolerability of NN2211, a new longacting GLP-1 derivative, in healthy men
    • Agerso H, Jensen LB, Elbrond B, Rolan P, and Zdravkovic M (2002) The pharmacokinetics, pharmacodymamics, safety and tolerability of NN2211, a new longacting GLP-1 derivative, in healthy men. Diabetologia 45:195-202.
    • (2002) Diabetologia , vol.45 , pp. 195-202
    • Agerso, H.1    Jensen, L.B.2    Elbrond, B.3    Rolan, P.4    Zdravkovic, M.5
  • 5
    • 0034113232 scopus 로고    scopus 로고
    • Treatment of inflammatory bowel disease in a rodent model with the intestinal growth factor glucagon-like peptide-2
    • Alavi K, Schwartz MZ, Palazzo JP, and Prasad R (2000) Treatment of inflammatory bowel disease in a rodent model with the intestinal growth factor glucagon-like peptide-2. J Pediatr Surg 35:847-851.
    • (2000) J Pediatr Surg , vol.35 , pp. 847-851
    • Alavi, K.1    Schwartz, M.Z.2    Palazzo, J.P.3    Prasad, R.4
  • 6
    • 0031046975 scopus 로고    scopus 로고
    • Homologous down-regulation of growth hormone-releasing hormone receptor messenger ribonucleic acid levels
    • Aleppo G, Moskal SF 2nd, De Grandis PA, Kineman RD, and Frohman, LA (1997) Homologous down-regulation of growth hormone-releasing hormone receptor messenger ribonucleic acid levels. Endocrinology 138:1058-1065.
    • (1997) Endocrinology , vol.138 , pp. 1058-1065
    • Aleppo, G.1    Moskal S.F. II2    De Grandis, P.A.3    Kineman, R.D.4    Frohman, L.A.5
  • 7
    • 0031781959 scopus 로고    scopus 로고
    • Discovery of amino acid variants in the human glucose-dependent insulinotropic polypeptide (GIP) receptor: The impact on the pancreatic beta cell responses and functional expression studies in Chinese hamster fibroblast cells
    • Almind K, Ambye L, Urhammer SA, Hansen T, Echwald SM, Holst JJ, Gromada J, Thorens B, and Pedersen O (1998) Discovery of amino acid variants in the human glucose-dependent insulinotropic polypeptide (GIP) receptor: the impact on the pancreatic beta cell responses and functional expression studies in Chinese hamster fibroblast cells. Diabetologia 41:1194-1198.
    • (1998) Diabetologia , vol.41 , pp. 1194-1198
    • Almind, K.1    Ambye, L.2    Urhammer, S.A.3    Hansen, T.4    Echwald, S.M.5    Holst, J.J.6    Gromada, J.7    Thorens, B.8    Pedersen, O.9
  • 8
    • 0033784976 scopus 로고    scopus 로고
    • Structural insights into the amino terminus of the secretin receptor: I. Status of cysteine and cystine residues
    • Asmann YW, Dong M, Ganguli S, Hadac EM, and Miller LJ (2000) Structural insights into the amino terminus of the secretin receptor: I. Status of cysteine and cystine residues. Mol Pharmacol 58:911-919.
    • (2000) Mol Pharmacol , vol.58 , pp. 911-919
    • Asmann, Y.W.1    Dong, M.2    Ganguli, S.3    Hadac, E.M.4    Miller, L.J.5
  • 9
    • 0017161317 scopus 로고
    • Identification of glucagon-producing cells (A cells) in dog gastric mucosa
    • Baetens D, Rufener C, Srikant BC, Dobbs R, Unger R, and Orci L (1976) Identification of glucagon-producing cells (A cells) in dog gastric mucosa. J Cell Biol 69:455-464.
    • (1976) J Cell Biol , vol.69 , pp. 455-464
    • Baetens, D.1    Rufener, C.2    Srikant, B.C.3    Dobbs, R.4    Unger, R.5    Orci, L.6
  • 10
    • 0026602528 scopus 로고
    • Expression of the growth hormone-releasing hormone gene and its peptide product in the rat ovary
    • Bagnato A, Moretti C, Ohnishi J, Frajese G, and Catt KJ (1992) Expression of the growth hormone-releasing hormone gene and its peptide product in the rat ovary. Endocrinology 130:1097-1102.
    • (1992) Endocrinology , vol.130 , pp. 1097-1102
    • Bagnato, A.1    Moretti, C.2    Ohnishi, J.3    Frajese, G.4    Catt, K.J.5
  • 11
    • 0020553968 scopus 로고
    • Transcriptional regulation of growth hormone gene expression by growth hormone-releasing factor
    • Barinaga M, Yamonoto G, Rivier C, Vale W, Evans R, and Rosenfeld MG (1983) Transcriptional regulation of growth hormone gene expression by growth hormone-releasing factor. Nature (Lond) 306:84-85.
    • (1983) Nature (Lond) , vol.306 , pp. 84-85
    • Barinaga, M.1    Yamonoto, G.2    Rivier, C.3    Vale, W.4    Evans, R.5    Rosenfeld, M.G.6
  • 12
    • 0032714917 scopus 로고    scopus 로고
    • Neural contribution to the effect of glucagon-like peptide-1-(7-36) amide on arterial blood pressure in rats
    • Barragan JM, Eng J, Rodriguez R, and Blazquez E (1999) Neural contribution to the effect of glucagon-like peptide-1-(7-36) amide on arterial blood pressure in rats. Am J Physiol 277:E784-E791.
    • (1999) Am J Physiol , vol.277
    • Barragan, J.M.1    Eng, J.2    Rodriguez, R.3    Blazquez, E.4
  • 13
    • 0000540807 scopus 로고    scopus 로고
    • Oxyntomodulin and its related peptides
    • Lefebvre PJ ed, Springer-Verlag, Berlin
    • Bataille D (1996a) Oxyntomodulin and its related peptides, in Glucagon III (Lefebvre PJ ed) pp 327-340, Springer-Verlag, Berlin.
    • (1996) Glucagon III , pp. 327-340
    • Bataille, D.1
  • 14
    • 0002273323 scopus 로고    scopus 로고
    • Preproglucagon and its processing
    • Lefebvre PJ ed, Springer-Verlag, Berlin
    • Bataille D (1996b) Preproglucagon and its processing, in Glucagon III (Lefebvre PJ ed) pp 31-51, Springer-Verlag, Berlin.
    • (1996) Glucagon III , pp. 31-51
    • Bataille, D.1
  • 15
    • 0001634180 scopus 로고
    • Localization of glucagon in the alpha cells in the pancreatic islet by immunofluoreseent techniques
    • Baum J, Simon BF, Unger RH, and Madison LL (1962) Localization of glucagon in the alpha cells in the pancreatic islet by immunofluoreseent techniques. Diabetes 11:371-374.
    • (1962) Diabetes , vol.11 , pp. 371-374
    • Baum, J.1    Simon, B.F.2    Unger, R.H.3    Madison, L.L.4
  • 16
    • 0030829977 scopus 로고    scopus 로고
    • The Dwarfs of Sindh: Severe growth hormone (GH) deficiency caused by a mutation in the GH-releasing hormone receptor gene
    • Baumann G and Maheshwari H (1997) The Dwarfs of Sindh: severe growth hormone (GH) deficiency caused by a mutation in the GH-releasing hormone receptor gene. Acta Paediatr Suppl 423:33-38.
    • (1997) Acta Paediatr Suppl , vol.423 , pp. 33-38
    • Baumann, G.1    Maheshwari, H.2
  • 17
    • 0001107006 scopus 로고
    • On the causation of the so-called "peripheral reflex secretion" of the pancreas
    • Bayliss WM and Starling EH (1902) On the causation of the so-called "peripheral reflex secretion" of the pancreas. Proc R Soc Lond Biol 69:352-353.
    • (1902) Proc R Soc Lond Biol , vol.69 , pp. 352-353
    • Bayliss, W.M.1    Starling, E.H.2
  • 18
    • 0029761505 scopus 로고    scopus 로고
    • Glucagon-like peptide-1 (GLP-1) releases thyrotropin (TSH): Characterization of binding sites for GLP-1 on alpha-TSH cells
    • Beak SA, Small CJ, Ilovaiskaia I, Hurley JD, Ghatei MA, Bloom SR, and Smith DM (1996) Glucagon-like peptide-1 (GLP-1) releases thyrotropin (TSH): characterization of binding sites for GLP-1 on alpha-TSH cells. Endocrinology 137:4130-4138.
    • (1996) Endocrinology , vol.137 , pp. 4130-4138
    • Beak, S.A.1    Small, C.J.2    Ilovaiskaia, I.3    Hurley, J.D.4    Ghatei, M.A.5    Bloom, S.R.6    Smith, D.M.7
  • 20
    • 0020596734 scopus 로고
    • Hamster preproglucagon contains the sequence of glucagon and two related peptides
    • Bell GI, Santerre RF, and Mullenbach GT (1983b) Hamster preproglucagon contains the sequence of glucagon and two related peptides. Nature (Lond) 302:716-718.
    • (1983) Nature (Lond) , vol.302 , pp. 716-718
    • Bell, G.I.1    Santerre, R.F.2    Mullenbach, G.T.3
  • 21
    • 0033944863 scopus 로고    scopus 로고
    • Glucagon-like peptide-2 enhances intestinal epithelial barrier function of both transcellular and paracellular pathways in the mouse
    • Benjamin MA, McKay DM, Yang PC, Cameron H, and Perdue MH (2000) Glucagon-like peptide-2 enhances intestinal epithelial barrier function of both transcellular and paracellular pathways in the mouse. Gut 47:112-119.
    • (2000) Gut , vol.47 , pp. 112-119
    • Benjamin, M.A.1    McKay, D.M.2    Yang, P.C.3    Cameron, H.4    Perdue, M.H.5
  • 22
    • 0023793510 scopus 로고
    • Identification of a rat GHRH-like substance and its messenger RNA in rat testis
    • Berry SA and Pescovitz OH (1988) Identification of a rat GHRH-like substance and its messenger RNA in rat testis. Endocrinology 123:661-663.
    • (1988) Endocrinology , vol.123 , pp. 661-663
    • Berry, S.A.1    Pescovitz, O.H.2
  • 23
    • 1842413392 scopus 로고
    • Growth hormone-releasing factor stimulates proliferation of somatotrophs in vitro
    • Billestrup N, Swanson LW, and Vale W (1986) Growth hormone-releasing factor stimulates proliferation of somatotrophs in vitro. Proc Natl Acad Sci USA 83:6854-6857.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 6854-6857
    • Billestrup, N.1    Swanson, L.W.2    Vale, W.3
  • 24
    • 0035940435 scopus 로고    scopus 로고
    • Modulation of specific intestinal epithelial progenitors by enteric neurons
    • Bjerknes M and Cheng H (2001) Modulation of specific intestinal epithelial progenitors by enteric neurons. Proc Natl Acad Sci USA 98:12497-12502.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 12497-12502
    • Bjerknes, M.1    Cheng, H.2
  • 25
    • 0033304977 scopus 로고    scopus 로고
    • Glucagon-like peptide 1 elevates cytosolic calcium in pancreatic beta-cells independently of protein kinase A
    • Bode HP, Moormann B, Dabew R, and Goke B (1999) Glucagon-like peptide 1 elevates cytosolic calcium in pancreatic beta-cells independently of protein kinase A. Endocrinology 140:3919-3927.
    • (1999) Endocrinology , vol.140 , pp. 3919-3927
    • Bode, H.P.1    Moormann, B.2    Dabew, R.3    Goke, B.4
  • 28
    • 0032714919 scopus 로고    scopus 로고
    • Glucagon-like peptide 2 decreases mortality and reduces the severity of indomethacin-induced murine enteritis
    • Boushey RP, Yusta B, and Drucker DJ (1999) Glucagon-like peptide 2 decreases mortality and reduces the severity of indomethacin-induced murine enteritis. Am J Physiol 277:E937-E947.
    • (1999) Am J Physiol , vol.277
    • Boushey, R.P.1    Yusta, B.2    Drucker, D.J.3
  • 29
    • 0035863327 scopus 로고    scopus 로고
    • Glucagon-like peptide (GLP)-2 reduces chemotherapy-associated mortality and enhances cell survival in cells expressing a transfected GLP-2 receptor
    • Boushey RP, Yusta B, and Drucker DJ (2001) Glucagon-like peptide (GLP)-2 reduces chemotherapy-associated mortality and enhances cell survival in cells expressing a transfected GLP-2 receptor. Cancer Res 61:687-693.
    • (2001) Cancer Res , vol.61 , pp. 687-693
    • Boushey, R.P.1    Yusta, B.2    Drucker, D.J.3
  • 30
    • 0032790607 scopus 로고    scopus 로고
    • Structure of the rat glucose-dependent insulinotropic polypeptide receptor gene
    • Boylan MO, Jepeal LI, and Wolfe MM (1999) Structure of the rat glucose-dependent insulinotropic polypeptide receptor gene. Peptides 20:219-228.
    • (1999) Peptides , vol.20 , pp. 219-228
    • Boylan, M.O.1    Jepeal, L.I.2    Wolfe, M.M.3
  • 31
    • 0029913366 scopus 로고    scopus 로고
    • A novel peptide from the growth hormone releasing hormone gene stimulates Sertoli cell activity
    • Breyer PR, Rothrock JK, Beaudry N, and Pescovitz OH (1996) A novel peptide from the growth hormone releasing hormone gene stimulates Sertoli cell activity. Endocrinology 137:2159-2162.
    • (1996) Endocrinology , vol.137 , pp. 2159-2162
    • Breyer, P.R.1    Rothrock, J.K.2    Beaudry, N.3    Pescovitz, O.H.4
  • 33
    • 0013411020 scopus 로고
    • Gastric inhibitory polypeptide
    • Springer-Verlag, Heidelberg
    • Brown JC (1982) Gastric inhibitory polypeptide, in Monographs in Endocrinology, Springer-Verlag, Heidelberg.
    • (1982) Monographs in Endocrinology
    • Brown, J.C.1
  • 34
    • 0030795767 scopus 로고    scopus 로고
    • Intestinal function in mice with small bowel growth induced by glucagon-like peptide-2
    • Brubaker PL, Izzo A, Hill M, and Drucker DJ (1997) Intestinal function in mice with small bowel growth induced by glucagon-like peptide-2. Am J Physiol 272:E1050-E1058.
    • (1997) Am J Physiol , vol.272
    • Brubaker, P.L.1    Izzo, A.2    Hill, M.3    Drucker, D.J.4
  • 36
    • 0023930669 scopus 로고
    • Naturally occurring products of proglucagon 111-160 in the porcine and human small intestine
    • Buhl T, Thim L, Kofod H, Orskov C, Harling H, and Holst JJ (1988) Naturally occurring products of proglucagon 111-160 in the porcine and human small intestine. J Biol Chem 263:8621-8624.
    • (1988) J Biol Chem , vol.263 , pp. 8621-8624
    • Buhl, T.1    Thim, L.2    Kofod, H.3    Orskov, C.4    Harling, H.5    Holst, J.J.6
  • 37
    • 0030013475 scopus 로고    scopus 로고
    • Tissue distribution of messenger ribonucleic acid encoding the rat glucagon-like peptide 1 receptor
    • Bullock BP, Heller RS, and Habener JF (1996) Tissue distribution of messenger ribonucleic acid encoding the rat glucagon-like peptide 1 receptor. Endocrinology 137:2968-2978.
    • (1996) Endocrinology , vol.137 , pp. 2968-2978
    • Bullock, B.P.1    Heller, R.S.2    Habener, J.F.3
  • 38
    • 0033005873 scopus 로고    scopus 로고
    • Long-lasting antidiabetic effect of a dipeptidyl peptidase IV-resistant analog of glucagon-like peptide-1
    • Burcelin R, Dolci W, and Thorens B (1999a) Long-lasting antidiabetic effect of a dipeptidyl peptidase IV-resistant analog of glucagon-like peptide-1. Metabolism 48:252-258.
    • (1999) Metabolism , vol.48 , pp. 252-258
    • Burcelin, R.1    Dolci, W.2    Thorens, B.3
  • 39
    • 0028801240 scopus 로고
    • Cloning and sequence analysis of the murine glucagon receptor-encoding gene
    • Burcelin R, Li J, and Charron MJ (1995) Cloning and sequence analysis of the murine glucagon receptor-encoding gene. Gene (Amst) 164:305-310.
    • (1995) Gene (Amst) , vol.164 , pp. 305-310
    • Burcelin, R.1    Li, J.2    Charron, M.J.3
  • 40
    • 0032774740 scopus 로고    scopus 로고
    • Encapsulated, genetically engineered cells, secreting glucagon-like peptide-1 for the treatment of non-insulin-dependent diabetes mellitus
    • Burcelin R, Rolland E, Dolci W, Germain S, Carrel V, and Thorens B (1999b) Encapsulated, genetically engineered cells, secreting glucagon-like peptide-1 for the treatment of non-insulin-dependent diabetes mellitus. Ann NY Acad Sci 875:277-285.
    • (1999) Ann NY Acad Sci , vol.875 , pp. 277-285
    • Burcelin, R.1    Rolland, E.2    Dolci, W.3    Germain, S.4    Carrel, V.5    Thorens, B.6
  • 41
    • 0037015018 scopus 로고    scopus 로고
    • The expression of growth hormone-releasing hormone (GHRH) and splice variants of its receptor in human gastroenteropancreatic carcinomas
    • Busto R, Schally AV, Varga JL, Garcia-Fernandez MO, Groot K, Armatis P, and Szepeshazi K (2002) The expression of growth hormone-releasing hormone (GHRH) and splice variants of its receptor in human gastroenteropancreatic carcinomas. Proc Natl Acad Sci USA 99:11866-11871.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 11866-11871
    • Busto, R.1    Schally, A.V.2    Varga, J.L.3    Garcia-Fernandez, M.O.4    Groot, K.5    Armatis, P.6    Szepeshazi, K.7
  • 42
    • 0022263242 scopus 로고
    • Glucagon receptors along the nephron: [125I]glucagon binding in rat tubules
    • Butlen D and Morel F (1985) Glucagon receptors along the nephron: [125I]glucagon binding in rat tubules. Pfluegers Arch 404:348-353.
    • (1985) Pfluegers Arch , vol.404 , pp. 348-353
    • Butlen, D.1    Morel, F.2
  • 43
    • 0029812185 scopus 로고    scopus 로고
    • Human studies with glucagon-like-peptide-1: Potential of the gut hormone for clinical use
    • Byrne MM and Goke B (1996) Human studies with glucagon-like-peptide-1: potential of the gut hormone for clinical use. Diabet Med 13:854-860.
    • (1996) Diabet Med , vol.13 , pp. 854-860
    • Byrne, M.M.1    Goke, B.2
  • 44
    • 0025735539 scopus 로고
    • GRF analogs and fragments: Correlation between receptor binding, activity and structure
    • Campbell RM, Lee Y, Rivier J, Heimer EP, Felix AM, and Mowles TF (1991) GRF analogs and fragments: correlation between receptor binding, activity and structure. Peptides 12:569-574.
    • (1991) Peptides , vol.12 , pp. 569-574
    • Campbell, R.M.1    Lee, Y.2    Rivier, J.3    Heimer, E.P.4    Felix, A.M.5    Mowles, T.F.6
  • 45
    • 0027034012 scopus 로고
    • Evolution of the growth hormone-releasing factor (GRF) family of peptides
    • Campbell RM and Scanes CG (1992) Evolution of the growth hormone-releasing factor (GRF) family of peptides. Growth Regul 2:175-191.
    • (1992) Growth Regul , vol.2 , pp. 175-191
    • Campbell, R.M.1    Scanes, C.G.2
  • 46
    • 0020996599 scopus 로고
    • Human pancreatic GRF stimulates phosphatidylinositol labeling in cultured anterior pituitary cells
    • Canonico PL, Cronin MJ, Thorner MO, and MacLeod RM (1983) Human pancreatic GRF stimulates phosphatidylinositol labeling in cultured anterior pituitary cells. Am J Physiol 245:E587-E590.
    • (1983) Am J Physiol , vol.245
    • Canonico, P.L.1    Cronin, M.J.2    Thorner, M.O.3    MacLeod, R.M.4
  • 47
    • 0028046153 scopus 로고
    • Synthesis and expression of a gene for the rat glucagon receptor. Replacement of an aspartic acid in the extracellular domain prevents glucagon binding
    • Carruthers CJL, Unson CG, Kim HN, and Sakmar TP (1994) Synthesis and expression of a gene for the rat glucagon receptor. Replacement of an aspartic acid in the extracellular domain prevents glucagon binding. J Biol Chem 269:29321-29328.
    • (1994) J Biol Chem , vol.269 , pp. 29321-29328
    • Carruthers, C.J.L.1    Unson, C.G.2    Kim, H.N.3    Sakmar, T.P.4
  • 48
    • 0032568002 scopus 로고    scopus 로고
    • Human growth hormone-releasing hormone hGHRH(1-29)-NH2: Systematic structure-activity relationship studies
    • Cervini LA, Donaldson CJ, Koerber SC, Vale WW, and Rivier JE (1998) Human growth hormone-releasing hormone hGHRH(1-29)-NH2: systematic structure-activity relationship studies. J Med Chem 41:717-727.
    • (1998) J Med Chem , vol.41 , pp. 717-727
    • Cervini, L.A.1    Donaldson, C.J.2    Koerber, S.C.3    Vale, W.W.4    Rivier, J.E.5
  • 49
    • 0030805335 scopus 로고    scopus 로고
    • Prevention of parenteral nutrition-induced gut hyoplasia by coinfusion of glucagon-like peptide-2
    • Chance WT, Foley-Nelson T, Thomas I, and Balasubramaniam A (1997) Prevention of parenteral nutrition-induced gut hyoplasia by coinfusion of glucagon-like peptide-2. Am J Physiol 273:G559-G563.
    • (1997) Am J Physiol , vol.273
    • Chance, W.T.1    Foley-Nelson, T.2    Thomas, I.3    Balasubramaniam, A.4
  • 50
    • 0033639262 scopus 로고    scopus 로고
    • Maintaining gut integrity during parenteral nutrition of tumor-bearing rats: Effects of glucagon-like peptide 2
    • Chance WT, Sheriff S, Foley-Nelson T, Thomas I, and Balasubramaniam A (2000) Maintaining gut integrity during parenteral nutrition of tumor-bearing rats: effects of glucagon-like peptide 2. Nutr Cancer 37:215-222.
    • (2000) Nutr Cancer , vol.37 , pp. 215-222
    • Chance, W.T.1    Sheriff, S.2    Foley-Nelson, T.3    Thomas, I.4    Balasubramaniam, A.5
  • 51
    • 0029781929 scopus 로고    scopus 로고
    • The effect of gastric inhibitory polypeptide and glucagon like peptides on intestinal hexose transport
    • Cheeseman CI and Tsang R (1996) The effect of gastric inhibitory polypeptide and glucagon like peptides on intestinal hexose transport. Am J Physiol 271:G477-G482.
    • (1996) Am J Physiol , vol.271
    • Cheeseman, C.I.1    Tsang, R.2
  • 52
    • 0028153118 scopus 로고
    • Ion channels and the signal transduction pathways in the regulation of growth hormone secretion
    • Chen C, Vincent JD, and Clarke IJ (1994) Ion channels and the signal transduction pathways in the regulation of growth hormone secretion. Trends Endocrinol Metab 5:227-233.
    • (1994) Trends Endocrinol Metab , vol.5 , pp. 227-233
    • Chen, C.1    Vincent, J.D.2    Clarke, I.J.3
  • 53
    • 0036178688 scopus 로고    scopus 로고
    • Over-expression of the glucagon-like peptide-1 receptor on INS-1 cells confers autocrine stimulation of insulin gene promoter activity: A strategy for production of pancreatic beta-cell lines for use in transplantation
    • Chepurny OG and Holz GG (2002) Over-expression of the glucagon-like peptide-1 receptor on INS-1 cells confers autocrine stimulation of insulin gene promoter activity: a strategy for production of pancreatic beta-cell lines for use in transplantation. Cell Tissue Res 307:191-201.
    • (2002) Cell Tissue Res , vol.307 , pp. 191-201
    • Chepurny, O.G.1    Holz, G.G.2
  • 55
    • 0030610245 scopus 로고    scopus 로고
    • FluoresceinTrp25-exendin-4, a biologically active fluorescent probe for the human GLP-1 receptor
    • Chicchi GG, Cascieri MA, Graziano MP, Calahan T, and Tota MR (1997) FluoresceinTrp25-exendin-4, a biologically active fluorescent probe for the human GLP-1 receptor. Peptides 18:319-321.
    • (1997) Peptides , vol.18 , pp. 319-321
    • Chicchi, G.G.1    Cascieri, M.A.2    Graziano, M.P.3    Calahan, T.4    Tota, M.R.5
  • 56
    • 0028979609 scopus 로고
    • Molecular cloning and functional characterization of a human secretin receptor
    • Chow BK (1995) Molecular cloning and functional characterization of a human secretin receptor. Biochem Biophys Res Commun 212:204-211.
    • (1995) Biochem Biophys Res Commun , vol.212 , pp. 204-211
    • Chow, B.K.1
  • 57
    • 0030469432 scopus 로고    scopus 로고
    • Glucagon and its receptor in various tissues
    • discussion 805:42-43
    • Christophe J (1996) Glucagon and its receptor in various tissues. Ann NY Acad Sci 805:31-42; discussion 805:42-43.
    • (1996) Ann NY Acad Sci , vol.805 , pp. 31-42
    • Christophe, J.1
  • 59
    • 0026443527 scopus 로고
    • Growth hormone-releasing hormone is produced by rat Leydig cell in culture and acts as a positive regulator of Leydig cell function
    • Ciampani T, Fabbri A, Isidori A, and Dufau ML (1992) Growth hormone-releasing hormone is produced by rat Leydig cell in culture and acts as a positive regulator of Leydig cell function. Endocrinology 131:2785-2792.
    • (1992) Endocrinology , vol.131 , pp. 2785-2792
    • Ciampani, T.1    Fabbri, A.2    Isidori, A.3    Dufau, M.L.4
  • 60
    • 0013358274 scopus 로고
    • Glucagon and gluconeogenesis
    • Lefebvre PJ ed, Springer-Verlag, Berlin
    • Claus TH, Park CR, and Pilkis SJ (1983) Glucagon and gluconeogenesis, in Glucagon I (Lefebvre PJ ed) pp 315-360, Springer-Verlag, Berlin.
    • (1983) Glucagon I , pp. 315-360
    • Claus, T.H.1    Park, C.R.2    Pilkis, S.J.3
  • 61
    • 0035014108 scopus 로고    scopus 로고
    • A randomized, double-blind, placebo-controlled trial of single-dose intravenous secretin as treatment for children with autism
    • Coniglio SJ, Lewis JD, Lang C, Burns TG, Subhani-Siddique R, Weintraub A, Schub H, and Holden EW (2001) A randomized, double-blind, placebo-controlled trial of single-dose intravenous secretin as treatment for children with autism. J Pediatr 138:649-655.
    • (2001) J Pediatr , vol.138 , pp. 649-655
    • Coniglio, S.J.1    Lewis, J.D.2    Lang, C.3    Burns, T.G.4    Subhani-Siddique, R.5    Weintraub, A.6    Schub, H.7    Holden, E.W.8
  • 62
    • 0030455393 scopus 로고    scopus 로고
    • Structural simplification of potent growth hormone-releasing hormone analogs: Implications for other members of the VIP/GHRH/PACAP family
    • Coy DH, Jiang NY, Fuselier J, and Murphy WA (1996) Structural simplification of potent growth hormone-releasing hormone analogs: implications for other members of the VIP/GHRH/PACAP family. Ann NY Acad Sci 805:149-158.
    • (1996) Ann NY Acad Sci , vol.805 , pp. 149-158
    • Coy, D.H.1    Jiang, N.Y.2    Fuselier, J.3    Murphy, W.A.4
  • 63
    • 0033516651 scopus 로고    scopus 로고
    • Two cytoplasmic loops of the glucagon receptor are required to elevate cAMP or intracellular calcium
    • Cypess AM, Unson CG, Wu CR, and Sakmar TP (1999) Two cytoplasmic loops of the glucagon receptor are required to elevate cAMP or intracellular calcium. J Biol Chem 274:19455-19464.
    • (1999) J Biol Chem , vol.274 , pp. 19455-19464
    • Cypess, A.M.1    Unson, C.G.2    Wu, C.R.3    Sakmar, T.P.4
  • 67
    • 0033574608 scopus 로고    scopus 로고
    • Miniglucagon (glucagon 19-29), a potent and efficient inhibitor of secretagogue-induced insulin release through a Ca2+ pathway
    • Dalle S, Smith P, Blache P, Le-Nguyen D, Le Brigand L, Bergeron F, Ashcroft FM, and Bataille D (1999) Miniglucagon (glucagon 19-29), a potent and efficient inhibitor of secretagogue-induced insulin release through a Ca2+ pathway. J Biol Chem 274:10869-10876.
    • (1999) J Biol Chem , vol.274 , pp. 10869-10876
    • Dalle, S.1    Smith, P.2    Blache, P.3    Le-Nguyen, D.4    Le Brigand, L.5    Bergeron, F.6    Ashcroft, F.M.7    Bataille, D.8
  • 68
    • 0031782440 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV resistant analogues of glucagon-like peptide-1 which have extended metabolic stability and improved biological activity
    • Deacon CF, Knudsen LB, Madsen K, Wiberg FC, Jacobsen O, and Holst, JJ (1998) Dipeptidyl peptidase IV resistant analogues of glucagon-like peptide-1 which have extended metabolic stability and improved biological activity. Diabetologia 41:271-278.
    • (1998) Diabetologia , vol.41 , pp. 271-278
    • Deacon, C.F.1    Knudsen, L.B.2    Madsen, K.3    Wiberg, F.C.4    Jacobsen, O.5    Holst, J.J.6
  • 69
    • 0032230249 scopus 로고    scopus 로고
    • Identification of binding domains of the growth hormone-releasing hormone receptor by analysis of mutant and chimeric receptor proteins
    • DeAlmeida VI and Mayo KE (1998) Identification of binding domains of the growth hormone-releasing hormone receptor by analysis of mutant and chimeric receptor proteins. Mol Endocrinol 12:750-765.
    • (1998) Mol Endocrinol , vol.12 , pp. 750-765
    • DeAlmeida, V.I.1    Mayo, K.E.2
  • 72
    • 0000284393 scopus 로고
    • Spasmolytic and clinical use of glucagon
    • Lefebvre PJ ed, Springer-Verlag, Berlin
    • Diamant B and Picazo J (1983) Spasmolytic and clinical use of glucagon, in Glucagon II (Lefebvre PJ ed) pp 611-643, Springer-Verlag, Berlin.
    • (1983) Glucagon II , pp. 611-643
    • Diamant, B.1    Picazo, J.2
  • 74
    • 0037105663 scopus 로고    scopus 로고
    • Silencing of secretin receptor function by dimerization with a misspliced variant secretin receptor in ductal pancreatic adenocarcinoma
    • Ding WQ, Cheng ZJ, McElhiney J, Kuntz SM, and Miller LJ (2002a) Silencing of secretin receptor function by dimerization with a misspliced variant secretin receptor in ductal pancreatic adenocarcinoma. Cancer Res 62:5223-5229.
    • (2002) Cancer Res , vol.62 , pp. 5223-5229
    • Ding, W.Q.1    Cheng, Z.J.2    McElhiney, J.3    Kuntz, S.M.4    Miller, L.J.5
  • 75
    • 0036158930 scopus 로고    scopus 로고
    • Dominant negative action of an abnormal secretin receptor arising from mRNA missplicing in a gastrinoma
    • Ding WQ, Kuntz S, Bohmig M, Wiedenmann B, and Miller LJ (2002b) Dominant negative action of an abnormal secretin receptor arising from mRNA missplicing in a gastrinoma. Gastroenterology 122:500-511.
    • (2002) Gastroenterology , vol.122 , pp. 500-511
    • Ding, W.Q.1    Kuntz, S.2    Bohmig, M.3    Wiedenmann, B.4    Miller, L.J.5
  • 76
    • 0033516657 scopus 로고    scopus 로고
    • Identification of an interaction between residue 6 of the natural peptide ligand and a distinct residue within the amino-terminal tail of the secretin receptor
    • Dong M, Wang Y, Hadac EM, Pinon DI, Holicky E, and Miller LJ (1999a) Identification of an interaction between residue 6 of the natural peptide ligand and a distinct residue within the amino-terminal tail of the secretin receptor. J Biol Chem 274:19161-19167.
    • (1999) J Biol Chem , vol.274 , pp. 19161-19167
    • Dong, M.1    Wang, Y.2    Hadac, E.M.3    Pinon, D.I.4    Holicky, E.5    Miller, L.J.6
  • 77
    • 0034516908 scopus 로고    scopus 로고
    • Dual contacts between peptide agonist ligands and the secretin receptor directly established by photoaffinity labeling
    • Dong M, Wang Y, and Miller LJ (2000) Dual contacts between peptide agonist ligands and the secretin receptor directly established by photoaffinity labeling. Ann NY Acad Sci 921:381-386.
    • (2000) Ann NY Acad Sci , vol.921 , pp. 381-386
    • Dong, M.1    Wang, Y.2    Miller, L.J.3
  • 78
    • 0033534683 scopus 로고    scopus 로고
    • Demonstration of a direct interaction between residue 22 in the carboxyl-terminal half of secretin and the amino-terminal tail of the secretin receptor using photoaffinity labeling
    • Dong M, Wang Y, Pinon DI, Hadac EM, and Miller LJ (1999b) Demonstration of a direct interaction between residue 22 in the carboxyl-terminal half of secretin and the amino-terminal tail of the secretin receptor using photoaffinity labeling. J Biol Chem 274:903-909.
    • (1999) J Biol Chem , vol.274 , pp. 903-909
    • Dong, M.1    Wang, Y.2    Pinon, D.I.3    Hadac, E.M.4    Miller, L.J.5
  • 79
    • 0036843029 scopus 로고    scopus 로고
    • Interaction among four residues distributed through the secretin pharmacophore and a focused region of the secretin receptor amino terminus
    • Dong M, Zang M, Pinon DI, Li Z, Lybrand TP, and Miller LJ (2002) Interaction among four residues distributed through the secretin pharmacophore and a focused region of the secretin receptor amino terminus. Mol Endocrinol 16:2490-2501.
    • (2002) Mol Endocrinol , vol.16 , pp. 2490-2501
    • Dong, M.1    Zang, M.2    Pinon, D.I.3    Li, Z.4    Lybrand, T.P.5    Miller, L.J.6
  • 80
    • 0034806376 scopus 로고    scopus 로고
    • Insertion of an N-terminal 6-aminohexanoic acid after the 7 amino acid position of glucagon-like peptide-1 produces a long-acting hypoglycemic agent
    • Doyle ME, Greig NH, Holloway HW, Betkey JA, Bernier M, and Egan JM (2001) Insertion of an N-terminal 6-aminohexanoic acid after the 7 amino acid position of glucagon-like peptide-1 produces a long-acting hypoglycemic agent. Endocrinology 142:4462-4468.
    • (2001) Endocrinology , vol.142 , pp. 4462-4468
    • Doyle, M.E.1    Greig, N.H.2    Holloway, H.W.3    Betkey, J.A.4    Bernier, M.5    Egan, J.M.6
  • 81
    • 0031936954 scopus 로고    scopus 로고
    • The glucagon-like peptides
    • Drucker DJ (1998) The glucagon-like peptides. Diabetes 47:159-169.
    • (1998) Diabetes , vol.47 , pp. 159-169
    • Drucker, D.J.1
  • 82
    • 0034857141 scopus 로고    scopus 로고
    • Develepment of glucagon-like peptide-1-based pharmaceuticals as therapeutic agents for the treatment of diabetes
    • Drucker DJ (2001a) Develepment of glucagon-like peptide-1-based pharmaceuticals as therapeutic agents for the treatment of diabetes. Curr Pharm Des 7:1399-1412.
    • (2001) Curr Pharm Des , vol.7 , pp. 1399-1412
    • Drucker, D.J.1
  • 83
    • 0035037843 scopus 로고    scopus 로고
    • Glucagon-like peptide 2
    • Drucker DJ (2001b) Glucagon-like peptide 2. J Clin Endocrinol Metab 86:1759-1764.
    • (2001) J Clin Endocrinol Metab , vol.86 , pp. 1759-1764
    • Drucker, D.J.1
  • 84
    • 0035106978 scopus 로고    scopus 로고
    • Minireview: The glucagon-like peptides
    • Drucker DJ (2001c) Minireview: the glucagon-like peptides. Endocrinology 142:521-527.
    • (2001) Endocrinology , vol.142 , pp. 521-527
    • Drucker, D.J.1
  • 85
    • 0036158954 scopus 로고    scopus 로고
    • Biological actions and therapeutic potential of the glucagon-like peptides
    • Drucker DJ (2002) Biological actions and therapeutic potential of the glucagon-like peptides. Gastroenterology 122:531-544.
    • (2002) Gastroenterology , vol.122 , pp. 531-544
    • Drucker, D.J.1
  • 86
    • 0037312818 scopus 로고    scopus 로고
    • Glucagon-like peptides: Regulators of cell proliferation, differentiation and apoptosis
    • Drucker DJ (2003) Glucagon-like peptides: regulators of cell proliferation, differentiation and apoptosis. Mol Endocrinol 17:161-171.
    • (2003) Mol Endocrinol , vol.17 , pp. 161-171
    • Drucker, D.J.1
  • 87
    • 0023787950 scopus 로고
    • Glucagon gene expression in vertebrate brain
    • Drucker DJ and Asa S (1988) Glucagon gene expression in vertebrate brain. J Biol Chem 263:13475-13478.
    • (1988) J Biol Chem , vol.263 , pp. 13475-13478
    • Drucker, D.J.1    Asa, S.2
  • 89
    • 0031417543 scopus 로고    scopus 로고
    • Intestinal response to growth factors administered alone or in combination with human [Gly2]glucagon-like peptide 2
    • Drucker DJ, DeForest L, and Brubaker PL (1997a) Intestinal response to growth factors administered alone or in combination with human [Gly2]glucagon-like peptide 2. Am J Physiol 273:G1252-G1262.
    • (1997) Am J Physiol , vol.273
    • Drucker, D.J.1    DeForest, L.2    Brubaker, P.L.3
  • 90
    • 0029795016 scopus 로고    scopus 로고
    • Induction of intestinal epithelial proliferation by glucagon-like peptide 2
    • Drucker DJ, Ehrlich P, Asa SL, and Brubaker PL (1996) Induction of intestinal epithelial proliferation by glucagon-like peptide 2. Proc Natl Acad Sci USA 93:7911-7916.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 7911-7916
    • Drucker, D.J.1    Ehrlich, P.2    Asa, S.L.3    Brubaker, P.L.4
  • 91
    • 0344357096 scopus 로고
    • Glucagon-like peptide I stimulates insulin gene expression and increases cyclic AMP levels in a rat islet cell line
    • Drucker DJ, Philippe J, Mojsov S, Chick WL, and Habener JF (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.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 3434-3438
    • Drucker, D.J.1    Philippe, J.2    Mojsov, S.3    Chick, W.L.4    Habener, J.F.5
  • 93
    • 0032621235 scopus 로고    scopus 로고
    • Human [Gly2]-GLP-2 reduces the severity of colonic injury in a murine model of experimental colitis
    • Drucker DJ, Yusta B, Boushey RP, Deforest L, and Brubaker PL (1999b) Human [Gly2]-GLP-2 reduces the severity of colonic injury in a murine model of experimental colitis. Am J Physiol 276:G79-G91.
    • (1999) Am J Physiol , vol.276
    • Drucker, D.J.1    Yusta, B.2    Boushey, R.P.3    Deforest, L.4    Brubaker, P.L.5
  • 94
    • 0032566004 scopus 로고    scopus 로고
    • Tissue distribution of rat glucagon receptor and GLP-1 receptor gene expression
    • Dunphy JL, Taylor RG, and Fuller PJ (1998) Tissue distribution of rat glucagon receptor and GLP-1 receptor gene expression. Mol Cell Endocrinol 141:179-186.
    • (1998) Mol Cell Endocrinol , vol.141 , pp. 179-186
    • Dunphy, J.L.1    Taylor, R.G.2    Fuller, P.J.3
  • 95
    • 0013942426 scopus 로고
    • Stimulation of release of insulin by an extract of intestinal mucosa
    • Dupre J and Beck JC (1966) Stimulation of release of insulin by an extract of intestinal mucosa. Diabetes 15:555-559.
    • (1966) Diabetes , vol.15 , pp. 555-559
    • Dupre, J.1    Beck, J.C.2
  • 96
    • 0015791989 scopus 로고
    • Stimulation of insulin secretion by gastric inhibitory polypeptide in man
    • Dupre J, Ross SA, Watson D, and Brown JC (1973) Stimulation of insulin secretion by gastric inhibitory polypeptide in man. J Clin Endocrinol Metab 37:826-828.
    • (1973) J Clin Endocrinol Metab , vol.37 , pp. 826-828
    • Dupre, J.1    Ross, S.A.2    Watson, D.3    Brown, J.C.4
  • 97
    • 0013409320 scopus 로고
    • Glucagon and lipoprotein regulation in man
    • Foa PP, Bajaj JS, and Foa NL eds, Springer-Verlag, Berlin
    • Eaton RP (1977) Glucagon and lipoprotein regulation in man, in Glucagon: Its Role in Physiology and Clinical Medicine (Foa PP, Bajaj JS, and Foa NL eds) p 553, Springer-Verlag, Berlin.
    • (1977) Glucagon: Its Role in Physiology and Clinical Medicine , pp. 553
    • Eaton, R.P.1
  • 98
    • 0023130739 scopus 로고
    • Gastrointestinal peptides and insulin secretion
    • Ebert R and Creutzfeldt W (1987) Gastrointestinal peptides and insulin secretion. Diabetes Metab Rev 3:1-26.
    • (1987) Diabetes Metab Rev , vol.3 , pp. 1-26
    • Ebert, R.1    Creutzfeldt, W.2
  • 99
    • 0036965113 scopus 로고    scopus 로고
    • The insulinotropic effect of acute exendin-4 administered to humans: Comparison of nondiabetic state to type 2 diabetes
    • Egan JM, Clocquet AR, and Elahi D (2002) The insulinotropic effect of acute exendin-4 administered to humans: comparison of nondiabetic state to type 2 diabetes. J Clin Endocrinol Metab 87:1282-1290.
    • (2002) J Clin Endocrinol Metab , vol.87 , pp. 1282-1290
    • Egan, J.M.1    Clocquet, A.R.2    Elahi, D.3
  • 100
    • 0035968291 scopus 로고    scopus 로고
    • A new pathway for glucose-dependent insulinotropic polypeptide (GIP) receptor signaling: Evidence for the involvement of phospholipase A2 in GIP-stimulated insulin secretion
    • Ehses JA, Lee SS, Pederson RA, and McIntosh CH (2001) A new pathway for glucose-dependent insulinotropic polypeptide (GIP) receptor signaling: evidence for the involvement of phospholipase A2 in GIP-stimulated insulin secretion. J Biol Chem 276:23667-23673.
    • (2001) J Biol Chem , vol.276 , pp. 23667-23673
    • Ehses, J.A.1    Lee, S.S.2    Pederson, R.A.3    McIntosh, C.H.4
  • 101
    • 0037020242 scopus 로고    scopus 로고
    • Glucose-dependent insulinotropic polypeptide activates the Raf-Mek1/2-ERK1/2 module via a cyclic AMP/cAMP-dependent protein kinase/Rap1-mediated pathway
    • Ehses JA, Pelech SL, Pederson RA, and McIntosh CH (2002) Glucose-dependent insulinotropic polypeptide activates the Raf-Mek1/2-ERK1/2 module via a cyclic AMP/cAMP-dependent protein kinase/Rap1-mediated pathway. J Biol Chem 277:37088-37097.
    • (2002) J Biol Chem , vol.277 , pp. 37088-37097
    • Ehses, J.A.1    Pelech, S.L.2    Pederson, R.A.3    McIntosh, C.H.4
  • 102
    • 0017078016 scopus 로고
    • Inherited ateliotic dwarfism in mice. Characteristics of the mutation, little, on chromosome 6
    • Eicher EM and Beamer WG (1976) Inherited ateliotic dwarfism in mice. Characteristics of the mutation, little, on chromosome 6. J Hered 67:87-91.
    • (1976) J Hered , vol.67 , pp. 87-91
    • Eicher, E.M.1    Beamer, W.G.2
  • 103
    • 0022515675 scopus 로고
    • Growth hormone-releasing factor does not stimulate phosphoinositides breakdown in primary cultures of rat and human pituitary cells
    • Escobar DC, Vicentini LM, Ghigo E, Ciccarelli E, Usellini L, Capella C, and Cocchi D (1986) Growth hormone-releasing factor does not stimulate phosphoinositides breakdown in primary cultures of rat and human pituitary cells. Acta Endocrinol (Copenh) 112:345-350.
    • (1986) Acta Endocrinol (Copenh) , vol.112 , pp. 345-350
    • Escobar, D.C.1    Vicentini, L.M.2    Ghigo, E.3    Ciccarelli, E.4    Usellini, L.5    Capella, C.6    Cocchi, D.7
  • 104
    • 0000251360 scopus 로고
    • Glucagon and the heart
    • Lefebvre PJ ed, Springer-Verlag, Berlin
    • Farah AE (1983) Glucagon and the heart, in Glucagon II (Lefebvre PJ ed) pp 553-609, Springer-Verlag, Berlin.
    • (1983) Glucagon II , pp. 553-609
    • Farah, A.E.1
  • 105
    • 0029127019 scopus 로고
    • Characterization of GIP(1-30) and GIP(1-42) as stimulators of proinsulin gene transcription
    • Fehmann H-C and Goke B (1995) Characterization of GIP(1-30) and GIP(1-42) as stimulators of proinsulin gene transcription. Peptides 16:1149-1152.
    • (1995) Peptides , vol.16 , pp. 1149-1152
    • Fehmann, H.-C.1    Goke, B.2
  • 106
    • 0029043139 scopus 로고
    • Cell and molecular biology of the incretin hormones glucagon-like peptide 1 and glucose-dependent releasing polypeptide
    • Fehmann H-C, Goke R, and Goke B (1995a) Cell and molecular biology of the incretin hormones glucagon-like peptide 1 and glucose-dependent releasing polypeptide. Endocr Rev 16:390-410.
    • (1995) Endocr Rev , vol.16 , pp. 390-410
    • Fehmann, H.-C.1    Goke, R.2    Goke, B.3
  • 107
    • 0026034765 scopus 로고
    • Functional receptors for the insulinotropic hormone glucagon-like peptide-I(7-37) on a somatostatin secreting cell line
    • Fehmann HC and Habener JF (1991) Functional receptors for the insulinotropic hormone glucagon-like peptide-I(7-37) on a somatostatin secreting cell line. FEBS Lett 279:335-340.
    • (1991) FEBS Lett , vol.279 , pp. 335-340
    • Fehmann, H.C.1    Habener, J.F.2
  • 108
    • 0026535588 scopus 로고
    • Insulinotropic hormone glucagon-like peptideI(7-37) stimulation of proinsulin gene expression and proinsulin biosynthesis in insulinoma βTC-1 cells
    • Fehmann H-C and Habener JF (1992) Insulinotropic hormone glucagon-like peptideI(7-37) stimulation of proinsulin gene expression and proinsulin biosynthesis in insulinoma βTC-1 cells. Endocrinology 130:159-166.
    • (1992) Endocrinology , vol.130 , pp. 159-166
    • Fehmann, H.-C.1    Habener, J.F.2
  • 110
    • 0025042644 scopus 로고
    • Effect of growth hormone-releasing factor on phosphoinositide hydrolysis in somatotrophs
    • French MB, Lussier BT, Moor BC, and Kraicer J (1990) Effect of growth hormone-releasing factor on phosphoinositide hydrolysis in somatotrophs. Mol Cell Endocrinol 72:221-226.
    • (1990) Mol Cell Endocrinol , vol.72 , pp. 221-226
    • French, M.B.1    Lussier, B.T.2    Moor, B.C.3    Kraicer, J.4
  • 111
    • 0024599588 scopus 로고
    • Dipeptidyl peptidase IV and trypsin-like enzymatic degradation of human growth hormone-releasing hormone in plasma
    • Frohman LA, Downs TR, Heimer EP, and Felix AM (1989a) Dipeptidyl peptidase IV and trypsin-like enzymatic degradation of human growth hormone-releasing hormone in plasma. J Clin Investig 83:1533-1540.
    • (1989) J Clin Investig , vol.83 , pp. 1533-1540
    • Frohman, L.A.1    Downs, T.R.2    Heimer, E.P.3    Felix, A.M.4
  • 112
    • 0022761775 scopus 로고
    • Growth hormone-releasing hormone
    • Frohman LA and Jansson JO (1986) Growth hormone-releasing hormone. Endocr Rev 7:223-253.
    • (1986) Endocr Rev , vol.7 , pp. 223-253
    • Frohman, L.A.1    Jansson, J.O.2
  • 113
    • 0019756333 scopus 로고
    • Ectopic production of growth hormone-releasing factor by carcinoid and pancreatic islet tumors associated with acromegaly
    • Frohman LA and Szabo M (1981) Ectopic production of growth hormone-releasing factor by carcinoid and pancreatic islet tumors associated with acromegaly. Prog Clin Biol Res 74:259-271.
    • (1981) Prog Clin Biol Res , vol.74 , pp. 259-271
    • Frohman, L.A.1    Szabo, M.2
  • 114
    • 0024431908 scopus 로고
    • Cloning and characterization of mouse growth hormone-releasing hormone (GRH) complementary DNA: Increased GRH messenger RNA levels in the growth hormone-deficient lit/lit mouse
    • Frohman MA, Downs TR, Chomczynski P, and Frohman LA (1989b) Cloning and characterization of mouse growth hormone-releasing hormone (GRH) complementary DNA: increased GRH messenger RNA levels in the growth hormone-deficient lit/lit mouse. Mol Endocrinol 3:1529-1536.
    • (1989) Mol Endocrinol , vol.3 , pp. 1529-1536
    • Frohman, M.A.1    Downs, T.R.2    Chomczynski, P.3    Frohman, L.A.4
  • 115
    • 0032475970 scopus 로고    scopus 로고
    • Contribution of a PSI-like element to the tissue- and cell-specific expression of the human GLP-1 receptor gene
    • Galehshahi FS, Goke B, and Lankat-Buttgereit B (1998) Contribution of a PSI-like element to the tissue- and cell-specific expression of the human GLP-1 receptor gene. FEBS Lett 436:163-168.
    • (1998) FEBS Lett , vol.436 , pp. 163-168
    • Galehshahi, F.S.1    Goke, B.2    Lankat-Buttgereit, B.3
  • 116
    • 0017106186 scopus 로고
    • Interaction of peptides related to secretin with hormone receptors on pancreatic acinar cells
    • Gardner JD, Conlon TP, Fink ML, and Bodanszky M (1976) Interaction of peptides related to secretin with hormone receptors on pancreatic acinar cells. Gastroenterology 71:965-970.
    • (1976) Gastroenterology , vol.71 , pp. 965-970
    • Gardner, J.D.1    Conlon, T.P.2    Fink, M.L.3    Bodanszky, M.4
  • 117
    • 0036289106 scopus 로고    scopus 로고
    • Characterization of the cellular and metabolic effects of a novel enzyme-resistant antagonist of glucose-dependent insulinotropic polypeptide
    • Gault VA, O'Harte FP, Harriott P, and Flatt PR (2002) Characterization of the cellular and metabolic effects of a novel enzyme-resistant antagonist of glucose-dependent insulinotropic polypeptide. Biochem Biophys Res Commun 290:1420-1426.
    • (2002) Biochem Biophys Res Commun , vol.290 , pp. 1420-1426
    • Gault, V.A.1    O'Harte, F.P.2    Harriott, P.3    Flatt, P.R.4
  • 118
    • 0032982394 scopus 로고    scopus 로고
    • Molecular and cell biology of the growth hormone-releasing hormone receptor
    • Gaylinn BD (1999) Molecular and cell biology of the growth hormone-releasing hormone receptor. Growth Horm IGF Res 9 (Suppl A):37-44.
    • (1999) Growth Horm IGF Res , vol.9 , Issue.SUPPL. A , pp. 37-44
    • Gaylinn, B.D.1
  • 119
    • 0033303550 scopus 로고    scopus 로고
    • The mutant growth hormone-releasing hormone (GHRH) receptor of the little mouse does not bind GHRH
    • Gaylinn BD, Dealmeida VI, Lyons CE Jr, Wu KC, Mayo KE, and Thorner MO (1999) The mutant growth hormone-releasing hormone (GHRH) receptor of the little mouse does not bind GHRH. Endocrinology 140:5066-5074.
    • (1999) Endocrinology , vol.140 , pp. 5066-5074
    • Gaylinn, B.D.1    Dealmeida, V.I.2    Lyons C.E., Jr.3    Wu, K.C.4    Mayo, K.E.5    Thorner, M.O.6
  • 120
    • 0027499362 scopus 로고
    • Molecular cloning and expression of a human anterior pituitary receptor for growth hormone-releasing hormone
    • Gaylinn BD, Harrison JK, Zysk JR, Lyons CE, Lynch KR, and Thorner MO (1993) Molecular cloning and expression of a human anterior pituitary receptor for growth hormone-releasing hormone. Mol Endocrinol 7:77-84.
    • (1993) Mol Endocrinol , vol.7 , pp. 77-84
    • Gaylinn, B.D.1    Harrison, J.K.2    Zysk, J.R.3    Lyons, C.E.4    Lynch, K.R.5    Thorner, M.O.6
  • 121
    • 0028058674 scopus 로고
    • Photoaffinity cross-linking to the pituitary receptor for growth hormone-releasing factor
    • Gaylinn BD, Lyons CE, Zysk JR, Clarke IJ, and Thorner MO (1994a) Photoaffinity cross-linking to the pituitary receptor for growth hormone-releasing factor. Endocrinology 135:950-955.
    • (1994) Endocrinology , vol.135 , pp. 950-955
    • Gaylinn, B.D.1    Lyons, C.E.2    Zysk, J.R.3    Clarke, I.J.4    Thorner, M.O.5
  • 122
    • 0028010013 scopus 로고
    • Assignment of the human growth hormone-releasing hormone receptor gene (GHRHR) to 7p14 by in situ hybridization
    • Gaylinn BD, von Kap-Herr C, Golden WL, and Thorner MO (1994b) Assignment of the human growth hormone-releasing hormone receptor gene (GHRHR) to 7p14 by in situ hybridization. Genomics 19:193-195.
    • (1994) Genomics , vol.19 , pp. 193-195
    • Gaylinn, B.D.1    Von Kap-Herr, C.2    Golden, W.L.3    Thorner, M.O.4
  • 123
    • 0030747857 scopus 로고    scopus 로고
    • GIP(6-30amide) contains the high affinity binding region of GIP and is a potent inhibitor of GIP1-42 action in vitro
    • Gelling RW, Coy DH, Pederson RA, Wheeler MB, Hinke S, Kwan T, and McIntosh CH (1997a) GIP(6-30amide) contains the high affinity binding region of GIP and is a potent inhibitor of GIP1-42 action in vitro. Regul Pept 69:151-154.
    • (1997) Regul Pept , vol.69 , pp. 151-154
    • Gelling, R.W.1    Coy, D.H.2    Pederson, R.A.3    Wheeler, M.B.4    Hinke, S.5    Kwan, T.6    McIntosh, C.H.7
  • 125
    • 0030913105 scopus 로고    scopus 로고
    • Localization of the domains involved in ligand binding and activation of the glucose-dependent insulinotropic polypeptide receptor
    • Gelling RW, Wheeler MB, Xue J, Gyomorey S, Nian C, Pederson RA, and McIntosh CH (1997b) Localization of the domains involved in ligand binding and activation of the glucose-dependent insulinotropic polypeptide receptor. Endocrinology 138:2640-2643.
    • (1997) Endocrinology , vol.138 , pp. 2640-2643
    • Gelling, R.W.1    Wheeler, M.B.2    Xue, J.3    Gyomorey, S.4    Nian, C.5    Pederson, R.A.6    McIntosh, C.H.7
  • 126
    • 0021344133 scopus 로고
    • Growth hormone-releasing factor regulates growth hormone mRNA in primary cultures of rat pituitary cells
    • Gick GG, Zeytin FN, Brazeau P, Ling NC, Esch FS, and Bancroft C (1984) Growth hormone-releasing factor regulates growth hormone mRNA in primary cultures of rat pituitary cells. Proc Natl Acad Sci USA 81:1553-1555.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 1553-1555
    • Gick, G.G.1    Zeytin, F.N.2    Brazeau, P.3    Ling, N.C.4    Esch, F.S.5    Bancroft, C.6
  • 127
    • 0033279518 scopus 로고    scopus 로고
    • Differential in vivo regulation of the pituitary growth hormone-releasing hormone (GHRH) receptor by GHRH in young and aged rats
    • Girard N, Boulanger L, Denis S, and Gaudreau P (1999) Differential in vivo regulation of the pituitary growth hormone-releasing hormone (GHRH) receptor by GHRH in young and aged rats. Endocrinology 140:2836-2842.
    • (1999) Endocrinology , vol.140 , pp. 2836-2842
    • Girard, N.1    Boulanger, L.2    Denis, S.3    Gaudreau, P.4
  • 128
    • 0027265595 scopus 로고
    • GHRH receptor of little mice contains a missense mutation in the extracellular domain that disrupts receptor function
    • Godfrey P, Rahal JO, Beamer WG, Copeland NG, Jenkins NA, and Mayo KE (1993) GHRH receptor of little mice contains a missense mutation in the extracellular domain that disrupts receptor function. Nat Genet 4:227-232.
    • (1993) Nat Genet , vol.4 , pp. 227-232
    • Godfrey, P.1    Rahal, J.O.2    Beamer, W.G.3    Copeland, N.G.4    Jenkins, N.A.5    Mayo, K.E.6
  • 129
    • 0024600552 scopus 로고
    • Characterization of the receptor for glucagon-like peptide-1(7-36)amide on plasma membranes from rat insulinoma-derived cells by covalent cross-linking
    • Goke R, Cole T, and Conlon JM (1989a) Characterization of the receptor for glucagon-like peptide-1(7-36)amide on plasma membranes from rat insulinoma-derived cells by covalent cross-linking. J Mol Endocrinol 2:93-98.
    • (1989) J Mol Endocrinol , vol.2 , pp. 93-98
    • Goke, R.1    Cole, T.2    Conlon, J.M.3
  • 130
    • 0023838544 scopus 로고
    • Receptors for glucagon-like peptide-1(7-36) amide on rat insulinoma-derived cells
    • Goke R and Conlon JM (1988) Receptors for glucagon-like peptide-1(7-36) amide on rat insulinoma-derived cells. J Endocrinol 116:357-362.
    • (1988) J Endocrinol , vol.116 , pp. 357-362
    • Goke, R.1    Conlon, J.M.2
  • 131
    • 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 β-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 β-cells. J Biol Chem 268:19650-19655.
    • (1993) J Biol Chem , vol.268 , pp. 19650-19655
    • Goke, R.1    Fehmann, H.-C.2    Linn, T.3    Schmidt, H.4    Krause, M.5    Eng, J.6    Goke, B.7
  • 132
    • 0028232090 scopus 로고
    • Glycosylation of the GLP-1 receptor is a prerequisite for regular receptor function
    • Goke R, Just R, Lankat-Buttgereit B, and Goke B (1994) Glycosylation of the GLP-1 receptor is a prerequisite for regular receptor function. Peptides 15:675-681.
    • (1994) Peptides , vol.15 , pp. 675-681
    • Goke, R.1    Just, R.2    Lankat-Buttgereit, B.3    Goke, B.4
  • 133
    • 0028867442 scopus 로고
    • Distribution of GLP-1 binding sites in the rat brain: Evidence that exendin-4 is a ligand of brain GLP-1 binding sites
    • Goke R, Larsen PJ, Mikkelsen JD, and Sheikh SP (1995) Distribution of GLP-1 binding sites in the rat brain: evidence that exendin-4 is a ligand of brain GLP-1 binding sites. Eur J Neurosci 7:2294-2300.
    • (1995) Eur J Neurosci , vol.7 , pp. 2294-2300
    • Goke, R.1    Larsen, P.J.2    Mikkelsen, J.D.3    Sheikh, S.P.4
  • 134
    • 0026548251 scopus 로고
    • Solubilization of active GLP-1(736)amide receptors from RINm5F plasma membranes
    • Goke R, Oltmer B, Sheikh SP, and Goke B (1992) Solubilization of active GLP-1(736)amide receptors from RINm5F plasma membranes. FEBS Lett 300:232-236.
    • (1992) FEBS Lett , vol.300 , pp. 232-236
    • Goke, R.1    Oltmer, B.2    Sheikh, S.P.3    Goke, B.4
  • 137
    • 0029077296 scopus 로고
    • Cloning, functional expression and chromosomal localization of the human pancreatic islet glucose-dependent insulinotropic polypeptide receptor
    • Gremlich S, Porret A, Hani EH, Cherif D, Vionnet D, Froguel P, and Thorens B (1995) Cloning, functional expression and chromosomal localization of the human pancreatic islet glucose-dependent insulinotropic polypeptide receptor. Diabetes 44:1202-1208.
    • (1995) Diabetes , vol.44 , pp. 1202-1208
    • Gremlich, S.1    Porret, A.2    Hani, E.H.3    Cherif, D.4    Vionnet, D.5    Froguel, P.6    Thorens, B.7
  • 138
    • 0000267888 scopus 로고
    • Characterization of high affinity receptors for glucagon-like peptide-1 (7-36)amide on a somatostatin-secreting cell line
    • Gros L, Demiprence E, Bataille D, and Kervra A (1992) Characterization of high affinity receptors for glucagon-like peptide-1 (7-36)amide on a somatostatin-secreting cell line. Biomed Res 13:143-150.
    • (1992) Biomed Res , vol.13 , pp. 143-150
    • Gros, L.1    Demiprence, E.2    Bataille, D.3    Kervra, A.4
  • 140
    • 0032966882 scopus 로고    scopus 로고
    • Glucagon-like peptide-1 promotes satiety and reduces food intake in patients with diabetes mellitus type 2
    • Gutzwiller JP, Drewe J, Goke B, Schmidt H, Rohrer B, Lareida J, and Beglinger C (1999) Glucagon-like peptide-1 promotes satiety and reduces food intake in patients with diabetes mellitus type 2. Am J Physiol 276:R1541-R1544.
    • (1999) Am J Physiol , vol.276
    • Gutzwiller, J.P.1    Drewe, J.2    Goke, B.3    Schmidt, H.4    Rohrer, B.5    Lareida, J.6    Beglinger, C.7
  • 141
    • 0025960524 scopus 로고
    • Reduced peptide bond pseudopeptide analogues of secretin. A new class of secretin receptor antagonists
    • Haffar BM, Hocart SJ, Coy DH, Mantey S, Chiang HC, and Jensen RT (1991) Reduced peptide bond pseudopeptide analogues of secretin. A new class of secretin receptor antagonists. J Biol Chem 266:316-322.
    • (1991) J Biol Chem , vol.266 , pp. 316-322
    • Haffar, B.M.1    Hocart, S.J.2    Coy, D.H.3    Mantey, S.4    Chiang, H.C.5    Jensen, R.T.6
  • 143
    • 0035831283 scopus 로고    scopus 로고
    • Different domains in the third intracellular loop of the GLP-1 receptor are responsible for Galpha(s) and Galpha(i)/Galpha(o) activation
    • Hallbrink M, Holmqvist T, Olsson M, Ostenson CG, Efendic S, and Langel U (2001) Different domains in the third intracellular loop of the GLP-1 receptor are responsible for Galpha(s) and Galpha(i)/Galpha(o) activation. Biochim Biophys Acta 1546:79-86.
    • (2001) Biochim Biophys Acta , vol.1546 , pp. 79-86
    • Hallbrink, M.1    Holmqvist, T.2    Olsson, M.3    Ostenson, C.G.4    Efendic, S.5    Langel, U.6
  • 144
    • 0036776259 scopus 로고    scopus 로고
    • Expression of growth hormone-releasing hormone and its receptor splice variants in human prostate cancer
    • Halmos G, Schally AV, Czompoly T, Krupa M, Varga JL, and Rekasi Z (2002) Expression of growth hormone-releasing hormone and its receptor splice variants in human prostate cancer. J Clin Endocrinol Metab 87:4707-4714.
    • (2002) J Clin Endocrinol Metab , vol.87 , pp. 4707-4714
    • Halmos, G.1    Schally, A.V.2    Czompoly, T.3    Krupa, M.4    Varga, J.L.5    Rekasi, Z.6
  • 145
    • 0021847770 scopus 로고
    • Expression of human growth hormone-releasing factor in transgenic mice results in increased somatic growth
    • Hammer RE, Brinster RL, Rosenfeld MG, Evans RM, and Mayo KE (1985) Expression of human growth hormone-releasing factor in transgenic mice results in increased somatic growth. Nature (Lond) 315:413-416.
    • (1985) Nature (Lond) , vol.315 , pp. 413-416
    • Hammer, R.E.1    Brinster, R.L.2    Rosenfeld, M.G.3    Evans, R.M.4    Mayo, K.E.5
  • 146
    • 0023752693 scopus 로고
    • Effect of truncated glucagon-like peptide 1 on cAMP in rat gastric glands and HGT-1 human gastric cancer cells
    • Hansen AB, Gespach CP, Rosselin GE, and Holst JJ (1988) Effect of truncated glucagon-like peptide 1 on cAMP in rat gastric glands and HGT-1 human gastric cancer cells. FEBS Lett 236:119-122.
    • (1988) FEBS Lett , vol.236 , pp. 119-122
    • Hansen, A.B.1    Gespach, C.P.2    Rosselin, G.E.3    Holst, J.J.4
  • 147
    • 0035134790 scopus 로고    scopus 로고
    • The growth hormone-releasing hormone receptor: Desensitisation following short-term agonist exposure
    • Hansen BS, Gerlach LO, Hansen A, Foged C, and Andersen PH (2001) The growth hormone-releasing hormone receptor: desensitisation following short-term agonist exposure. Pharmacol Toxicol 88:81-88.
    • (2001) Pharmacol Toxicol , vol.88 , pp. 81-88
    • Hansen, B.S.1    Gerlach, L.O.2    Hansen, A.3    Foged, C.4    Andersen, P.H.5
  • 149
    • 0035716295 scopus 로고    scopus 로고
    • Family-B G-protein-coupled receptors
    • REVIEWS3013
    • Harmar AJ (2001) Family-B G-protein-coupled receptors. Genome Biol 2:REVIEWS3013.
    • (2001) Genome Biol , vol.2
    • Harmar, A.J.1
  • 151
    • 0037198482 scopus 로고    scopus 로고
    • Immunoneutralization of endogenous glucagon-like peptide-2 reduces adaptive intestinal growth in diabetic rats
    • Hartmann B, Thulesen J, Hare KJ, Kissow H, Orskov C, Poulsen SS, and Holst JJ (2002) Immunoneutralization of endogenous glucagon-like peptide-2 reduces adaptive intestinal growth in diabetic rats. Regul Pept 105:173-179.
    • (2002) Regul Pept , vol.105 , pp. 173-179
    • Hartmann, B.1    Thulesen, J.2    Hare, K.J.3    Kissow, H.4    Orskov, C.5    Poulsen, S.S.6    Holst, J.J.7
  • 152
    • 0033680541 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV inhibition enhances the intestinotrophic effect of glucagon-like peptide-2 in rats and mice
    • Hartmann B, Thulesen J, Kissow H, Thulesen S, Orskov C, Ropke C, Paulsen SS, and Holst JJ (2000b) Dipeptidyl peptidase IV inhibition enhances the intestinotrophic effect of glucagon-like peptide-2 in rats and mice. Endocrinology 141:4013-4020.
    • (2000) Endocrinology , vol.141 , pp. 4013-4020
    • Hartmann, B.1    Thulesen, J.2    Kissow, H.3    Thulesen, S.4    Orskov, C.5    Ropke, C.6    Paulsen, S.S.7    Holst, J.J.8
  • 154
    • 0035264042 scopus 로고    scopus 로고
    • Biological activities of two porcine growth hormone-releasing hormone receptor isoforms
    • Hassan HA (2001) Biological activities of two porcine growth hormone-releasing hormone receptor isoforms. Arch Biochem Biophys 387:20-26.
    • (2001) Arch Biochem Biophys , vol.387 , pp. 20-26
    • Hassan, H.A.1
  • 155
    • 0028868548 scopus 로고
    • Characterization of growth hormone-releasing hormone (GHRH) binding to cloned porcine GHRH receptor
    • Hassan HA, Hsiung HM, Zhang XY, Smith DP, Smiley DL, and Heiman ML (1995) Characterization of growth hormone-releasing hormone (GHRH) binding to cloned porcine GHRH receptor. Peptides 16:1469-1473.
    • (1995) Peptides , vol.16 , pp. 1469-1473
    • Hassan, H.A.1    Hsiung, H.M.2    Zhang, X.Y.3    Smith, D.P.4    Smiley, D.L.5    Heiman, M.L.6
  • 156
    • 0030975613 scopus 로고    scopus 로고
    • Insulinotropic glucagon-like peptide I receptor expression in glucagon-producing alpha-cells of the rat endocrine pancreas
    • Heller RS, Kieffer TJ, and Habener JF (1997) Insulinotropic glucagon-like peptide I receptor expression in glucagon-producing alpha-cells of the rat endocrine pancreas. Diabetes 46:785-791.
    • (1997) Diabetes , vol.46 , pp. 785-791
    • Heller, R.S.1    Kieffer, T.J.2    Habener, J.F.3
  • 157
    • 0036317496 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV-resistant [D-Ala(2)]glucose-dependent insulinotropic polypeptide (GIP) improves glucose tolerance in normal and obese diabetic rats
    • Hinke SA, Gelling RW, Pederson RA, Manhart S, Nian C, Demuth HU, and McIntosh CH (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.
    • (2002) Diabetes , vol.51 , pp. 652-661
    • Hinke, S.A.1    Gelling, R.W.2    Pederson, R.A.3    Manhart, S.4    Nian, C.5    Demuth, H.U.6    McIntosh, C.H.7
  • 159
    • 0032812191 scopus 로고    scopus 로고
    • The human secretin receptor gene: Genomic organization and promoter characterization
    • Ho PK, Fong RS, Kai HS, Lau EH, Ngan ES, Cotton CU, and Chow BK (1999) The human secretin receptor gene: genomic organization and promoter characterization. FEBS Lett 455:209-214.
    • (1999) FEBS Lett , vol.455 , pp. 209-214
    • Ho, P.K.1    Fong, R.S.2    Kai, H.S.3    Lau, E.H.4    Ngan, E.S.5    Cotton, C.U.6    Chow, B.K.7
  • 160
    • 0023920443 scopus 로고
    • Intracellular calcium concentration and growth hormone secretion in individual somatotropes: Effects of growth hormone-releasing factor and somatostatin
    • Holl RW, Thorner MO, and Leong DA (1988) Intracellular calcium concentration and growth hormone secretion in individual somatotropes: effects of growth hormone-releasing factor and somatostatin. Endocrinology 122:2927-2932.
    • (1988) Endocrinology , vol.122 , pp. 2927-2932
    • Holl, R.W.1    Thorner, M.O.2    Leong, D.A.3
  • 161
    • 0030876081 scopus 로고    scopus 로고
    • The pathogenesis of NIDDM involves a defective expression of the GIP receptor
    • Holst JJ, Gromada J, and Nauck MA (1997) The pathogenesis of NIDDM involves a defective expression of the GIP receptor. Diabetologia 40:984-986.
    • (1997) Diabetologia , vol.40 , pp. 984-986
    • Holst, J.J.1    Gromada, J.2    Nauck, M.A.3
  • 162
    • 15844385219 scopus 로고    scopus 로고
    • Multiple extracellular loop domains contribute critical determinants for agonist binding and activation of the secretin receptor
    • Holtmann MH, Ganguli S, Hadac EM, Dolu V, and Miller LJ (1996a) Multiple extracellular loop domains contribute critical determinants for agonist binding and activation of the secretin receptor. J Biol Chem 271:14944-14949.
    • (1996) J Biol Chem , vol.271 , pp. 14944-14949
    • Holtmann, M.H.1    Ganguli, S.2    Hadac, E.M.3    Dolu, V.4    Miller, L.J.5
  • 163
    • 0029043789 scopus 로고
    • Critical contributions of aminoterminal extracellular domains in agonist binding and activation of secretin and vasoactive intestinal polypeptide receptors. Studies of chimeric receptors
    • Holtmann MH, Hadac EM, and Miller LJ (1995) Critical contributions of aminoterminal extracellular domains in agonist binding and activation of secretin and vasoactive intestinal polypeptide receptors. Studies of chimeric receptors. J Biol Chem 270:14394-14398.
    • (1995) J Biol Chem , vol.270 , pp. 14394-14398
    • Holtmann, M.H.1    Hadac, E.M.2    Miller, L.J.3
  • 164
    • 0029790078 scopus 로고    scopus 로고
    • Role of receptor phosphorylation in desensitization and internalization of the secretin receptor
    • Holtmann MR, Roettger BF, Pinon DI, and Miller LJ (1996b) Role of receptor phosphorylation in desensitization and internalization of the secretin receptor. J Biol Chem 271:23566-23571.
    • (1996) J Biol Chem , vol.271 , pp. 23566-23571
    • Holtmann, M.R.1    Roettger, B.F.2    Pinon, D.I.3    Miller, L.J.4
  • 165
    • 0028978243 scopus 로고
    • Activation of a cAMP-regulated Ca2+signaling pathway in pancreatic b-cells by the insulinotropic hormone glucagonlike peptide-1
    • Holz GG, Leech CA, and Habener JF (1995) Activation of a cAMP-regulated Ca2+signaling pathway in pancreatic b-cells by the insulinotropic hormone glucagonlike peptide-1. J Biol Chem 270:17749-17757.
    • (1995) J Biol Chem , vol.270 , pp. 17749-17757
    • Holz, G.G.1    Leech, C.A.2    Habener, J.F.3
  • 166
    • 0033553547 scopus 로고    scopus 로고
    • cAMP dependent mobilization of intracellular Ca2+ stores by activation of ryanodine receptors in pancreatic beta-cells. A Ca2+ signaling system stimulated by the insulinotropic hormone glucagon-like peptide-1-(7-37)
    • Holz GG, Leech CA, Heller RS, Castonguay M, and Habener JF (1999) cAMPdependent mobilization of intracellular Ca2+ stores by activation of ryanodine receptors in pancreatic beta-cells. A Ca2+ signaling system stimulated by the insulinotropic hormone glucagon-like peptide-1-(7-37). J Biol Chem 274:14147-14156.
    • (1999) J Biol Chem , vol.274 , pp. 14147-14156
    • Holz, G.G.1    Leech, C.A.2    Heller, R.S.3    Castonguay, M.4    Habener, J.F.5
  • 167
    • 0021691124 scopus 로고
    • Human glucagon-like peptides 1 and 2 activate rat brain adenylate cyclase
    • Hoosein NM and Gurd RS (1984a) Human glucagon-like peptides 1 and 2 activate rat brain adenylate cyclase. FEBS Lett 178:83-86.
    • (1984) FEBS Lett , vol.178 , pp. 83-86
    • Hoosein, N.M.1    Gurd, R.S.2
  • 168
    • 0021136896 scopus 로고
    • Identification of glucagon receptors in rat brain
    • Hoosein NM and Gurd RS (1984b) Identification of glucagon receptors in rat brain. Proc Natl Acad Sci USA 81:4368-4372.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 4368-4372
    • Hoosein, N.M.1    Gurd, R.S.2
  • 169
    • 0036479823 scopus 로고    scopus 로고
    • Isolated GH deficiency due to inactivating mutation of GHRH receptor
    • Horikawa R (2002) [Isolated GH deficiency due to inactivating mutation of GHRH receptor]. Nippon Rinsho 60:297-305.
    • (2002) Nippon Rinsho , vol.60 , pp. 297-305
    • Horikawa, R.1
  • 170
    • 0035001171 scopus 로고    scopus 로고
    • Molecular cloning of ovine and bovine growth hormone-releasing hormone receptors: The ovine receptor is C-terminally truncated
    • Horikawa R, Gaylinn BD, Lyons CE Jr, and Thorner MO (2001) Molecular cloning of ovine and bovine growth hormone-releasing hormone receptors: the ovine receptor is C-terminally truncated. Endocrinology 142:2660-2668.
    • (2001) Endocrinology , vol.142 , pp. 2660-2668
    • Horikawa, R.1    Gaylinn, B.D.2    Lyons C.E., Jr.3    Thorner, M.O.4
  • 172
    • 0027279412 scopus 로고
    • Structure and functional expression of a complementary DNA for porcine growth hormone-releasing hormone receptor
    • Hsiung HM, Smith DP, Zhang XY, Bennett T, Rosteck PR Jr, and Lai MH (1993) Structure and functional expression of a complementary DNA for porcine growth hormone-releasing hormone receptor. Neuropeptides 25:1-10.
    • (1993) Neuropeptides , vol.25 , pp. 1-10
    • Hsiung, H.M.1    Smith, D.P.2    Zhang, X.Y.3    Bennett, T.4    Rosteck P.R., Jr.5    Lai, M.H.6
  • 173
    • 0033847126 scopus 로고    scopus 로고
    • Glucagon receptors on human islet cells contribute to glucose competence of insulin release
    • Huypens P, Ling Z, Pipeleers D, and Schuit F (2000) Glucagon receptors on human islet cells contribute to glucose competence of insulin release. Diabetologia 43:1012-1019.
    • (2000) Diabetologia , vol.43 , pp. 1012-1019
    • Huypens, P.1    Ling, Z.2    Pipeleers, D.3    Schuit, F.4
  • 174
    • 0033597229 scopus 로고    scopus 로고
    • Cloning and characterization of the 5′-flanking region of the human growth hormone-releasing hormone receptor gene
    • Iguchi G, Okimura Y, Takahashi T, Mizuno I, Fumoto M, Takahashi Y, Kaji H, Abe H, and Chihara K (1999) Cloning and characterization of the 5′-flanking region of the human growth hormone-releasing hormone receptor gene. J Biol Chem 274:12108-12114.
    • (1999) J Biol Chem , vol.274 , pp. 12108-12114
    • Iguchi, G.1    Okimura, Y.2    Takahashi, T.3    Mizuno, I.4    Fumoto, M.5    Takahashi, Y.6    Kaji, H.7    Abe, H.8    Chihara, K.9
  • 175
    • 0035795227 scopus 로고    scopus 로고
    • Molecular evolution of proglucagon
    • Irwin DM (2001) Molecular evolution of proglucagon. Regul Pept 98:1-12.
    • (2001) Regul Pept , vol.98 , pp. 1-12
    • Irwin, D.M.1
  • 176
    • 0015325141 scopus 로고
    • Unusual effect of secretin on serum gastrin, serum calcium and gastric acid secretion in a patient with suspected Zollinger-Ellison syndrome
    • Isenberg JI, Walsh JH, Passaro E Jr, Moore EW, and Grossman MI (1972) Unusual effect of secretin on serum gastrin, serum calcium and gastric acid secretion in a patient with suspected Zollinger-Ellison syndrome. Gastroenterology 62:626-631.
    • (1972) Gastroenterology , vol.62 , pp. 626-631
    • Isenberg, J.I.1    Walsh, J.H.2    Passaro E., Jr.3    Moore, E.W.4    Grossman, M.I.5
  • 178
    • 0021342010 scopus 로고
    • Structural analysis of the hepatic glucagon receptor. Identification of a guanine nucleotide-sensitive hormone-binding region
    • Iyengar R and Herberg JT (1984) Structural analysis of the hepatic glucagon receptor. Identification of a guanine nucleotide-sensitive hormone-binding region. J Biol Chem 259:5222-5229.
    • (1984) J Biol Chem , vol.259 , pp. 5222-5229
    • Iyengar, R.1    Herberg, J.T.2
  • 181
    • 0023950336 scopus 로고
    • Distribution of glucagonlike peptide 1 (GLP-1), glucagon and glicentin in the rat brain: An immunocytochemical study
    • Jin S-LC, Han VKM, Simmons JG, Towle AC, Lauder JM, and Lund PK (1988) Distribution of glucagonlike peptide 1 (GLP-1), glucagon and glicentin in the rat brain: an immunocytochemical study. J Comp Neurol 271:519-532.
    • (1988) J Comp Neurol , vol.271 , pp. 519-532
    • Jin, S.-L.C.1    Han, V.K.M.2    Simmons, J.G.3    Towle, A.C.4    Lauder, J.M.5    Lund, P.K.6
  • 182
    • 0032712930 scopus 로고    scopus 로고
    • Evidence for kinship between diverse G-protein coupled receptors
    • Josefsson LG (1999) Evidence for kinship between diverse G-protein coupled receptors. Gene (Amst) 239:333-340.
    • (1999) Gene (Amst) , vol.239 , pp. 333-340
    • Josefsson, L.G.1
  • 183
    • 0036066641 scopus 로고    scopus 로고
    • Bedtime administration of NN2211, a long-acting GLP-1 derivative, substantially reduces fasting and postprandial glycemia in type 2 diabetes
    • Juhl CB, Hollingdal M, Sturis J, Jakobsen G, Agerso H, Veldhuis J, Porksen N, and Schmitz O (2002) Bedtime administration of NN2211, a long-acting GLP-1 derivative, substantially reduces fasting and postprandial glycemia in type 2 diabetes. Diabetes 51:424-429.
    • (2002) Diabetes , vol.51 , pp. 424-429
    • Juhl, C.B.1    Hollingdal, M.2    Sturis, J.3    Jakobsen, G.4    Agerso, H.5    Veldhuis, J.6    Porksen, N.7    Schmitz, O.8
  • 184
    • 0031036423 scopus 로고    scopus 로고
    • Investigation of growth hormone releasing hormone receptor structure and activity using yeast expression technologies
    • Kajkowski EM, Price LA, Pausch MH, Young KH, and Ozenberger BA (1997) Investigation of growth hormone releasing hormone receptor structure and activity using yeast expression technologies. J Recept Signal Transduct Res 17:293-303.
    • (1997) J Recept Signal Transduct Res , vol.17 , pp. 293-303
    • Kajkowski, E.M.1    Price, L.A.2    Pausch, M.H.3    Young, K.H.4    Ozenberger, B.A.5
  • 185
    • 0035886966 scopus 로고    scopus 로고
    • cAMP-regulated guanine nucleotide exchange factor II (Epac2) mediates Ca(2+)-induced Ca(2+) release in INS-1 pancreatic beta-cells
    • Kang G, Chepurny OG, and Holz GG (2001) cAMP-regulated guanine nucleotide exchange factor II (Epac2) mediates Ca(2+)-induced Ca(2+) release in INS-1 pancreatic beta-cells. J Physiol (Lond) 536:375-385.
    • (2001) J Physiol (Lond) , vol.536 , pp. 375-385
    • Kang, G.1    Chepurny, O.G.2    Holz, G.G.3
  • 186
    • 0035824548 scopus 로고    scopus 로고
    • Critical role of cAMP-GEFII/Rim2 complex in incretin-potentiated insulin secretion
    • Kashima Y, Miki T, Shibasaki T, Ozaki N, Miyazaki M, Yano H, and Seino S (2001) Critical role of cAMP-GEFII/Rim2 complex in incretin-potentiated insulin secretion. J Biol Chem 276:45045-45053.
    • (2001) J Biol Chem , vol.276 , pp. 45045-45053
    • Kashima, Y.1    Miki, T.2    Shibasaki, T.3    Ozaki, N.4    Miyazaki, M.5    Yano, H.6    Seino, S.7
  • 187
    • 0036198285 scopus 로고    scopus 로고
    • Interactions of glucagon-like peptide-1 (GLP-1) with the blood-brain barrier
    • Kastin AJ, Akerstrom V, and Pan W (2002) Interactions of glucagon-like peptide-1 (GLP-1) with the blood-brain barrier. J Mol Neurosci 18:7-14.
    • (2002) J Mol Neurosci , vol.18 , pp. 7-14
    • Kastin, A.J.1    Akerstrom, V.2    Pan, W.3
  • 188
    • 0032906822 scopus 로고    scopus 로고
    • Glucagonlike peptide-2 enhances small intestinal absorptive function and mucosal mass in vivo
    • Kato Y, Yu D, and Schwartz MZ (1999) Glucagonlike peptide-2 enhances small intestinal absorptive function and mucosal mass in vivo. J Pediatr Surg 34:18-20.
    • (1999) J Pediatr Surg , vol.34 , pp. 18-20
    • Kato, Y.1    Yu, D.2    Schwartz, M.Z.3
  • 189
    • 0028893424 scopus 로고
    • Evidence that glucagon stimulates insulin secretion through its own receptor in rats
    • Kawai K, Yokota C, Ohashi S, Watanabe Y, and Yamashita K (1995) Evidence that glucagon stimulates insulin secretion through its own receptor in rats. Diabetologia 38:274-276.
    • (1995) Diabetologia , vol.38 , pp. 274-276
    • Kawai, K.1    Yokota, C.2    Ohashi, S.3    Watanabe, Y.4    Yamashita, K.5
  • 190
    • 0000153983 scopus 로고
    • Extractable glucagon of the human pancreas
    • Kenny AJ (1955) Extractable glucagon of the human pancreas. J Clin Endocrinol Metab 15:1089-1105.
    • (1955) J Clin Endocrinol Metab , vol.15 , pp. 1089-1105
    • Kenny, A.J.1
  • 191
    • 0033304603 scopus 로고    scopus 로고
    • The glucagon-like peptides
    • Kieffer TJ and Habener JF (1999) The glucagon-like peptides. Endocr Rev 20:876-913.
    • (1999) Endocr Rev , vol.20 , pp. 876-913
    • Kieffer, T.J.1    Habener, J.F.2
  • 192
    • 0029118049 scopus 로고
    • Degradation of glucose-dependent insulinotropic polypeptide and truncated glucagon-like peptide 1 in vitro and in vivo by dipeptidyl peptidase IV
    • Kieffer TJ, McIntosh CH, and Pederson RA (1995) Degradation of glucose-dependent insulinotropic polypeptide and truncated glucagon-like peptide 1 in vitro and in vivo by dipeptidyl peptidase IV. Endocrinology 136:3585-3596.
    • (1995) Endocrinology , vol.136 , pp. 3585-3596
    • Kieffer, T.J.1    McIntosh, C.H.2    Pederson, R.A.3
  • 193
    • 0001693313 scopus 로고
    • Aqueous extracts of pancreas
    • Kimball CP and Murlin JR (1923) Aqueous extracts of pancreas. J Biol Chem 58:337-346.
    • (1923) J Biol Chem , vol.58 , pp. 337-346
    • Kimball, C.P.1    Murlin, J.R.2
  • 194
    • 0034681150 scopus 로고    scopus 로고
    • Antitumorigenic actions of growth hormone-releasing hormone antagonists
    • Kineman RD (2000) Antitumorigenic actions of growth hormone-releasing hormone antagonists. Proc Natl Acad Sci USA 97:532-534.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 532-534
    • Kineman, R.D.1
  • 195
    • 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. 16-19
    • Kolligs, F.1    Fehmann, H.-C.2    Goke, R.3    Goke, B.4
  • 196
    • 0025253193 scopus 로고
    • Secretin: Structure of the precursor and tissue distribution of the mRNA
    • Kopin AS, Wheeler MB, and Leiter AB (1990) Secretin: structure of the precursor and tissue distribution of the mRNA. Proc Natl Acad Sci USA 87:2299-2303.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 2299-2303
    • Kopin, A.S.1    Wheeler, M.B.2    Leiter, A.B.3
  • 198
    • 0031044446 scopus 로고    scopus 로고
    • Thyroid hormone and glucocorticoid regulation of pituitary growth hormone-releasing hormone receptor gene expression
    • Korytko AI and Cuttler L (1997) Thyroid hormone and glucocorticoid regulation of pituitary growth hormone-releasing hormone receptor gene expression. J Endocrinol 152:R13-R37.
    • (1997) J Endocrinol , vol.152
    • Korytko, A.I.1    Cuttler, L.2
  • 199
    • 0029965376 scopus 로고    scopus 로고
    • Developmental regulation of pituitary growth hormone-releasing hormone receptor gene expression in the rat
    • Korytko AI, Zeitler P, and Cuttler L (1996) Developmental regulation of pituitary growth hormone-releasing hormone receptor gene expression in the rat. Endocrinology 137:1326-1331.
    • (1996) Endocrinology , vol.137 , pp. 1326-1331
    • Korytko, A.I.1    Zeitler, P.2    Cuttler, L.3
  • 200
    • 0001782772 scopus 로고    scopus 로고
    • Synthetic analogs of growth hormone releasing factor (GHRF) with improved pharmaceutical properties
    • Berc BB and Walker RF eds, Springer Publishing, New York
    • Kubiak TM, Friedman AR, and Moseley WM (1996) Synthetic analogs of growth hormone releasing factor (GHRF) with improved pharmaceutical properties, in Growth Hormone Secretagogues (Berc BB and Walker RF eds) pp 31-52, Springer Publishing, New York.
    • (1996) Growth Hormone Secretagogues , pp. 31-52
    • Kubiak, T.M.1    Friedman, A.R.2    Moseley, W.M.3
  • 201
    • 10544249875 scopus 로고    scopus 로고
    • Identification of two missense mutations in the GIP receptor gene: A functional study and association analysis with NIDDM: No evidence of association with Japanese NIDDM subjects
    • Kubota A, Yamada Y, Hayami T, Yasuda K, Someya Y, Ihara Y, Kagimoto S, Watanabe R, Taminato T, Tsuda K, et al. (1996) Identification of two missense mutations in the GIP receptor gene: a functional study and association analysis with NIDDM: no evidence of association with Japanese NIDDM subjects. Diabetes 45:1701-1705.
    • (1996) Diabetes , vol.45 , pp. 1701-1705
    • Kubota, A.1    Yamada, Y.2    Hayami, T.3    Yasuda, K.4    Someya, Y.5    Ihara, Y.6    Kagimoto, S.7    Watanabe, R.8    Taminato, T.9    Tsuda, K.10
  • 204
    • 0029886191 scopus 로고    scopus 로고
    • Gene expression of the receptor for growth-hormone-releasing hormone is physiologically regulated by glucocorticoids and estrogen
    • Lam KS, Lee MF, Tam SP, and Srivastava G (1996) Gene expression of the receptor for growth-hormone-releasing hormone is physiologically regulated by glucocorticoids and estrogen. Neuroendocrinology 63:475-480.
    • (1996) Neuroendocrinology , vol.63 , pp. 475-480
    • Lam, K.S.1    Lee, M.F.2    Tam, S.P.3    Srivastava, G.4
  • 206
    • 0030747262 scopus 로고    scopus 로고
    • Cloning and characterization of the 5′flanking sequences (promoter region) of the human GLP-1 receptor gene
    • Lankat-Buttgereit B and Goke B (1997) Cloning and characterization of the 5′flanking sequences (promoter region) of the human GLP-1 receptor gene. Peptides 18:617-624.
    • (1997) Peptides , vol.18 , pp. 617-624
    • Lankat-Buttgereit, B.1    Goke, B.2
  • 208
    • 0031029936 scopus 로고    scopus 로고
    • Distribution of glucagon-like peptide-1 and other preproglucagon-derived peptides in the rat hypothalamus and brainstem
    • Larsen PJ, Tang-Christensen M, Holst JJ, and Orskov C (1997) Distribution of glucagon-like peptide-1 and other preproglucagon-derived peptides in the rat hypothalamus and brainstem. Neuroscience 77:257-270.
    • (1997) Neuroscience , vol.77 , pp. 257-270
    • Larsen, P.J.1    Tang-Christensen, M.2    Holst, J.J.3    Orskov, C.4
  • 209
    • 0034999426 scopus 로고    scopus 로고
    • Differential GHreleasing hormone regulation of GHRH receptor mRNA expression in the rat pituitary
    • Lasko CM, Korytko AI, Wehrenberg WB, and Cuttler L (2001) Differential GHreleasing hormone regulation of GHRH receptor mRNA expression in the rat pituitary. Am J Physiol Endocrinol Metab 280:E626-E631.
    • (2001) Am J Physiol Endocrinol Metab , vol.280
    • Lasko, C.M.1    Korytko, A.I.2    Wehrenberg, W.B.3    Cuttler, L.4
  • 212
    • 0037414781 scopus 로고    scopus 로고
    • Glucagon-like peptide-1 receptor signaling modulates beta cell apoptosis
    • Li Y, Hansotia T, Yusta B, Ris F, Halban PA, and Drucker DJ (2003) Glucagon-like peptide-1 receptor signaling modulates beta cell apoptosis. J Biol Chem 278:471-478.
    • (2003) J Biol Chem , vol.278 , pp. 471-478
    • Li, Y.1    Hansotia, T.2    Yusta, B.3    Ris, F.4    Halban, P.A.5    Drucker, D.J.6
  • 213
    • 0036718447 scopus 로고    scopus 로고
    • Glucagon-like peptide-1 inhibits pancreatic ATP-sensitive potassium channels via a protein kinase A- and ADP-dependent mechanism
    • Light PE, Manning Fox JE, Riedel MJ, and Wheeler MB (2002) Glucagon-like peptide-1 inhibits pancreatic ATP-sensitive potassium channels via a protein kinase A- and ADP-dependent mechanism. Mol Endocrinol 16:2135-2144.
    • (2002) Mol Endocrinol , vol.16 , pp. 2135-2144
    • Light, P.E.1    Manning Fox, J.E.2    Riedel, M.J.3    Wheeler, M.B.4
  • 214
    • 0027076516 scopus 로고
    • Pit-1-dependent expression of the receptor for growth hormone releasing factor mediates pituitary cell growth
    • Lin C, Lin SC, Chang CP, and Rosenfeld MG (1992) Pit-1-dependent expression of the receptor for growth hormone releasing factor mediates pituitary cell growth. Nature (Lond) 360:765-768.
    • (1992) Nature (Lond) , vol.360 , pp. 765-768
    • Lin, C.1    Lin, S.C.2    Chang, C.P.3    Rosenfeld, M.G.4
  • 215
    • 0027236844 scopus 로고
    • Molecular basis of the little mouse phenotype and implications for cell type-specific growth
    • Lin SC, Lin CR, Gukovsky I, Lusis AJ, Sawchenko PE, and Rosenfeld MG (1993) Molecular basis of the little mouse phenotype and implications for cell type-specific growth. Nature (Lond) 364:208-213.
    • (1993) Nature (Lond) , vol.364 , pp. 208-213
    • Lin, S.C.1    Lin, C.R.2    Gukovsky, I.3    Lusis, A.J.4    Sawchenko, P.E.5    Rosenfeld, M.G.6
  • 218
    • 0021180916 scopus 로고
    • Synthesis and in vitro bioactivity of C-terminal deleted analogs of human growth hormone-releasing factor
    • Ling N, Baird A, Wehrenberg WB, Ueno N, Munegumi T, and Brazeau P (1984a) Synthesis and in vitro bioactivity of C-terminal deleted analogs of human growth hormone-releasing factor. Biochem Biophys Res Commun 123:854-861.
    • (1984) Biochem Biophys Res Commun , vol.123 , pp. 854-861
    • Ling, N.1    Baird, A.2    Wehrenberg, W.B.3    Ueno, N.4    Munegumi, T.5    Brazeau, P.6
  • 219
    • 0344650195 scopus 로고
    • Isolation, primary structure and synthesis of human hypothalamic somatocrinin: Growth hormone-releasing factor
    • Ling N, Esch F, Bohlen P, Brazeau P, Wehrenberg WB, and Guillemin R (1984b) Isolation, primary structure and synthesis of human hypothalamic somatocrinin: growth hormone-releasing factor. Proc Natl Acad Sci USA 81:4302-4306.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 4302-4306
    • Ling, N.1    Esch, F.2    Bohlen, P.3    Brazeau, P.4    Wehrenberg, W.B.5    Guillemin, R.6
  • 223
  • 224
    • 0035877847 scopus 로고    scopus 로고
    • Glucagon-like peptide-2 action in the murine central nervous system is enhanced by elimination of GLP-1 receptor signaling
    • Lovshin J, Estall J, Yusta B, Brown TJ, and Drucker DJ (2001) Glucagon-like peptide-2 action in the murine central nervous system is enhanced by elimination of GLP-1 receptor signaling. J Biol Chem 276:21489-21499.
    • (2001) J Biol Chem , vol.276 , pp. 21489-21499
    • Lovshin, J.1    Estall, J.2    Yusta, B.3    Brown, T.J.4    Drucker, D.J.5
  • 226
    • 0027393644 scopus 로고
    • The role of the free cytoplasmic calcium level in β-cell signal transduction by gastric inhibitory polypeptide and glucagon-like peptide I(7-37)
    • Lu M, Wheeler MB, Leng X-H, and Boyd AEI (1993) The role of the free cytoplasmic calcium level in β-cell signal transduction by gastric inhibitory polypeptide and glucagon-like peptide I(7-37). Endocrinology 132:94-100.
    • (1993) Endocrinology , vol.132 , pp. 94-100
    • Lu, M.1    Wheeler, M.B.2    Leng, X.-H.3    Boyd, A.E.I.4
  • 227
    • 0020026919 scopus 로고
    • Pancreatic preproglucagon cDNA contains two glucagon-related coding sequences arranged in tandem
    • Lund PK, Goodman RH, Dee PC, and Habener JF (1982) Pancreatic preproglucagon cDNA contains two glucagon-related coding sequences arranged in tandem. Proc Natl Acad Sci USA 79:345-349.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 345-349
    • Lund, P.K.1    Goodman, R.H.2    Dee, P.C.3    Habener, J.F.4
  • 228
    • 0025924622 scopus 로고
    • Free intracellular Ca2+ concentration ([Ca2+]i) and growth hormone release from purified rat somatotrophs. I. GH-releasing factor-induced Ca2+ influx raises [Ca2+]i
    • Lussier BT, French MB, Moore BC, and Kraicer J (1991) Free intracellular Ca2+ concentration ([Ca2+]i) and growth hormone release from purified rat somatotrophs. I. GH-releasing factor-induced Ca2+ influx raises [Ca2+]i. Endocrinology 128:570-582.
    • (1991) Endocrinology , vol.128 , pp. 570-582
    • Lussier, B.T.1    French, M.B.2    Moore, B.C.3    Kraicer, J.4
  • 229
    • 0027196424 scopus 로고
    • Control of cholecystokinin receptor dephosphorylation in pancreatic acinar cells
    • Lutz MP, Pinon DI, Gates LK, Shenolikar S, and Miller LJ (1993) Control of cholecystokinin receptor dephosphorylation in pancreatic acinar cells. J Biol Chem 268:12136-12142.
    • (1993) J Biol Chem , vol.268 , pp. 12136-12142
    • Lutz, M.P.1    Pinon, D.I.2    Gates, L.K.3    Shenolikar, S.4    Miller, L.J.5
  • 230
    • 0035041250 scopus 로고    scopus 로고
    • Defective glucose-dependent insulinotropic polypeptide receptor expression in diabetic fatty Zucker rats
    • Lynn FC, Pamir N, Ng EH, McIntosh CH, Kieffer TJ, and Pederson RA (2001) Defective glucose-dependent insulinotropic polypeptide receptor expression in diabetic fatty Zucker rats. Diabetes 50:1004-1011.
    • (2001) Diabetes , vol.50 , pp. 1004-1011
    • Lynn, F.C.1    Pamir, N.2    Ng, E.H.3    McIntosh, C.H.4    Kieffer, T.J.5    Pederson, R.A.6
  • 233
    • 0032542247 scopus 로고    scopus 로고
    • Discovery and structureactivity relationship of the first non-peptide competitive human glucagon receptor antagonists
    • Madsen P, Knudsen LB, Wiberg FC, and Carr RD (1998) Discovery and structureactivity relationship of the first non-peptide competitive human glucagon receptor antagonists. J Med Chem 41:5150-5157.
    • (1998) J Med Chem , vol.41 , pp. 5150-5157
    • Madsen, P.1    Knudsen, L.B.2    Wiberg, F.C.3    Carr, R.D.4
  • 234
    • 0023128223 scopus 로고
    • A glucagon fragment is responsible for the inhibition of the liver Ca pump by glucagon
    • Mallat A, Pavoine C, Dufour M, Lotersztajn S, Bataille D, and Pecker F (1987) A glucagon fragment is responsible for the inhibition of the liver Ca pump by glucagon. Nature (Lond) 325:620-622.
    • (1987) Nature (Lond) , vol.325 , pp. 620-622
    • Mallat, A.1    Pavoine, C.2    Dufour, M.3    Lotersztajn, S.4    Bataille, D.5    Pecker, F.6
  • 235
    • 0025020981 scopus 로고
    • Expression and localization of growth hormone-releasing hormone messenger ribonucleic acid in rat placenta: In vitro secretion and regulation of its peptide product
    • Margioris AN, Brockmann G, Bohler HC Jr, Grino M, Vamvakopoulos N, and Chrousos GP (1990) Expression and localization of growth hormone-releasing hormone messenger ribonucleic acid in rat placenta: in vitro secretion and regulation of its peptide product. Endocrinology 126:151-158.
    • (1990) Endocrinology , vol.126 , pp. 151-158
    • Margioris, A.N.1    Brockmann, G.2    Bohler H.C., Jr.3    Grino, M.4    Vamvakopoulos, N.5    Chrousos, G.P.6
  • 236
    • 0028803893 scopus 로고
    • Localization of the gene encoding the secretin receptor, SCTR, on human chromosome 2q14.1 by fluorescence in situ hybridization and chromosome morphometry
    • Mark HF and Chow BK (1995) Localization of the gene encoding the secretin receptor, SCTR, on human chromosome 2q14.1 by fluorescence in situ hybridization and chromosome morphometry. Genomics 29:817-818.
    • (1995) Genomics , vol.29 , pp. 817-818
    • Mark, H.F.1    Chow, B.K.2
  • 237
    • 0029121045 scopus 로고
    • Differential gene expression of growth hormone (GH)-releasing hormone (GRH) and GRH receptor in various rat tissues
    • Matsubara S, Sato M, Mizobuchi M, Niimi M, and Takahara J (1995) Differential gene expression of growth hormone (GH)-releasing hormone (GRH) and GRH receptor in various rat tissues. Endocrinology 136:4147-4150.
    • (1995) Endocrinology , vol.136 , pp. 4147-4150
    • Matsubara, S.1    Sato, M.2    Mizobuchi, M.3    Niimi, M.4    Takahara, J.5
  • 238
    • 0026803163 scopus 로고
    • Molecular cloning and expression of a pituitary-specific receptor for growth hormone-releasing hormone
    • Mayo KE (1992) Molecular cloning and expression of a pituitary-specific receptor for growth hormone-releasing hormone. Mol Endocrinol 6:1734-1744.
    • (1992) Mol Endocrinol , vol.6 , pp. 1734-1744
    • Mayo, K.E.1
  • 239
    • 0021981803 scopus 로고
    • Characterization of cDNA and genomic clones encoding the precursor to rat hypothalamic growth hormone-releasing factor
    • Mayo KE, Cerelli GM, Rosenfeld MG, and Evans RM (1985) Characterization of cDNA and genomic clones encoding the precursor to rat hypothalamic growth hormone-releasing factor. Nature (Lond) 314:464-467.
    • (1985) Nature (Lond) , vol.314 , pp. 464-467
    • Mayo, K.E.1    Cerelli, G.M.2    Rosenfeld, M.G.3    Evans, R.M.4
  • 241
    • 0023710510 scopus 로고
    • Dramatic pituitary hyperplasia in transgenic mice expressing a human growth hormone-releasing factor gene
    • Mayo KE, Hammer RE, Swanson LW, Brinster RL, Rosenfeld MG, and Evans RM (1988) Dramatic pituitary hyperplasia in transgenic mice expressing a human growth hormone-releasing factor gene. Mol Endocrinol 2:606-612.
    • (1988) Mol Endocrinol , vol.2 , pp. 606-612
    • Mayo, K.E.1    Hammer, R.E.2    Swanson, L.W.3    Brinster, R.L.4    Rosenfeld, M.G.5    Evans, R.M.6
  • 242
    • 0034505956 scopus 로고    scopus 로고
    • Regulation of the pituitary somatotroph cell by GHRH and its receptor
    • discussion 55:266-267
    • Mayo KE, Miller T, DeAlmeida V, Godfrey P, Zheng J, and Cunha SR (2000) Regulation of the pituitary somatotroph cell by GHRH and its receptor. Recent Prog Horm Res 55:237-266; discussion 55:266-267.
    • (2000) Recent Prog Horm Res , vol.55 , pp. 237-266
    • Mayo, K.E.1    Miller, T.2    DeAlmeida, V.3    Godfrey, P.4    Zheng, J.5    Cunha, S.R.6
  • 243
    • 0030464704 scopus 로고    scopus 로고
    • The growth-hormone-releasing hormone receptor: Signal transduction, gene expression and physiological function in growth regulation
    • Mayo KE, Miller TL, DeAlmeida V, Zheng J, and Godfrey PA (1996) The growth-hormone-releasing hormone receptor: signal transduction, gene expression and physiological function in growth regulation. Ann NY Acad Sci 805:184-203.
    • (1996) Ann NY Acad Sci , vol.805 , pp. 184-203
    • Mayo, K.E.1    Miller, T.L.2    DeAlmeida, V.3    Zheng, J.4    Godfrey, P.A.5
  • 244
    • 0020545404 scopus 로고
    • Expression-cloning and sequence of a cDNA encoding human growth hormone-releasing factor
    • Mayo KE, Vale W, Rivier J, Rosenfeld MG, and Evans RM (1983) Expression-cloning and sequence of a cDNA encoding human growth hormone-releasing factor. Nature (Lond) 306:86-88.
    • (1983) Nature (Lond) , vol.306 , pp. 86-88
    • Mayo, K.E.1    Vale, W.2    Rivier, J.3    Rosenfeld, M.G.4    Evans, R.M.5
  • 245
    • 0032870219 scopus 로고    scopus 로고
    • Gastric inhibitory polypeptide stimulates glucocorticoid secretion in rats, acting through specific receptors coupled with the adenylate cyclase-dependent signaling pathway
    • Mazzocchi G, Rebuffat P, Meneghelli V, Malendowicz LK, Tortorella C, Gottardo G and Nussdorfer, GG (1999) Gastric inhibitory polypeptide stimulates glucocorticoid secretion in rats, acting through specific receptors coupled with the adenylate cyclase-dependent signaling pathway. Peptides 20:589-594.
    • (1999) Peptides , vol.20 , pp. 589-594
    • Mazzocchi, G.1    Rebuffat, P.2    Meneghelli, V.3    Malendowicz, L.K.4    Tortorella, C.5    Gottardo, G.6    Nussdorfer, G.G.7
  • 247
    • 0035512742 scopus 로고    scopus 로고
    • Reduced insulinotropic effect of gastric inhibitory polypeptide in first-degree relatives of patients with type 2 diabetes
    • Meier JJ, Hucking K, Holst JJ, Deacon CF, Schmiegel WH, and Nauck MA (2001) Reduced insulinotropic effect of gastric inhibitory polypeptide in first-degree relatives of patients with type 2 diabetes. Diabetes 50:2497-2504.
    • (2001) Diabetes , vol.50 , pp. 2497-2504
    • Meier, J.J.1    Hucking, K.2    Holst, J.J.3    Deacon, C.F.4    Schmiegel, W.H.5    Nauck, M.A.6
  • 248
    • 0027215348 scopus 로고
    • Dipeptidyl-peptidase IV hydrolyses gastric inhibitory polypeptide, glucagon-like peptide-1(7-36)amide, peptide histidine methionine and is responsible for their degradation in human serum
    • Mentlein R, Gallwitz B, and Schmidt WE (1993) Dipeptidyl-peptidase IV hydrolyses gastric inhibitory polypeptide, glucagon-like peptide-1(7-36)amide, peptide histidine methionine and is responsible for their degradation in human serum. Eur J Biochem 214:829-835.
    • (1993) Eur J Biochem , vol.214 , pp. 829-835
    • Mentlein, R.1    Gallwitz, B.2    Schmidt, W.E.3
  • 250
    • 0033545166 scopus 로고    scopus 로고
    • Distribution of pre-pro-glucagon and glucagon-like peptide-1 receptor messenger RNAs in the rat central nervous system
    • Merchenthaler I, Lane M, and Shughrue P (1999) Distribution of pre-pro-glucagon and glucagon-like peptide-1 receptor messenger RNAs in the rat central nervous system. J Comp Neurol 403:261-280.
    • (1999) J Comp Neurol , vol.403 , pp. 261-280
    • Merchenthaler, I.1    Lane, M.2    Shughrue, P.3
  • 251
    • 0021269669 scopus 로고
    • Immunocytochemical localization of growth hormone-releasing factor in the rat hypothalamus
    • Merchenthaler I, Vigh S, Schally AV, and Petrusz P (1984) Immunocytochemical localization of growth hormone-releasing factor in the rat hypothalamus. Endocrinology 114:1082-1085.
    • (1984) Endocrinology , vol.114 , pp. 1082-1085
    • Merchenthaler, I.1    Vigh, S.2    Schally, A.V.3    Petrusz, P.4
  • 252
    • 0013355914 scopus 로고
    • Glucagon and growth hormone
    • Lefebvre PJ ed, Springer-Verlag, Berlin
    • Merimee TJ (1983) Glucagon and growth hormone, in Glucagon II (Lefebvre PJ ed) pp 545-551, Springer-Verlag, Berlin.
    • (1983) Glucagon II , pp. 545-551
    • Merimee, T.J.1
  • 255
    • 0033304980 scopus 로고    scopus 로고
    • The rat growth hormone-releasing hormone receptor gene: Structure, regulation and generation of receptor isoforms with different signaling properties
    • Miller TL, Godfrey PA, Dealmeida VI, and Mayo KE (1999) The rat growth hormone-releasing hormone receptor gene: structure, regulation and generation of receptor isoforms with different signaling properties. Endocrinology 140:4152-4165.
    • (1999) Endocrinology , vol.140 , pp. 4152-4165
    • Miller, T.L.1    Godfrey, P.A.2    Dealmeida, V.I.3    Mayo, K.E.4
  • 256
    • 0030919843 scopus 로고    scopus 로고
    • Glucocorticoids regulate pituitary growth hormone-releasing hormone receptor messenger ribonucleic acid expression
    • Miller TL and Mayo KE (1997) Glucocorticoids regulate pituitary growth hormone-releasing hormone receptor messenger ribonucleic acid expression. Endocrinology 138:2458-2465.
    • (1997) Endocrinology , vol.138 , pp. 2458-2465
    • Miller, T.L.1    Mayo, K.E.2
  • 259
    • 0036313576 scopus 로고    scopus 로고
    • Assessment of the role of interstitial glucagon in the acute glucose secretory responsiveness of in situ pancreatic beta-cells
    • Moens K, Berger V, Ahn JM, Van Schravendijk C, Hruby VJ, Pipeleers D, and Schuit F (2002) Assessment of the role of interstitial glucagon in the acute glucose secretory responsiveness of in situ pancreatic beta-cells. Diabetes 51:669-675.
    • (2002) Diabetes , vol.51 , pp. 669-675
    • Moens, K.1    Berger, V.2    Ahn, J.M.3    Van Schravendijk, C.4    Hruby, V.J.5    Pipeleers, D.6    Schuit, F.7
  • 260
    • 0031965605 scopus 로고    scopus 로고
    • Dual glucagon recognition by pancreatic beta-cells via glucagon and glucagon-like peptide 1 receptors
    • Moens K, Flamez D, Van Schravendijk C, Ling Z, Pipeleers D, and Schuit F (1998) Dual glucagon recognition by pancreatic beta-cells via glucagon and glucagon-like peptide 1 receptors. Diabetes 47:66-72.
    • (1998) Diabetes , vol.47 , pp. 66-72
    • Moens, K.1    Flamez, D.2    Van Schravendijk, C.3    Ling, Z.4    Pipeleers, D.5    Schuit, F.6
  • 261
    • 13344293675 scopus 로고    scopus 로고
    • Expression and functional activity of glucagon, glucagon-like peptide 1 and glucose-dependent insulinotropic peptide receptors in rat pancreatic islet cells
    • Moens K, Heimberg H, Flamez D, Huypens P, Quartier E, Ling Z, Pipeleers D, Gremlich S, Thorens B and Schuit, F (1996) Expression and functional activity of glucagon, glucagon-like peptide 1 and glucose-dependent insulinotropic peptide receptors in rat pancreatic islet cells. Diabetes 45:257-261.
    • (1996) Diabetes , vol.45 , pp. 257-261
    • Moens, K.1    Heimberg, H.2    Flamez, D.3    Huypens, P.4    Quartier, E.5    Ling, Z.6    Pipeleers, D.7    Gremlich, S.8    Thorens, B.9    Schuit, F.10
  • 262
    • 0023008693 scopus 로고
    • Preproglucagon gene expression in pancreas and intestine diversifies at the level of post-translational processing
    • Mojsov S, Heinrich G, Wilson IB, Ravazzola M, Orci L, and Habener JF (1986) Preproglucagon gene expression in pancreas and intestine diversifies at the level of post-translational processing. J Biol Chem 261:11880-11889.
    • (1986) J Biol Chem , vol.261 , pp. 11880-11889
    • Mojsov, S.1    Heinrich, G.2    Wilson, I.B.3    Ravazzola, M.4    Orci, L.5    Habener, J.F.6
  • 263
    • 0033775408 scopus 로고    scopus 로고
    • Molecular evolution of the growth hormone-releasing hormone/pituitary adenylate cyclase-activating polypeptide gene family. Functional implication in the regulation of growth hormone secretion
    • Montero M, Yon L, Kikuyama S, Dufour S, and Vaudry H (2000) Molecular evolution of the growth hormone-releasing hormone/pituitary adenylate cyclase-activating polypeptide gene family. Functional implication in the regulation of growth hormone secretion. J Mol Endocrinol 25:157-168.
    • (2000) J Mol Endocrinol , vol.25 , pp. 157-168
    • Montero, M.1    Yon, L.2    Kikuyama, S.3    Dufour, S.4    Vaudry, H.5
  • 264
    • 0030884317 scopus 로고    scopus 로고
    • Novel signal transduction and peptide specificity of glucagon-like peptide receptor in 3T3-L1 adipocytes
    • Montrose-Rafizadeh C, Yang H, Wang Y, Roth J, Montrose MH, and Adams LG (1997) Novel signal transduction and peptide specificity of glucagon-like peptide receptor in 3T3-L1 adipocytes. J Cell Physiol 172:275-283.
    • (1997) J Cell Physiol , vol.172 , pp. 275-283
    • Montrose-Rafizadeh, C.1    Yang, H.2    Wang, Y.3    Roth, J.4    Montrose, M.H.5    Adams, L.G.6
  • 265
    • 0032861148 scopus 로고    scopus 로고
    • Restricted presence of the growth hormone-releasing hormone receptor to somatotropes in rat and human pituitaries
    • Morel G, Gallego R, Boulanger L, Pintos E, Garcia-Caballero T, and Gaudreau P (1999) Restricted presence of the growth hormone-releasing hormone receptor to somatotropes in rat and human pituitaries. Neuroendocrinology 70:128-136.
    • (1999) Neuroendocrinology , vol.70 , pp. 128-136
    • Morel, G.1    Gallego, R.2    Boulanger, L.3    Pintos, E.4    Garcia-Caballero, T.5    Gaudreau, P.6
  • 266
    • 0030479371 scopus 로고    scopus 로고
    • Hypothesis: Glucagon receptor glycine to serine missense mutation contributes to one in 20 cases of essential hypertension
    • Morris BJ and Chambers SM (1996) Hypothesis: glucagon receptor glycine to serine missense mutation contributes to one in 20 cases of essential hypertension. Clin Exp Pharmacol Physiol 23:1035-1037.
    • (1996) Clin Exp Pharmacol Physiol , vol.23 , pp. 1035-1037
    • Morris, B.J.1    Chambers, S.M.2
  • 267
    • 0031810145 scopus 로고    scopus 로고
    • Inhibition of signal transduction by a splice variant of the growth hormone-releasing hormone receptor expressed in human pituitary adenomas
    • Motomura T, Hashimoto K, Koga M, Arita N, Hayakawa T, Kishimoto T, and Kasayama S (1998) Inhibition of signal transduction by a splice variant of the growth hormone-releasing hormone receptor expressed in human pituitary adenomas. Metab Clin Exp 47:804-808.
    • (1998) Metab Clin Exp , vol.47 , pp. 804-808
    • Motomura, T.1    Hashimoto, K.2    Koga, M.3    Arita, N.4    Hayakawa, T.5    Kishimoto, T.6    Kasayama, S.7
  • 270
    • 0003111499 scopus 로고
    • Secretin: Isolation, structure and functions
    • Glass GBJ ed, Raven Press, New York
    • Mutt V (1980) Secretin: isolation, structure and functions, in Gastrointestinal Hormones (Glass GBJ ed) pp 85-126, Raven Press, New York.
    • (1980) Gastrointestinal Hormones , pp. 85-126
    • Mutt, V.1
  • 272
    • 0027391607 scopus 로고
    • Preserved incretin activity of glucagon-like peptide 1 [7-36 amide] but not of synthetic human gastric inhibitory polypeptide in patients with type-2 diabetes mellitus
    • Nauck MA, Heimesaat MM, Orskov C, Holst JJ, Ebert R, and Creutzfeldt W (1993) Preserved incretin activity of glucagon-like peptide 1 [7-36 amide] but not of synthetic human gastric inhibitory polypeptide in patients with type-2 diabetes mellitus. J Clin Investig 91:301-307.
    • (1993) J Clin Investig , vol.91 , pp. 301-307
    • Nauck, M.A.1    Heimesaat, M.M.2    Orskov, C.3    Holst, J.J.4    Ebert, R.5    Creutzfeldt, W.6
  • 273
    • 0031732852 scopus 로고    scopus 로고
    • Extensive phenotypic analysis of a family with growth hormone (GH) deficiency caused by a mutation in the GH-releasing hormone receptor gene
    • Netchine I, Talon P, Dastot F, Vitaux F, Goossens M, and Amselem S (1998) Extensive phenotypic analysis of a family with growth hormone (GH) deficiency caused by a mutation in the GH-releasing hormone receptor gene. J Clin Endocrinol Metab 83:432-436.
    • (1998) J Clin Endocrinol Metab , vol.83 , pp. 432-436
    • Netchine, I.1    Talon, P.2    Dastot, F.3    Vitaux, F.4    Goossens, M.5    Amselem, S.6
  • 274
    • 0032867337 scopus 로고    scopus 로고
    • Functional studies of a glucagon receptor isolated from frog Rana tigrina rugulosa: Implications on the molecular evolution of glucagon receptors in vertebrates
    • Ngan ES, Chow LS, Tse DL, Du X, Wei Y, Mojsov S, and Chow BK (1999) Functional studies of a glucagon receptor isolated from frog Rana tigrina rugulosa: implications on the molecular evolution of glucagon receptors in vertebrates. FEBS Lett 457:499-504.
    • (1999) FEBS Lett , vol.457 , pp. 499-504
    • Ngan, E.S.1    Chow, L.S.2    Tse, D.L.3    Du, X.4    Wei, Y.5    Mojsov, S.6    Chow, B.K.7
  • 275
    • 0033305490 scopus 로고    scopus 로고
    • Posttranslational processing of progrowth hormone-releasing hormone
    • Nillni EA, Steinmetz R, and Pescovitz OH (1999) Posttranslational processing of progrowth hormone-releasing hormone. Endocrinology 140:5817-5827.
    • (1999) Endocrinology , vol.140 , pp. 5817-5827
    • Nillni, E.A.1    Steinmetz, R.2    Pescovitz, O.H.3
  • 277
    • 0032587206 scopus 로고    scopus 로고
    • NH2-terminally modified gastric inhibitory polypeptide exhibits amino-peptidase resistance and enhanced antihyperglycemic activity
    • O'Harte FP, Mooney MH, and Flatt PR (1999) NH2-terminally modified gastric inhibitory polypeptide exhibits amino-peptidase resistance and enhanced antihyperglycemic activity. Diabetes 48:758-765.
    • (1999) Diabetes , vol.48 , pp. 758-765
    • O'Harte, F.P.1    Mooney, M.H.2    Flatt, P.R.3
  • 278
    • 0034131227 scopus 로고    scopus 로고
    • Improved glycaemic control in obese diabetic ob/ob mice using N-terminally modified gastric inhibitory polypeptide
    • O'Harte FP, Mooney MH, Kelly CM, and Flatt PR (2000) Improved glycaemic control in obese diabetic ob/ob mice using N-terminally modified gastric inhibitory polypeptide. J Endocrinol 165:639-648.
    • (2000) J Endocrinol , vol.165 , pp. 639-648
    • O'Harte, F.P.1    Mooney, M.H.2    Kelly, C.M.3    Flatt, P.R.4
  • 279
    • 0025056609 scopus 로고
    • The correlation between calcium outflow and growth hormone release in perifused rat somatotrophs
    • Ohlsson L and Lindstrom P (1990) The correlation between calcium outflow and growth hormone release in perifused rat somatotrophs. Endocrinology 126:488-497.
    • (1990) Endocrinology , vol.126 , pp. 488-497
    • Ohlsson, L.1    Lindstrom, P.2
  • 281
    • 0022971804 scopus 로고
    • Glucagon-like peptides GLP-1 and GLP-2, predicted products of the glucagon gene, are secreted separately from pig small intestine but not pancreas
    • Orskov C, Holst JJ, Knuhtsen S, Baldissera FGA, Poulsen SS, and Nielsen OV (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.
    • (1986) Endocrinology , vol.119 , pp. 1467-1475
    • Orskov, C.1    Holst, J.J.2    Knuhtsen, S.3    Baldissera, F.G.A.4    Poulsen, S.S.5    Nielsen, O.V.6
  • 282
    • 0027157849 scopus 로고
    • Biological effects and metabolic rates of glucagonlike peptide-1 7-36 amide and glucagonlike peptide-1 7-37 in healthy subjects are indistinguishable
    • Orskov C, Wettergren A, and Holst JJ (1993) Biological effects and metabolic rates of glucagonlike peptide-1 7-36 amide and glucagonlike peptide-1 7-37 in healthy subjects are indistinguishable. Diabetes 42:658-661.
    • (1993) Diabetes , vol.42 , pp. 658-661
    • Orskov, C.1    Wettergren, A.2    Holst, J.J.3
  • 284
    • 0028828037 scopus 로고
    • Agonist-stimulated phosphorylation of the carboxyl-terminal tail of the secretin receptor
    • Ozcelebi F, Holtmann MH, Rentsch RU, Rao R, and Miller LJ (1995) Agonist-stimulated phosphorylation of the carboxyl-terminal tail of the secretin receptor. Mol Pharmacol 48:818-824.
    • (1995) Mol Pharmacol , vol.48 , pp. 818-824
    • Ozcelebi, F.1    Holtmann, M.H.2    Rentsch, R.U.3    Rao, R.4    Miller, L.J.5
  • 285
    • 0033780267 scopus 로고    scopus 로고
    • Cross-chimeric analysis of selectivity of secretin and VPAC(1) receptor activation
    • Park CG, Ganguli SC, Pinon DI, Hadac EM, and Miller LJ (2000) Cross-chimeric analysis of selectivity of secretin and VPAC(1) receptor activation. J Pharmacol Exp Ther 295:682-688.
    • (2000) J Pharmacol Exp Ther , vol.295 , pp. 682-688
    • Park, C.G.1    Ganguli, S.C.2    Pinon, D.I.3    Hadac, E.M.4    Miller, L.J.5
  • 288
    • 0029830703 scopus 로고    scopus 로고
    • Investigation of glucose-dependent insulinotropic polypeptide-(1-42) and glucagon-like peptide-1-(7-36) degradation in vitro by dipeptidyl peptidase IV using matrix-assisted laser desorption/ionization-time of flight mass spectrometry. A novel kinetic approach
    • Pauly RP, Rosche F, Wermann M, McIntosh CH, Pederson RA, and Demuth HU (1996) Investigation of glucose-dependent insulinotropic polypeptide-(1-42) and glucagon-like peptide-1-(7-36) degradation in vitro by dipeptidyl peptidase IV using matrix-assisted laser desorption/ionization-time of flight mass spectrometry. A novel kinetic approach. J Biol Chem 271:23222-23229.
    • (1996) J Biol Chem , vol.271 , pp. 23222-23229
    • Pauly, R.P.1    Rosche, F.2    Wermann, M.3    McIntosh, C.H.4    Pederson, R.A.5    Demuth, H.U.6
  • 289
    • 0035090038 scopus 로고    scopus 로고
    • The growth hormone (GH)-axis of GH receptor/binding protein gene-disrupted and metallothionein-human GH-releasing hormone transgenic mice: Hypothalamic neuropeptide and pituitary receptor expression in the absence and presence of GH feedback
    • Peng XD, Park S, Gadelha MR, Coschigano KT, Kopchick JJ, Frohman LA and Kineman, RD (2001) The growth hormone (GH)-axis of GH receptor/binding protein gene-disrupted and metallothionein-human GH-releasing hormone transgenic mice: hypothalamic neuropeptide and pituitary receptor expression in the absence and presence of GH feedback. Endocrinology 142:1117-1123.
    • (2001) Endocrinology , vol.142 , pp. 1117-1123
    • Peng, X.D.1    Park, S.2    Gadelha, M.R.3    Coschigano, K.T.4    Kopchick, J.J.5    Frohman, L.A.6    Kineman, R.D.7
  • 290
    • 0036721026 scopus 로고    scopus 로고
    • Protection and reversal of excitotoxic neuronal damage by glucagon-like Peptide-1 and exendin-4
    • Perry T, Haughey NJ, Mattson MP, Egan JM, and Greig NH (2002a) Protection and reversal of excitotoxic neuronal damage by glucagon-like Peptide-1 and exendin-4. J Pharmacol Exp Ther 302:881-888.
    • (2002) J Pharmacol Exp Ther , vol.302 , pp. 881-888
    • Perry, T.1    Haughey, N.J.2    Mattson, M.P.3    Egan, J.M.4    Greig, N.H.5
  • 291
    • 0036182251 scopus 로고    scopus 로고
    • A novel neurotrophic property of glucagon-like Peptide 1: A promoter of nerve growth factor-mediated differentiation in PC12 cells
    • Perry T, Lahiri DK, Chen D, Zhou J, Shaw KT, Egan JM, and Greig NH (2002b) A novel neurotrophic property of glucagon-like Peptide 1: a promoter of nerve growth factor-mediated differentiation in PC12 cells. J Pharmacol Exp Ther 300:958-966.
    • (2002) J Pharmacol Exp Ther , vol.300 , pp. 958-966
    • Perry, T.1    Lahiri, D.K.2    Chen, D.3    Zhou, J.4    Shaw, K.T.5    Egan, J.M.6    Greig, N.H.7
  • 292
    • 0035195977 scopus 로고    scopus 로고
    • Effects of a novel glucagon receptor antagonist (Bay 27-9955) on glucagon-stimulated glucose production in humans
    • Petersen KF and Sullivan JT (2001) Effects of a novel glucagon receptor antagonist (Bay 27-9955) on glucagon-stimulated glucose production in humans. Diabetologia 44:2018-2024.
    • (2001) Diabetologia , vol.44 , pp. 2018-2024
    • Petersen, K.F.1    Sullivan, J.T.2
  • 293
    • 0032230229 scopus 로고    scopus 로고
    • Structure and regulation of the human growth hormone-releasing hormone receptor gene
    • Petersenn S, Rasch AC, Heyens M, and Schulte HM (1998) Structure and regulation of the human growth hormone-releasing hormone receptor gene. Mol Endocrinol 12:233-247.
    • (1998) Mol Endocrinol , vol.12 , pp. 233-247
    • Petersenn, S.1    Rasch, A.C.2    Heyens, M.3    Schulte, H.M.4
  • 294
    • 0034457676 scopus 로고    scopus 로고
    • Growth hormone-releasing hormone stimulates mitogen-activated protein kinase
    • Pombo CM, Zalvide J, Gaylinn BD, and Dieguez C (2000) Growth hormone-releasing hormone stimulates mitogen-activated protein kinase. Endocrinology 141:2113-2119.
    • (2000) Endocrinology , vol.141 , pp. 2113-2119
    • Pombo, C.M.1    Zalvide, J.2    Gaylinn, B.D.3    Dieguez, C.4
  • 295
    • 0033583195 scopus 로고    scopus 로고
    • Identification of a glucose response element in the promoter ofthe rat glucagon receptor gene
    • Portois L, Maget B, Tastenoy M, Perret J, and Svoboda M (1999) Identification of a glucose response element in the promoter ofthe rat glucagon receptor gene. J Biol Chem 274:8181-8190.
    • (1999) J Biol Chem , vol.274 , pp. 8181-8190
    • Portois, L.1    Maget, B.2    Tastenoy, M.3    Perret, J.4    Svoboda, M.5
  • 296
    • 0033964619 scopus 로고    scopus 로고
    • Glucagonlike peptide-2 analogue enhances intestinal mucosal mass after ischemia and reperfusion
    • Prasad R, Alavi K, and Schwartz MZ (2000) Glucagonlike peptide-2 analogue enhances intestinal mucosal mass after ischemia and reperfusion. J Pediatr Surg 35:357-359.
    • (2000) J Pediatr Surg , vol.35 , pp. 357-359
    • Prasad, R.1    Alavi, K.2    Schwartz, M.Z.3
  • 297
    • 0034744761 scopus 로고    scopus 로고
    • GLP-2alpha accelerates recovery of mucosal absorptive function after intestinal ischemia/reperfusion
    • Prasad R, Alavi K, and Schwartz MZ (2001) GLP-2alpha accelerates recovery of mucosal absorptive function after intestinal ischemia/reperfusion. J Pediatr Surg 36:570-572.
    • (2001) J Pediatr Surg , vol.36 , pp. 570-572
    • Prasad, R.1    Alavi, K.2    Schwartz, M.Z.3
  • 298
    • 0032982651 scopus 로고    scopus 로고
    • Growth hormone (GH)-releasing factor differentially activates cyclic adenosine 3′, 5′-monophosphate- and inositol phosphate-dependent pathways to stimulate GH release in two porcine somatotrope subpopulations
    • Ramirez JL, Castano JP, Torronteras R, Martinez-Fuentes AJ, Frawley LS, Garcia-Navarro S, and Gracia-Navarro F (1999) Growth hormone (GH)-releasing factor differentially activates cyclic adenosine 3′, 5′-monophosphate- and inositol phosphate-dependent pathways to stimulate GH release in two porcine somatotrope subpopulations. Endocrinology 140:1752-1759.
    • (1999) Endocrinology , vol.140 , pp. 1752-1759
    • Ramirez, J.L.1    Castano, J.P.2    Torronteras, R.3    Martinez-Fuentes, A.J.4    Frawley, L.S.5    Garcia-Navarro, S.6    Gracia-Navarro, F.7
  • 299
    • 0035462466 scopus 로고    scopus 로고
    • Impaired incretin response after a mixed meal is associated with insulin resistance in nondiabetic men
    • Rask E, Olsson T, Soderberg S, Johnson O, Seckl J, Holst JJ, and Ahren B (2001) Impaired incretin response after a mixed meal is associated with insulin resistance in nondiabetic men. Diabetes Care 24:1640-1645.
    • (2001) Diabetes Care , vol.24 , pp. 1640-1645
    • Rask, E.1    Olsson, T.2    Soderberg, S.3    Johnson, O.4    Seckl, J.5    Holst, J.J.6    Ahren, B.7
  • 300
    • 0034641750 scopus 로고    scopus 로고
    • Isolation and sequencing of cDNAs for splice variants of growth hormone-releasing hormone receptors from human cancers
    • Rekasi Z, Czompoly T, Schally AV, and Halmos G (2000) Isolation and sequencing of cDNAs for splice variants of growth hormone-releasing hormone receptors from human cancers. Proc Natl Acad Sci USA 97:10561-10566.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 10561-10566
    • Rekasi, Z.1    Czompoly, T.2    Schally, A.V.3    Halmos, G.4
  • 302
    • 0025359627 scopus 로고
    • Characterization of receptors for glucagon-like peptide-1(7-36)amide on rat lung membranes
    • Richter G, Goke R, Goke B, and Arnold R (1990) Characterization of receptors for glucagon-like peptide-1(7-36)amide on rat lung membranes. FEBS Lett 267:78-80.
    • (1990) FEBS Lett , vol.267 , pp. 78-80
    • Richter, G.1    Goke, R.2    Goke, B.3    Arnold, R.4
  • 303
    • 0026024546 scopus 로고
    • Characterization of glucagon-like peptide-I(7-36)amide receptors of rat lung membranes by covalent cross-linking
    • Richter G, Goke R, Goke B, Schmidt H, and Arnold R (1991) Characterization of glucagon-like peptide-I(7-36)amide receptors of rat lung membranes by covalent cross-linking. FEBS Lett 280:247-250.
    • (1991) FEBS Lett , vol.280 , pp. 247-250
    • Richter, G.1    Goke, R.2    Goke, B.3    Schmidt, H.4    Arnold, R.5
  • 305
    • 0020428780 scopus 로고
    • Characterization of a growth hormone-releasing factor from a human pancreatic islet tumour
    • Rivier J, Spiess J, Thorner M, and Vale W (1982) Characterization of a growth hormone-releasing factor from a human pancreatic islet tumour. Nature (Lond) 300:276-278.
    • (1982) Nature (Lond) , vol.300 , pp. 276-278
    • Rivier, J.1    Spiess, J.2    Thorner, M.3    Vale, W.4
  • 306
    • 0022404614 scopus 로고
    • Structural requirements for the activation of rat anterior pituitary adenylate cyclase by growth hormone-releasing factor (GRF): Discovery of (N-Ac-Tyr1, D-Arg2)-GRF(1-29)-NH2 as a GRF antagonist on membranes
    • Robberecht P, Coy DH, Waelbroeck M, Heiman ML, de Neef P, Camus JC, and Christophe J (1985) Structural requirements for the activation of rat anterior pituitary adenylate cyclase by growth hormone-releasing factor (GRF): discovery of (N-Ac-Tyr1, D-Arg2)-GRF(1-29)-NH2 as a GRF antagonist on membranes. Endocrinology 117:1759-1764.
    • (1985) Endocrinology , vol.117 , pp. 1759-1764
    • Robberecht, P.1    Coy, D.H.2    Waelbroeck, M.3    Heiman, M.L.4    De Neef, P.5    Camus, J.C.6    Christophe, J.7
  • 307
    • 0015239313 scopus 로고
    • The glucagon-sensitive adenyl cyclase system in plasma membranes of rat liver. V. An obligatory role of guanylnucleotides in glucagon action
    • Rodbell M, Birnbaumer L, Pohl SL, and Krans HM (1971a) The glucagon-sensitive adenyl cyclase system in plasma membranes of rat liver. V. An obligatory role of guanylnucleotides in glucagon action. J Biol Chem 246:1877-1882.
    • (1971) J Biol Chem , vol.246 , pp. 1877-1882
    • Rodbell, M.1    Birnbaumer, L.2    Pohl, S.L.3    Krans, H.M.4
  • 308
    • 0015239327 scopus 로고
    • The glucagon-sensitive adenyl cyclase system in plasma membranes of rat liver. 3. Binding of glucagon: Method of assay and specificity
    • Rodbell M, Krans HM, Pohl SL, and Birnbaumer L (1971b) The glucagon-sensitive adenyl cyclase system in plasma membranes of rat liver. 3. Binding of glucagon: method of assay and specificity. J Biol Chem 246:1861-1871.
    • (1971) J Biol Chem , vol.246 , pp. 1861-1871
    • Rodbell, M.1    Krans, H.M.2    Pohl, S.L.3    Birnbaumer, L.4
  • 310
    • 0036188123 scopus 로고    scopus 로고
    • Decreased expression of the GHRH receptor gene due to a mutation in a Pit-1 binding site
    • Salvatori R, Fan X, Mullis PE, Haile A, and Levine MA (2002) Decreased expression of the GHRH receptor gene due to a mutation in a Pit-1 binding site. Mol Endocrinol 16:450-458.
    • (2002) Mol Endocrinol , vol.16 , pp. 450-458
    • Salvatori, R.1    Fan, X.2    Mullis, P.E.3    Haile, A.4    Levine, M.A.5
  • 314
    • 0013977135 scopus 로고
    • Interrelationship of glucagon, insulin and glucose: The insulinogenic effect of glucagon
    • Samols E, Marri G, and Marks V (1966) Interrelationship of glucagon, insulin and glucose: the insulinogenic effect of glucagon. Diabetes 15:855-865.
    • (1966) Diabetes , vol.15 , pp. 855-865
    • Samols, E.1    Marri, G.2    Marks, V.3
  • 316
    • 0031427659 scopus 로고    scopus 로고
    • Gene regulation of growth hormone-releasing hormone and its receptor
    • Sato M and Takahara J (1997) Gene regulation of growth hormone-releasing hormone and its receptor. Endocr J 44:765-774.
    • (1997) Endocr J , vol.44 , pp. 765-774
    • Sato, M.1    Takahara, J.2
  • 317
    • 0021802620 scopus 로고
    • The distribution of growth-hormone-releasing factor (GRF) immunoreactivity in the central nervous system of the rat: An immunohistochemical study using antisera directed against rat hypothalamic GRF
    • Sawchenko PE, Swanson LW, Rivier J, and Vale WW (1985) The distribution of growth-hormone-releasing factor (GRF) immunoreactivity in the central nervous system of the rat: an immunohistochemical study using antisera directed against rat hypothalamic GRF. J Comp Neurol 237:100-115.
    • (1985) J Comp Neurol , vol.237 , pp. 100-115
    • Sawchenko, P.E.1    Swanson, L.W.2    Rivier, J.3    Vale, W.W.4
  • 318
    • 0033485288 scopus 로고    scopus 로고
    • Antagonistic analogs of growth hormone-releasing hormone:New potential antitumor agents
    • Schally AV and Varga JL (1999) Antagonistic analogs of growth hormone-releasing hormone:new potential antitumor agents. Trends Endocrinol Metab 10:383-391.
    • (1999) Trends Endocrinol Metab , vol.10 , pp. 383-391
    • Schally, A.V.1    Varga, J.L.2
  • 319
    • 0030966001 scopus 로고    scopus 로고
    • Differential effects of subcutaneous GLP-1 on gastric emptying, antroduodenal motility and pancreatic function in men
    • Schirra J, Kuwert P, Wank U, Leicht P, Arnold R, Goke B, and Katschinski M (1997) Differential effects of subcutaneous GLP-1 on gastric emptying, antroduodenal motility and pancreatic function in men. Proc Assoc Am Physicians 109:84-97.
    • (1997) Proc Assoc Am Physicians , vol.109 , pp. 84-97
    • Schirra, J.1    Kuwert, P.2    Wank, U.3    Leicht, P.4    Arnold, R.5    Goke, B.6    Katschinski, M.7
  • 320
    • 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 Investig 101:1421-1430.
    • (1998) J Clin Investig , vol.101 , pp. 1421-1430
    • Schirra, J.1    Sturm, K.2    Leicht, P.3    Arnold, R.4    Goke, B.5    Katschinski, M.6
  • 322
    • 0031735064 scopus 로고    scopus 로고
    • GLP-2 augments the adaptive response to massive intestinal resection in rat
    • Scott RB, Kirk D, MacNaughton WK, and Meddings JB (1998) GLP-2 augments the adaptive response to massive intestinal resection in rat. Am J Physiol 275:G911-G921.
    • (1998) Am J Physiol , vol.275
    • Scott, R.B.1    Kirk, D.2    MacNaughton, W.K.3    Meddings, J.B.4
  • 323
  • 324
    • 0033857422 scopus 로고    scopus 로고
    • Elimination of GLP-1R signaling does not modify weight gain and islet adaptation in mice with combined disruption of leptin and GLP-1 action
    • Scrocchi LA, Hill ME, Saleh J, Perkins B, and Drucker DJ (2000) Elimination of GLP-1R signaling does not modify weight gain and islet adaptation in mice with combined disruption of leptin and GLP-1 action. Diabetes 49:1552-1560.
    • (2000) Diabetes , vol.49 , pp. 1552-1560
    • Scrocchi, L.A.1    Hill, M.E.2    Saleh, J.3    Perkins, B.4    Drucker, D.J.5
  • 325
    • 85047681645 scopus 로고    scopus 로고
    • Targeted gene disruption in endocrine research: The case of GLP-1 and neuroendocrine function
    • Seeley RJ, Woods SC, and D'Alessio D (2000) Targeted gene disruption in endocrine research: The case of GLP-1 and neuroendocrine function. Endocrinology 141:473-475.
    • (2000) Endocrinology , vol.141 , pp. 473-475
    • Seeley, R.J.1    Woods, S.C.2    D'Alessio, D.3
  • 326
    • 0021996309 scopus 로고
    • Binding sites for growth hormone releasing factor on rat anterior pituitary cells
    • Seifert H, Perrin M, Rivier J, and Vale W (1985) Binding sites for growth hormone releasing factor on rat anterior pituitary cells. Nature (Lond) 313:487-489.
    • (1985) Nature (Lond) , vol.313 , pp. 487-489
    • Seifert, H.1    Perrin, M.2    Rivier, J.3    Vale, W.4
  • 327
    • 0032549651 scopus 로고    scopus 로고
    • A role for receptor kinases in the regulation of class II G protein-coupled receptors. Phosphorylation and desensitization of the secretin receptor
    • Shetzline MA, Premont RT, Walker JK, Vigna SR, and Caron MG (1998) A role for receptor kinases in the regulation of class II G protein-coupled receptors. Phosphorylation and desensitization of the secretin receptor. J Biol Chem 273:6756-6762.
    • (1998) J Biol Chem , vol.273 , pp. 6756-6762
    • Shetzline, M.A.1    Premont, R.T.2    Walker, J.K.3    Vigna, S.R.4    Caron, M.G.5
  • 328
    • 0023266561 scopus 로고
    • Identification and localization of glucagon-like peptide-1 and its receptor in rat brain
    • Shimizu I, Hirota M, Ohboshi C, and Shima K (1987) Identification and localization of glucagon-like peptide-1 and its receptor in rat brain. Endocrinology 121:1076-1082.
    • (1987) Endocrinology , vol.121 , pp. 1076-1082
    • Shimizu, I.1    Hirota, M.2    Ohboshi, C.3    Shima, K.4
  • 329
    • 0036242214 scopus 로고    scopus 로고
    • Role of the Gly40Ser mutation in the glucagon receptor gene in Brazilian patients with type 2 diabetes mellitus
    • Shiota D, Kasamatsu T, Dib SA, Chacra AR, and Moises RS (2002) Role of the Gly40Ser mutation in the glucagon receptor gene in Brazilian patients with type 2 diabetes mellitus. Pancreas 24:386-390.
    • (2002) Pancreas , vol.24 , pp. 386-390
    • Shiota, D.1    Kasamatsu, T.2    Dib, S.A.3    Chacra, A.R.4    Moises, R.S.5
  • 330
    • 0029806072 scopus 로고    scopus 로고
    • Glucagon-like peptide-1 receptor (GLP1-R) mRNA in the rat hypothalamus
    • Shughrue PJ, Lane MV, and Merchenthaler I (1996) Glucagon-like peptide-1 receptor (GLP1-R) mRNA in the rat hypothalamus. Endocrinology 137:5159-5162.
    • (1996) Endocrinology , vol.137 , pp. 5159-5162
    • Shughrue, P.J.1    Lane, M.V.2    Merchenthaler, I.3
  • 333
    • 0020503608 scopus 로고
    • Characterization of rat hypothalamic growth hormone-releasing factor
    • Spiess J, Rivier J, and Vale W (1983) Characterization of rat hypothalamic growth hormone-releasing factor. Nature (Lond) 303:532-535.
    • (1983) Nature (Lond) , vol.303 , pp. 532-535
    • Spiess, J.1    Rivier, J.2    Vale, W.3
  • 334
    • 0002693237 scopus 로고
    • Glucagon and liver glycogen metabolism
    • Lefebvre PJ ed, Springer-Verlag, Berlin
    • Stalmans W (1983) Glucagon and liver glycogen metabolism, in Glucagon I (Lefebvre PJ ed) pp 291-314, Springer-Verlag, Berlin.
    • (1983) Glucagon I , pp. 291-314
    • Stalmans, W.1
  • 335
    • 0024464381 scopus 로고
    • Adenohypophysial changes in mice transgenic for human growth hormone-releasing factor: A histological, immunocytochemical and electron microscopic investigation
    • Stefaneanu L, Kovacs K, Horvath E, Asa SL, Losinski NE, Billestrup N, Price J, and Vale W (1989) Adenohypophysial changes in mice transgenic for human growth hormone-releasing factor: a histological, immunocytochemical and electron microscopic investigation. Endocrinology 125:2710-2718.
    • (1989) Endocrinology , vol.125 , pp. 2710-2718
    • Stefaneanu, L.1    Kovacs, K.2    Horvath, E.3    Asa, S.L.4    Losinski, N.E.5    Billestrup, N.6    Price, J.7    Vale, W.8
  • 336
    • 0013359055 scopus 로고
    • Direct effect of glucagon on release of unesterified fatty acids (UFA) from adipose tissue
    • Steinberg DM, Shafrir E, and Vaughan M (1959) Direct effect of glucagon on release of unesterified fatty acids (UFA) from adipose tissue. Clin Res 7:250.
    • (1959) Clin Res , vol.7 , pp. 250
    • Steinberg, D.M.1    Shafrir, E.2    Vaughan, M.3
  • 337
    • 0025881718 scopus 로고
    • Production of a growth hormone-releasing hormone-like peptide and its mRNA by human lymphocytes
    • Stephanou A, Knight RA, and Lightman SL (1991) Production of a growth hormone-releasing hormone-like peptide and its mRNA by human lymphocytes. Neuroendocrinology 53:628-633.
    • (1991) Neuroendocrinology , vol.53 , pp. 628-633
    • Stephanou, A.1    Knight, R.A.2    Lightman, S.L.3
  • 338
    • 0027202020 scopus 로고
    • Human glucagon-like peptide-1 receptor gene: Localization to chromosome band 6p21 by fluorescence in situ hybridization and linkage of a highly polymorphic simple tandem repeat DNA polymorphism to other markers on chromosome 6
    • Stoffel M, Espinosa R III, Le Beau MM, and Bell GI (1993) Human glucagon-like peptide-1 receptor gene: localization to chromosome band 6p21 by fluorescence in situ hybridization and linkage of a highly polymorphic simple tandem repeat DNA polymorphism to other markers on chromosome 6. Diabetes 42:1215-1218.
    • (1993) Diabetes , vol.42 , pp. 1215-1218
    • Stoffel, M.1    Espinosa R. III2    Le Beau, M.M.3    Bell, G.I.4
  • 339
    • 0034032317 scopus 로고    scopus 로고
    • Insulinotropic glucagon-like peptide-1 agonists stimulate expression of homeodomain protein IDX-1 and increase β-cell mass in mouse pancreas
    • Stoffers DA, Kieffer TJ, Hussain MA, Drucker DJ, Egan JM, Bonner-Weir S, and Habener JF (2000) Insulinotropic glucagon-like peptide-1 agonists stimulate expression of homeodomain protein IDX-1 and increase β-cell mass in mouse pancreas. Diabetes 49:741-748.
    • (2000) Diabetes , vol.49 , pp. 741-748
    • Stoffers, D.A.1    Kieffer, T.J.2    Hussain, M.A.3    Drucker, D.J.4    Egan, J.M.5    Bonner-Weir, S.6    Habener, J.F.7
  • 340
    • 0024355831 scopus 로고
    • Mouse growth-hormone-releasing hormone: Precursor structure and expression in brain and placenta
    • Suhr ST, Rahal JO, and Mayo KE (1989) Mouse growth-hormone-releasing hormone: precursor structure and expression in brain and placenta. Mol Endocrinol 3:1693-1700.
    • (1989) Mol Endocrinol , vol.3 , pp. 1693-1700
    • Suhr, S.T.1    Rahal, J.O.2    Mayo, K.E.3
  • 341
    • 0013452668 scopus 로고
    • The effect of the hyperglycemic factor of the pancreas and of epinephrine on glycogenolysis
    • Sutherland EW (1950) The effect of the hyperglycemic factor of the pancreas and of epinephrine on glycogenolysis. Recent Prog Horm Res 5:441-459.
    • (1950) Recent Prog Horm Res , vol.5 , pp. 441-459
    • Sutherland, E.W.1
  • 343
    • 0031856534 scopus 로고    scopus 로고
    • Molecular cloning and in vitro properties of the recombinant rabbit secretin receptor
    • Svoboda M, Tastenoy M, De Neef P, Delporte C, Waelbroeck M, and Robberecht P (1998) Molecular cloning and in vitro properties of the recombinant rabbit secretin receptor. Peptides 19:1055-1062.
    • (1998) Peptides , vol.19 , pp. 1055-1062
    • Svoboda, M.1    Tastenoy, M.2    De Neef, P.3    Delporte, C.4    Waelbroeck, M.5    Robberecht, P.6
  • 344
    • 0027971885 scopus 로고
    • Relative quantitative analysis of glucagon receptor mRNA in rat tissues
    • Svoboda M, Tastenoy M, Vertongen P, and Robberecht P (1994) Relative quantitative analysis of glucagon receptor mRNA in rat tissues. Mol Cell Endocrinol 105:131-137.
    • (1994) Mol Cell Endocrinol , vol.105 , pp. 131-137
    • Svoboda, M.1    Tastenoy, M.2    Vertongen, P.3    Robberecht, P.4
  • 345
  • 346
    • 0029156720 scopus 로고
    • Identification of human growth hormone-releasing hormone receptor splicing variants
    • Tang J, Lagace G, Castagne J, and Collu R (1995) Identification of human growth hormone-releasing hormone receptor splicing variants. J Clin Endocrinol Metab 80:2381-2387.
    • (1995) J Clin Endocrinol Metab , vol.80 , pp. 2381-2387
    • Tang, J.1    Lagace, G.2    Castagne, J.3    Collu, R.4
  • 347
    • 0033914183 scopus 로고    scopus 로고
    • The proglucagon-derived peptide, glucagon-like peptide-2, is a neurotransmitter in-volved in the regulation of food intake
    • Tang-Christensen M, Larsen PJ, Thulesen J, Romer J, and Vrang N (2000) The proglucagon-derived peptide, glucagon-like peptide-2, is a neurotransmitter in-volved in the regulation of food intake. Nat Med 6:802-807.
    • (2000) Nat Med , vol.6 , pp. 802-807
    • Tang-Christensen, M.1    Larsen, P.J.2    Thulesen, J.3    Romer, J.4    Vrang, N.5
  • 348
    • 0026775150 scopus 로고
    • Expression cloning of the pancreatic β cell receptor for the glucoincretin hormone glucagon-like peptide 1
    • Thorens B (1992) Expression cloning of the pancreatic β cell receptor for the glucoincretin hormone glucagon-like peptide 1. Proe Natl Acad Sci USA 89:8641-8645.
    • (1992) Proe Natl Acad Sci USA , vol.89 , pp. 8641-8645
    • Thorens, B.1
  • 349
    • 0027425034 scopus 로고
    • Cloning and functional expression of the human islet GLP-1 receptor: Demonstration that exendin-4 is an agonist and exendin-(9-39) an antagonist of the receptor
    • Thorens B, Porret A, BŸhler L, Deng S-P, Morel P, and Widmann C (1993) Cloning and functional expression of the human islet GLP-1 receptor: demonstration that exendin-4 is an agonist and exendin-(9-39) an antagonist of the receptor. Diabetes 42:1678-1682.
    • (1993) Diabetes , vol.42 , pp. 1678-1682
    • Thorens, B.1    Porret, A.2    Bÿhler, L.3    Deng, S.-P.4    Morel, P.5    Widmann, C.6
  • 350
    • 0013411029 scopus 로고    scopus 로고
    • Structure and function of the glucagon-like peptide-1 receptor
    • Lefebvre PJ ed, Springer-Verlag, Berlin
    • Thorens B and Widmann C (1996) Structure and function of the glucagon-like peptide-1 receptor, in Handbook of Experimental Pharmacology Glucagon III (Lefebvre PJ ed) pp 255-273, Springer-Verlag, Berlin.
    • (1996) Handbook of Experimental Pharmacology Glucagon III , pp. 255-273
    • Thorens, B.1    Widmann, C.2
  • 351
    • 0020419989 scopus 로고
    • Somatotroph hyperplasia. Successful treatment of acromegaly by removal of a pancreatic islet tumor secreting a growth hormone-releasing factor
    • Thorner MO, Perryman RL, Cronin MJ, Rogol AD, Draznin M, Johanson A, Vale W, Horvath E, and Kovacs K (1982) Somatotroph hyperplasia. Successful treatment of acromegaly by removal of a pancreatic islet tumor secreting a growth hormone-releasing factor. J Clin Investig 70:965-977.
    • (1982) J Clin Investig , vol.70 , pp. 965-977
    • Thorner, M.O.1    Perryman, R.L.2    Cronin, M.J.3    Rogol, A.D.4    Draznin, M.5    Johanson, A.6    Vale, W.7    Horvath, E.8    Kovacs, K.9
  • 352
    • 0033790612 scopus 로고    scopus 로고
    • Potential targets for glucagon-like peptide 2 (GLP-2) in the rat: Distribution and binding of i. v. injected (125)I-GLP-2
    • Thulesen J, Hartmann B, Orskov C, Jeppesen PB, Holst JJ, and Poulsen SS (2000) Potential targets for glucagon-like peptide 2 (GLP-2) in the rat: distribution and binding of i. v. injected (125)I-GLP-2. Peptides 21:1511-1517.
    • (2000) Peptides , vol.21 , pp. 1511-1517
    • Thulesen, J.1    Hartmann, B.2    Orskov, C.3    Jeppesen, P.B.4    Holst, J.J.5    Poulsen, S.S.6
  • 354
    • 0035851103 scopus 로고    scopus 로고
    • A small molecule ligand of the glucagon-like peptide 1 receptor targets its amino-terminal hormone binding domain
    • Tibaduiza EC, Chen C, and Beinborn M (2001) A small molecule ligand of the glucagon-like peptide 1 receptor targets its amino-terminal hormone binding domain. J Biol Chem 276:37787-37793.
    • (2001) J Biol Chem , vol.276 , pp. 37787-37793
    • Tibaduiza, E.C.1    Chen, C.2    Beinborn, M.3
  • 355
    • 0023193492 scopus 로고
    • Secretin stimulates cyclic AMP and inositol trisphosphate production in rat pancreatic acinar tissue by two fully independent mechanisms
    • Trimble ER, Bruzzone R, Biden TJ, Meehan CJ, Andreu D, and Merrifield RB (1987) Secretin stimulates cyclic AMP and inositol trisphosphate production in rat pancreatic acinar tissue by two fully independent mechanisms. Proc Natl Acad Sci USA 84:3146-3150.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 3146-3150
    • Trimble, E.R.1    Bruzzone, R.2    Biden, T.J.3    Meehan, C.J.4    Andreu, D.5    Merrifield, R.B.6
  • 356
    • 0034838323 scopus 로고    scopus 로고
    • Glucose-dependent insulinotropic polypeptide is a growth factor for beta (INS-1) cells by pleiotropic signaling
    • Trumper A, Trumper K, Trusheim H, Arnold R, Goke B, and Horsch D (2001) Glucose-dependent insulinotropic polypeptide is a growth factor for beta (INS-1) cells by pleiotropic signaling. Mol Endocrinol 15:1559-1570.
    • (2001) Mol Endocrinol , vol.15 , pp. 1559-1570
    • Trumper, A.1    Trumper, K.2    Trusheim, H.3    Arnold, R.4    Goke, B.5    Horsch, D.6
  • 357
    • 0030759264 scopus 로고    scopus 로고
    • Intestinal growth-promoting properties of glucagon-like peptide 2 in mice
    • Tsai C-H, Hill M, Asa SL, Brubaker PL, and Drucker DJ (1997a) Intestinal growth-promoting properties of glucagon-like peptide 2 in mice. Am J Physiol 273:E77-E84.
    • (1997) Am J Physiol , vol.273
    • Tsai, C.-H.1    Hill, M.2    Asa, S.L.3    Brubaker, P.L.4    Drucker, D.J.5
  • 358
    • 0030977884 scopus 로고    scopus 로고
    • Biological determinants of intestinotrophic properties of GLP-2 in vivo
    • Tsai C-H, Hill M, and Drucker DJ (1997b) Biological determinants of intestinotrophic properties of GLP-2 in vivo. Am J Physiol 272:G662-G668.
    • (1997) Am J Physiol , vol.272
    • Tsai, C.-H.1    Hill, M.2    Drucker, D.J.3
  • 359
    • 0027532178 scopus 로고
    • Glucose-dependent insulinotropic peptide: Structure of the precursor and tissue-specific expression in rat
    • Tseng CC, Jarboe LA, Landau SB, Williams EK, and Wolfe MM (1993) Glucose-dependent insulinotropic peptide: structure of the precursor and tissue-specific expression in rat. Proc Natl Acad Sci USA 90:1992-1996.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 1992-1996
    • Tseng, C.C.1    Jarboe, L.A.2    Landau, S.B.3    Williams, E.K.4    Wolfe, M.M.5
  • 360
    • 0029834106 scopus 로고    scopus 로고
    • Postprandial stimulation of insulin release by glucose-dependent insulinotropic polypeptide (GIP). Effect of a specific glucose-dependent insulinotropic polypeptide receptor antagonist in the rat
    • Tseng CC, Kieffer TJ, Jarboe LA, Usdin TB, and Wolfe MM (1996) Postprandial stimulation of insulin release by glucose-dependent insulinotropic polypeptide (GIP). Effect of a specific glucose-dependent insulinotropic polypeptide receptor antagonist in the rat. J Clin Investig 98:2440-2445.
    • (1996) J Clin Investig , vol.98 , pp. 2440-2445
    • Tseng, C.C.1    Kieffer, T.J.2    Jarboe, L.A.3    Usdin, T.B.4    Wolfe, M.M.5
  • 361
    • 0031555863 scopus 로고    scopus 로고
    • A point mutation in the glucose-dependent insulinotropic peptide receptor confers constitutive activity
    • Tseng C-C and Lin L (1997) A point mutation in the glucose-dependent insulinotropic peptide receptor confers constitutive activity. Biochem Biophys Res Commun 232:96-100.
    • (1997) Biochem Biophys Res Commun , vol.232 , pp. 96-100
    • Tseng, C.-C.1    Lin, L.2
  • 362
    • 0032580293 scopus 로고    scopus 로고
    • The cysteine of the cytoplasmic tail of glucose-dependent insulinotropic peptide receptor mediates its chronic desensitization and down-regulation
    • Tseng CC and Zhang XY (1998) The cysteine of the cytoplasmic tail of glucose-dependent insulinotropic peptide receptor mediates its chronic desensitization and down-regulation. Mol Cell Endocrinol 139:179-186.
    • (1998) Mol Cell Endocrinol , vol.139 , pp. 179-186
    • Tseng, C.C.1    Zhang, X.Y.2
  • 364
    • 0031936197 scopus 로고    scopus 로고
    • Secretin and vasoactive intestinal peptide receptors: Members of a unique family of G protein-coupled receptors
    • Ulrich CD, Holtmann M, and Miller LJ (1998) Secretin and vasoactive intestinal peptide receptors: Members of a unique family of G protein-coupled receptors. Gastroenterology 114:382-397.
    • (1998) Gastroenterology , vol.114 , pp. 382-397
    • Ulrich, C.D.1    Holtmann, M.2    Miller, L.J.3
  • 367
    • 0028788229 scopus 로고
    • Characterization of deletion and truncation mutants of the rat glucagon receptor. Seven transmembrane segments are necessary for receptor transport to the plasma membrane and glucagon binding
    • Unson CG, Cypess AM, Kim HN, Goldsmith PK, Carruthers CJL, Merrifield RB, and Sakmar TP (1995) Characterization of deletion and truncation mutants of the rat glucagon receptor. Seven transmembrane segments are necessary for receptor transport to the plasma membrane and glucagon binding. J Biol Chem 270:27720-27727.
    • (1995) J Biol Chem , vol.270 , pp. 27720-27727
    • Unson, C.G.1    Cypess, A.M.2    Kim, H.N.3    Goldsmith, P.K.4    Carruthers, C.J.L.5    Merrifield, R.B.6    Sakmar, T.P.7
  • 369
    • 0025810274 scopus 로고
    • Position 9 replacement analogs of glucagon uncouple biological activity and receptor binding
    • Unson CG, Macdonald D, Ray K, Durrah TL, and Merrifield RB (1991) Position 9 replacement analogs of glucagon uncouple biological activity and receptor binding. J Biol Chem 266:2763-2766.
    • (1991) J Biol Chem , vol.266 , pp. 2763-2766
    • Unson, C.G.1    Macdonald, D.2    Ray, K.3    Durrah, T.L.4    Merrifield, R.B.5
  • 370
    • 0028115807 scopus 로고
    • Identification of an essential serine residue in glucagon: Implication for an active site triad
    • Unson CG and Merrifield RB (1994) Identification of an essential serine residue in glucagon: implication for an active site triad. Proc Natl Acad Sci USA 91:454-458.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 454-458
    • Unson, C.G.1    Merrifield, R.B.2
  • 371
    • 0036786132 scopus 로고    scopus 로고
    • Roles of specific extracellular domains of the glucagon receptor in ligand binding and signaling
    • Unson CG, Wu CR, Jiang Y, Yoo B, Cheung C, Sakmar TP, and Merrifield RB (2002) Roles of specific extracellular domains of the glucagon receptor in ligand binding and signaling. Biochemistry 41:11795-11803.
    • (2002) Biochemistry , vol.41 , pp. 11795-11803
    • Unson, C.G.1    Wu, C.R.2    Jiang, Y.3    Yoo, B.4    Cheung, C.5    Sakmar, T.P.6    Merrifield, R.B.7
  • 372
    • 0034647923 scopus 로고    scopus 로고
    • Selective stabilization of the high affinity binding conformation of glucagon receptor by the long splice variant of Galpha(s)
    • Unson CG, Wu CR, Sakmar TP, and Merrifield RB (2000) Selective stabilization of the high affinity binding conformation of glucagon receptor by the long splice variant of Galpha(s). J Biol Chem 275:21631-21638.
    • (2000) J Biol Chem , vol.275 , pp. 21631-21638
    • Unson, C.G.1    Wu, C.R.2    Sakmar, T.P.3    Merrifield, R.B.4
  • 373
    • 0027136670 scopus 로고
    • Gastric inhibitory polypeptide receptor, a member of the secretin-vasoactive intestinal peptide receptor family, is widely distributed in peripheral organs and the brain
    • Usdin TB, Mezey E, Button DC, Brownstein MJ, and Bonner TI (1993) Gastric inhibitory polypeptide receptor, a member of the secretin-vasoactive intestinal peptide receptor family, is widely distributed in peripheral organs and the brain. Endocrinology 133:2861-2870.
    • (1993) Endocrinology , vol.133 , pp. 2861-2870
    • Usdin, T.B.1    Mezey, E.2    Button, D.C.3    Brownstein, M.J.4    Bonner, T.I.5
  • 374
    • 0025246652 scopus 로고
    • Characterization of high affinity receptors for glucagon-like peptide-1 in rat gastric glands
    • Uttenthal LO and Blazquez E (1990) Characterization of high affinity receptors for glucagon-like peptide-1 in rat gastric glands. FEBS Lett 262:139-141.
    • (1990) FEBS Lett , vol.262 , pp. 139-141
    • Uttenthal, L.O.1    Blazquez, E.2
  • 375
    • 0027397282 scopus 로고
    • Presence and characterization of glucagon-like peptide-1(7-36) amide receptors in solubilized membranes of rat adipose tissue
    • Valverde I, Merida E, Delgado E, Trapote MA, and Villanueva-Penacarillo ML (1993) Presence and characterization of glucagon-like peptide-1(7-36) amide receptors in solubilized membranes of rat adipose tissue. Endocrinology 132:75-79.
    • (1993) Endocrinology , vol.132 , pp. 75-79
    • Valverde, I.1    Merida, E.2    Delgado, E.3    Trapote, M.A.4    Villanueva-Penacarillo, M.L.5
  • 376
    • 0028233622 scopus 로고
    • Signal transduction of the GLP-1-receptor cloned from a human insulinoma
    • Van Eyll B, Lankat-Buttgereit B, Bode HP, Goke R, and Goke B (1994) Signal transduction of the GLP-1-receptor cloned from a human insulinoma. FEBS Lett 348:7-13.
    • (1994) FEBS Lett , vol.348 , pp. 7-13
    • Van Eyll, B.1    Lankat-Buttgereit, B.2    Bode, H.P.3    Goke, R.4    Goke, B.5
  • 377
    • 0033582289 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of antagonists of growth hormone-releasing hormone with high and protracted in vivo activities
    • Varga JL, Schally AV, Csernus VJ, Zarandi M, Halmos G, Groot K, and Rekasi Z (1999) Synthesis and biological evaluation of antagonists of growth hormone-releasing hormone with high and protracted in vivo activities. Proc Natl Acad Sci USA 96:692-697.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 692-697
    • Varga, J.L.1    Schally, A.V.2    Csernus, V.J.3    Zarandi, M.4    Halmos, G.5    Groot, K.6    Rekasi, Z.7
  • 378
    • 0034048147 scopus 로고    scopus 로고
    • Pituitary adenylate cyclase-activating polypeptide and its receptors: From structure to functions
    • Vaudry D, Gonzalez BJ, Basille M, Yon L, Fournier A, and Vaudry H (2000) Pituitary adenylate cyclase-activating polypeptide and its receptors: from structure to functions. Pharmacol Rev 52:269-324.
    • (2000) Pharmacol Rev , vol.52 , pp. 269-324
    • Vaudry, D.1    Gonzalez, B.J.2    Basille, M.3    Yon, L.4    Fournier, A.5    Vaudry, H.6
  • 379
    • 0022004035 scopus 로고
    • Specific binding of synthetic human pancreatic growth hormone releasing factor (1-40-OH) to bovine anterior pituitaries
    • Velicelebi G, Santacroce TM, and Harpold MM (1985) Specific binding of synthetic human pancreatic growth hormone releasing factor (1-40-OH) to bovine anterior pituitaries. Biochem Biophys Res Commun 126:33-39.
    • (1985) Biochem Biophys Res Commun , vol.126 , pp. 33-39
    • Velicelebi, G.1    Santacroce, T.M.2    Harpold, M.M.3
  • 381
    • 0029016549 scopus 로고
    • Properties of chimeric secretin and VIP receptor proteins indicate the importance of the N-terminal domain for ligand discrimination
    • Vilardaga JP, De Neef P, Di Paolo E, Bollen A, Waelbroeck M, and Robberecht P (1995) Properties of chimeric secretin and VIP receptor proteins indicate the importance of the N-terminal domain for ligand discrimination. Biochem Biophys Res Commun 211:885-891.
    • (1995) Biochem Biophys Res Commun , vol.211 , pp. 885-891
    • Vilardaga, J.P.1    De Neef, P.2    Di Paolo, E.3    Bollen, A.4    Waelbroeck, M.5    Robberecht, P.6
  • 382
    • 0001095690 scopus 로고    scopus 로고
    • Reduced postprandial concentrations of intact biologically active glucagon-like peptide 1 in type 2 diabetic patients
    • Vilsboll T, Krarup T, Deacon CF, Madsbad S, and Holst JJ (2001) Reduced postprandial concentrations of intact biologically active glucagon-like peptide 1 in type 2 diabetic patients. Diabetes 50:609-613.
    • (2001) Diabetes , vol.50 , pp. 609-613
    • Vilsboll, T.1    Krarup, T.2    Deacon, C.F.3    Madsbad, S.4    Holst, J.J.5
  • 383
    • 0028501308 scopus 로고
    • Human growth hormone-releasing hormone receptor (GHRHR) maps to a YAC at chromosome 7p15
    • Wajnrajch MP, Chua SC, Green ED, and Leibel RL (1994) Human growth hormone-releasing hormone receptor (GHRHR) maps to a YAC at chromosome 7p15. Mamm Genome 5:595.
    • (1994) Mamm Genome , vol.5 , pp. 595
    • Wajnrajch, M.P.1    Chua, S.C.2    Green, E.D.3    Leibel, R.L.4
  • 384
    • 0030033150 scopus 로고    scopus 로고
    • Nonsense mutation in the human growth hormone-releasing hormone receptor causes growth failure analogous to the little (lit) mouse
    • Wajnrajch MP, Gertner JM, Harbison MD, Chua SC Jr, and Leibel RL (1996) Nonsense mutation in the human growth hormone-releasing hormone receptor causes growth failure analogous to the little (lit) mouse. Nat Genet 12:88-90.
    • (1996) Nat Genet , vol.12 , pp. 88-90
    • Wajnrajch, M.P.1    Gertner, J.M.2    Harbison, M.D.3    Chua S.C., Jr.4    Leibel, R.L.5
  • 385
    • 0023041534 scopus 로고
    • Activation of two signal-transduction systems in hepatocytes by glucagon
    • Wakelam MJ, Murphy GJ, Hruby VJ, and Houslay MD (1986) Activation of two signal-transduction systems in hepatocytes by glucagon. Nature (Lond) 323:68-71.
    • (1986) Nature (Lond) , vol.323 , pp. 68-71
    • Wakelam, M.J.1    Murphy, G.J.2    Hruby, V.J.3    Houslay, M.D.4
  • 386
    • 0028900758 scopus 로고
    • Tissue-specific expression of the human receptor for glucagon-like peptide 1: Brain, heart and pancreatic forms have the same deduced amino acid sequences
    • Wei Y and Mojsov S (1995) Tissue-specific expression of the human receptor for glucagon-like peptide 1: brain, heart and pancreatic forms have the same deduced amino acid sequences. FEBS Lett 358:219-224.
    • (1995) FEBS Lett , vol.358 , pp. 219-224
    • Wei, Y.1    Mojsov, S.2
  • 387
    • 0033609824 scopus 로고    scopus 로고
    • Characterization of the carboxyl-terminal domain of the rat glucose-dependent insulinotropic polypeptide (GIP) receptor. A role for serines 426 and 427 in regulating the rate of internalization
    • Wheeler MB, Gelling RW, Hinke SA, Tu B, Pederson RA, Lynn F, Ehses J, and McIntosh CH (1999) Characterization of the carboxyl-terminal domain of the rat glucose-dependent insulinotropic polypeptide (GIP) receptor. A role for serines 426 and 427 in regulating the rate of internalization. J Biol Chem 274:24593-24601.
    • (1999) J Biol Chem , vol.274 , pp. 24593-24601
    • Wheeler, M.B.1    Gelling, R.W.2    Hinke, S.A.3    Tu, B.4    Pederson, R.A.5    Lynn, F.6    Ehses, J.7    McIntosh, C.H.8
  • 388
    • 0029082308 scopus 로고
    • Functional expression of the rat pancreatic islet glucose-dependent insulinotropic polypeptide receptor: Ligand binding and intracellular signaling properties
    • Wheeler MB, Gelling RW, McIntosh CH, Georgiou J, Brown JC, and Pederson RA (1995) Functional expression of the rat pancreatic islet glucose-dependent insulinotropic polypeptide receptor: ligand binding and intracellular signaling properties. Endocrinology 136:4629-4639.
    • (1995) Endocrinology , vol.136 , pp. 4629-4639
    • Wheeler, M.B.1    Gelling, R.W.2    McIntosh, C.H.3    Georgiou, J.4    Brown, J.C.5    Pederson, R.A.6
  • 389
    • 0031001096 scopus 로고    scopus 로고
    • Internalization and homologous desensitization of the GLP-1 receptor depend on phosphorylation of the receptor carboxyl tail at the same three sites
    • Widmann C, Dolci W, and Thorens B (1997) Internalization and homologous desensitization of the GLP-1 receptor depend on phosphorylation of the receptor carboxyl tail at the same three sites. Mol Endocrinol 11:1094-1102.
    • (1997) Mol Endocrinol , vol.11 , pp. 1094-1102
    • Widmann, C.1    Dolci, W.2    Thorens, B.3
  • 390
    • 0032955215 scopus 로고    scopus 로고
    • Gene expression of the human glucagon-like peptide-1 receptor is regulated by Sp1 and Sp3
    • Wildhage I, Trusheim H, Goke B, and Lankat-Buttgereit B (1999) Gene expression of the human glucagon-like peptide-1 receptor is regulated by Sp1 and Sp3. Endocrinology 140:624-631.
    • (1999) Endocrinology , vol.140 , pp. 624-631
    • Wildhage, I.1    Trusheim, H.2    Goke, B.3    Lankat-Buttgereit, B.4
  • 391
    • 0030921314 scopus 로고    scopus 로고
    • Five out ofsix tryptophan residues in the N-terminal extracellular domain of the rat GLP-1 receptor are essential for its ability to bind GLP-1
    • Wilmen A, Van Eyll B, Goke B, and Goke R (1997) Five out ofsix tryptophan residues in the N-terminal extracellular domain of the rat GLP-1 receptor are essential for its ability to bind GLP-1. Peptides 18:301-305.
    • (1997) Peptides , vol.18 , pp. 301-305
    • Wilmen, A.1    Van Eyll, B.2    Goke, B.3    Goke, R.4
  • 392
    • 0033998750 scopus 로고    scopus 로고
    • Circulating levels of glucagon-like peptide-2 in human subjects with inflammatory bowel disease
    • Xiao Q, Boushey RP, Cino M, Drucker DJ, and Brubaker PL (2000a) Circulating levels of glucagon-like peptide-2 in human subjects with inflammatory bowel disease. Am J Physiol 278:R1057-R1063.
    • (2000) Am J Physiol , vol.278
    • Xiao, Q.1    Boushey, R.P.2    Cino, M.3    Drucker, D.J.4    Brubaker, P.L.5
  • 393
    • 0033028489 scopus 로고    scopus 로고
    • Secretion of the intestinotropic hormone glucagon-like peptide 2 is differentially regulated by nutrients in humans
    • Xiao Q, Boushey RP, Drucker DJ, and Brubaker PL (1999) Secretion of the intestinotropic hormone glucagon-like peptide 2 is differentially regulated by nutrients in humans. Gastroenterology 117:99-105.
    • (1999) Gastroenterology , vol.117 , pp. 99-105
    • Xiao, Q.1    Boushey, R.P.2    Drucker, D.J.3    Brubaker, P.L.4
  • 395
    • 0034522536 scopus 로고    scopus 로고
    • Characterization of glucagon-like peptide-1 receptor-binding determinants
    • Xiao Q, Jeng W, and Wheeler MB (2000b) Characterization of glucagon-like peptide-1 receptor-binding determinants. J Mol Endocrinol 25:321-335.
    • (2000) J Mol Endocrinol , vol.25 , pp. 321-335
    • Xiao, Q.1    Jeng, W.2    Wheeler, M.B.3
  • 396
    • 0027484189 scopus 로고
    • Glucagon-like peptide-1-(7-36)amide and a rise in cyclic adenosine 3′, 5′-monophosphate increase cytosolic free Ca2+ in rat pancreatic b-cells by enhancing Ca2+ channel activity
    • Yada T, Itoh K, and Nakata M (1993) Glucagon-like peptide-1-(7-36)amide and a rise in cyclic adenosine 3′, 5′-monophosphate increase cytosolic free Ca2+ in rat pancreatic b-cells by enhancing Ca2+ channel activity. Endocrinology 133:1685-1692.
    • (1993) Endocrinology , vol.133 , pp. 1685-1692
    • Yada, T.1    Itoh, K.2    Nakata, M.3
  • 399
    • 0030996638 scopus 로고    scopus 로고
    • Tissue-specific and glucose-dependent expression of receptor genes for glucagon and glucagon-like peptide-1 (GLP-1)
    • Yamato E, Ikegami H, Takekawa K, Fujisawa T, Nakagawa Y, Hamada Y, Ueda H, and Ogihara T (1997) Tissue-specific and glucose-dependent expression of receptor genes for glucagon and glucagon-like peptide-1 (GLP-1). Horm Metab Res 29:56-59.
    • (1997) Horm Metab Res , vol.29 , pp. 56-59
    • Yamato, E.1    Ikegami, H.2    Takekawa, K.3    Fujisawa, T.4    Nakagawa, Y.5    Hamada, Y.6    Ueda, H.7    Ogihara, T.8
  • 400
    • 0028556401 scopus 로고
    • Hamster gastric inhibitory polypeptide receptor expressed in pancreatic islets and clonal insulin-secreting cells: Its structure and functional properties
    • Yasuda K, Inagaki N, Yamada Y, Kubota A, Seino S, and Seino Y (1994) Hamster gastric inhibitory polypeptide receptor expressed in pancreatic islets and clonal insulin-secreting cells: its structure and functional properties. Biochem Biophys Res Commun 205:1556-1562.
    • (1994) Biochem Biophys Res Commun , vol.205 , pp. 1556-1562
    • Yasuda, K.1    Inagaki, N.2    Yamada, Y.3    Kubota, A.4    Seino, S.5    Seino, Y.6
  • 401
    • 0033520869 scopus 로고    scopus 로고
    • GIP biology and fat metabolism
    • Yip RG and Wolfe MM (2000) GIP biology and fat metabolism. Life Sci 66:91-103.
    • (2000) Life Sci , vol.66 , pp. 91-103
    • Yip, R.G.1    Wolfe, M.M.2
  • 402
    • 0034634637 scopus 로고    scopus 로고
    • The glucagon-like peptide-2 receptor mediates direct inhibition of cellular apoptosis via a cAMP-dependent protein kinase-independent pathway
    • Yusta B, Boushey RP, and Drucker DJ (2000a) The glucagon-like peptide-2 receptor mediates direct inhibition of cellular apoptosis via a cAMP-dependent protein kinase-independent pathway. J Biol Chem 275:35345-35352.
    • (2000) J Biol Chem , vol.275 , pp. 35345-35352
    • Yusta, B.1    Boushey, R.P.2    Drucker, D.J.3
  • 403
    • 0037067677 scopus 로고    scopus 로고
    • Glucago-like peptide-2 receptor activation engages Bad and glycogen synthase kinase 3 in a protein kinase A-dependent manner and prevents apoptosis following inhibition of phosphatidylinositol 3-kinase
    • Yusta B, Estall J, and Drucker DJ (2002) Glucago-like peptide-2 receptor activation engages Bad and glycogen synthase kinase 3 in a protein kinase A-dependent manner and prevents apoptosis following inhibition of phosphatidylinositol 3-kinase. J Biol Chem 277:24896-24906.
    • (2002) J Biol Chem , vol.277 , pp. 24896-24906
    • Yusta, B.1    Estall, J.2    Drucker, D.J.3
  • 405
    • 0032718059 scopus 로고    scopus 로고
    • Identification of glucagon-like peptide-2 (GLP-2)-activated signaling pathways in baby hamster kidney fibroblasts expressing the rat GLP-2 receptor
    • Yusta B, Somwar R, Wang F, Munroe D, Grinstein S, Klip A, and Drucker DJ (1999) Identification of glucagon-like peptide-2 (GLP-2)-activated signaling pathways in baby hamster kidney fibroblasts expressing the rat GLP-2 receptor. J Biol Chem 274:30459-30467.
    • (1999) J Biol Chem , vol.274 , pp. 30459-30467
    • Yusta, B.1    Somwar, R.2    Wang, F.3    Munroe, D.4    Grinstein, S.5    Klip, A.6    Drucker, D.J.7
  • 406
    • 0037045845 scopus 로고    scopus 로고
    • Effect of 6-week course of glucagon-like peptide 1 on glycaemic control, insulin sensitivity and beta-cell function in type 2 diabetes: A parallel-group study
    • Zander M, Madsbad S, Madsen JL, and Holst JJ (2002) Effect of 6-week course of glucagon-like peptide 1 on glycaemic control, insulin sensitivity and beta-cell function in type 2 diabetes: a parallel-group study. Lancet 359:824-830.
    • (2002) Lancet , vol.359 , pp. 824-830
    • Zander, M.1    Madsbad, S.2    Madsen, J.L.3    Holst, J.J.4
  • 408
    • 0033919689 scopus 로고    scopus 로고
    • Stimulation of mitogen-activated protein kinase pathway in rat somatotrophs by growth hormone-releasing hormone
    • Zeitler P and Siriwardana G (2000) Stimulation of mitogen-activated protein kinase pathway in rat somatotrophs by growth hormone-releasing hormone. Endocrine 12:257-264.
    • (2000) Endocrine , vol.12 , pp. 257-264
    • Zeitler, P.1    Siriwardana, G.2
  • 409
    • 0032413906 scopus 로고    scopus 로고
    • Functional GHRH receptor carboxyl terminal isoforms in normal and dwarf (dw) rats
    • Zeitler P, Stevens P, and Siriwardana G (1998) Functional GHRH receptor carboxyl terminal isoforms in normal and dwarf (dw) rats. J Mol Endocrinol 21:363-371.
    • (1998) J Mol Endocrinol , vol.21 , pp. 363-371
    • Zeitler, P.1    Stevens, P.2    Siriwardana, G.3
  • 410
    • 0033866831 scopus 로고    scopus 로고
    • New approaches in the treatment of type 2 diabetes
    • Zhang BB and Moller DE (2000) New approaches in the treatment of type 2 diabetes. Curr Opin Chem Biol 4:461-467.
    • (2000) Curr Opin Chem Biol , vol.4 , pp. 461-467
    • Zhang, B.B.1    Moller, D.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.