메뉴 건너뛰기




Volumn 50, Issue , 2010, Pages 121-135

Glucagon and glucagon-like peptides 1 and 2

Author keywords

[No Author keywords available]

Indexed keywords

GLUCAGON; GLUCAGON LIKE PEPTIDE; GLUCAGON LIKE PEPTIDE 1; GLUCAGON LIKE PEPTIDE 2; PEPTIDE; PEPTIDE FRAGMENT; PROPROTEIN CONVERTASE 1; PROPROTEIN CONVERTASE 2;

EID: 77950221874     PISSN: 00801844     EISSN: 18610412     Source Type: Book Series    
DOI: 10.1007/400_2009_35     Document Type: Article
Times cited : (42)

References (109)
  • 1
    • 0021362497 scopus 로고
    • Glucagon-related peptides in the human gastrointestinal mucosa
    • Baldissera FG, Holst JJ (1984) Glucagon-related peptides in the human gastrointestinal mucosa. Diabetologia 26:223-228
    • (1984) Diabetologia , vol.26 , pp. 223-228
    • Baldissera, F.G.1    Holst, J.J.2
  • 2
    • 0022531614 scopus 로고
    • Glicentin 1-61 probably represents a major fraction of glucagonrelated peptides in plasma of anaesthetized uraemic pigs
    • Baldissera FG, Holst JJ (1986) Glicentin 1-61 probably represents a major fraction of glucagonrelated peptides in plasma of anaesthetized uraemic pigs. Diabetologia 29:462-467
    • (1986) Diabetologia , vol.29 , pp. 462-467
    • Baldissera, F.G.1    Holst, J.J.2
  • 3
    • 34447325119 scopus 로고    scopus 로고
    • Pro-protein convertases in intermediary metabolism: Islet hormones, brain/gut hormones and integrated physiology
    • Bataille D (2007) Pro-protein convertases in intermediary metabolism: islet hormones, brain/gut hormones and integrated physiology. J Mol Med 85:673-684
    • (2007) J Mol Med , vol.85 , pp. 673-684
    • Bataille, D.1
  • 4
    • 0020377971 scopus 로고
    • Isolation of glucagon-37 (bioactive enteroglucagon/ oxyntomodulin) from porcine jejuno-ileum. Characterization of the peptide
    • Bataille D, Tatemoto K, Gespach C et al (1982) Isolation of glucagon-37 (bioactive enteroglucagon/ oxyntomodulin) from porcine jejuno-ileum. Characterization of the peptide. FEBS Lett 146:79-86
    • (1982) FEBS Lett , vol.146 , pp. 79-86
    • Bataille, D.1    Tatemoto, K.2    Gespach, C.3
  • 5
    • 0020535282 scopus 로고
    • Exon duplication and divergence in the human preproglucagon gene
    • Bell GI, Sanchez-Pescador R, Laybourn PJ et al (1983a) Exon duplication and divergence in the human preproglucagon gene. Nature 304:368-371
    • (1983) Nature , vol.304 , pp. 368-371
    • Bell, G.I.1    Sanchez-Pescador, R.2    Laybourn, P.J.3
  • 6
    • 0020596734 scopus 로고
    • Hamster preproglucagon contains the sequence of glucagon and two related peptides
    • Bell GI, Santerre RF, Mullenbach GT (1983b) Hamster preproglucagon contains the sequence of glucagon and two related peptides. Nature 302:716-718
    • (1983) Nature , vol.302 , pp. 716-718
    • Bell, G.I.1    Santerre, R.F.2    Mullenbach, G.T.3
  • 7
    • 0022617570 scopus 로고
    • Co-existence of glicentin and peptide YY in colorectal L-cells in cat and man. An electron microscopic study
    • Bottcher G, Alumets J, Hakanson R et al (1986) Co-existence of glicentin and peptide YY in colorectal L-cells in cat and man. An electron microscopic study. Regul Pept 13:283-291
    • (1986) Regul Pept , vol.13 , pp. 283-291
    • Bottcher, G.1    Alumets, J.2    Hakanson, R.3
  • 8
    • 0020657971 scopus 로고
    • Measurement of gut hormonal peptides in biopsies from human stomach and proximal small intestine
    • Bryant MG, Bloom SR, Polak JM et al (1983) Measurement of gut hormonal peptides in biopsies from human stomach and proximal small intestine. Gut 24:114-119
    • (1983) Gut , vol.24 , pp. 114-119
    • Bryant, M.G.1    Bloom, S.R.2    Polak, J.M.3
  • 9
    • 0018121828 scopus 로고
    • Types of endocrine cells in the human colon and rectum
    • Buffa R, Capella C, Fontana P et al (1978) Types of endocrine cells in the human colon and rectum. Cell Tissue Res 192:227-240
    • (1978) Cell Tissue Res , vol.192 , pp. 227-240
    • Buffa, R.1    Capella, C.2    Fontana, P.3
  • 10
    • 0023930669 scopus 로고
    • Naturally occurring products of proglucagon 111-160 in the porcine and human small intestine
    • Buhl T, Thim L, Kofod H et al (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
  • 11
    • 0029954211 scopus 로고    scopus 로고
    • Glucagonostatic actions and reduction of fasting hyperglycemia by exogenous glucagon-like peptide I(7-36) amide in type i diabetic patients
    • Creutzfeldt WO, Kleine N, Willms B et al (1996) Glucagonostatic actions and reduction of fasting hyperglycemia by exogenous glucagon-like peptide I(7-36) amide in type I diabetic patients. Diabetes Care 19:580-586
    • (1996) Diabetes Care , vol.19 , pp. 580-586
    • Creutzfeldt, W.O.1    Kleine, N.2    Willms, B.3
  • 12
    • 55649108863 scopus 로고    scopus 로고
    • Glucagon-like peptide-1, but not glucose-dependent insulinotropic peptide, inhibits glucagon secretion via somatostatin (receptor subtype 2) in the perfused rat pancreas
    • de Heer J, Rasmussen C, Coy DH et al (2008) Glucagon-like peptide-1, but not glucose-dependent insulinotropic peptide, inhibits glucagon secretion via somatostatin (receptor subtype 2) in the perfused rat pancreas. Diabetologia 51:2263-2270
    • (2008) Diabetologia , vol.51 , pp. 2263-2270
    • De Heer, J.1    Rasmussen, C.2    Coy, D.H.3
  • 13
    • 0028953577 scopus 로고
    • Degradation of glucagon-like peptide-1 by human plasma in vitro yields an N-terminally truncated peptide that is a major endogenous metabolite in vivo
    • Deacon CF, Johnsen AH, Holst JJ (1995) Degradation of glucagon-like peptide-1 by human plasma in vitro yields an N-terminally truncated peptide that is a major endogenous metabolite in vivo. J Clin Endocrinol Metab 80:952-957
    • (1995) J Clin Endocrinol Metab , vol.80 , pp. 952-957
    • Deacon, C.F.1    Johnsen, A.H.2    Holst, J.J.3
  • 14
    • 0029797540 scopus 로고    scopus 로고
    • Glucagon-like peptide 1 undergoes differential tissue-specific metabolism in the anesthetized pig
    • Deacon CF, Pridal L, Klarskov L et al (1996) Glucagon-like peptide 1 undergoes differential tissue-specific metabolism in the anesthetized pig. Am J Physiol 271:E458-E464
    • (1996) Am J Physiol , vol.271
    • Deacon, C.F.1    Pridal, L.2    Klarskov, L.3
  • 16
    • 33644618433 scopus 로고    scopus 로고
    • The biology of incretin hormones
    • Drucker DJ (2006) The biology of incretin hormones. Cell Metab 3:153-165
    • (2006) Cell Metab , vol.3 , pp. 153-165
    • Drucker, D.J.1
  • 17
    • 0023787950 scopus 로고
    • Glucagon gene expression in vertebrate brain
    • Drucker DJ, 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
  • 18
    • 0026510891 scopus 로고
    • Glucagon-like peptide-1 cells in the gastrointestinal tract and pancreas of rat, pig and man
    • Eissele R, Goke R, Willemer S et al (1992) Glucagon-like peptide-1 cells in the gastrointestinal tract and pancreas of rat, pig and man. Eur J Clin Invest 22:283-291
    • (1992) Eur J Clin Invest , vol.22 , pp. 283-291
    • Eissele, R.1    Goke, R.2    Willemer, S.3
  • 19
    • 0031898957 scopus 로고    scopus 로고
    • Mouse pancreatic beta-cells exhibit preserved glucose competence after disruption of the glucagon-like peptide-1 receptor gene
    • Flamez D, Van Breusegem A, Scrocchi LA et al (1998) Mouse pancreatic beta-cells exhibit preserved glucose competence after disruption of the glucagon-like peptide-1 receptor gene. Diabetes 47:646-652
    • (1998) Diabetes , vol.47 , pp. 646-652
    • Flamez, D.1    Van Breusegem, A.2    Scrocchi, L.A.3
  • 20
    • 12644253798 scopus 로고    scopus 로고
    • Defective prohormone processing and altered pancreatic islet morphology in mice lacking active SPC2
    • Furuta M, Yano H, Zhou A et al (1997) Defective prohormone processing and altered pancreatic islet morphology in mice lacking active SPC2. Proc Natl Acad Sci USA 94:6646-6651
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 6646-6651
    • Furuta, M.1    Yano, H.2    Zhou, A.3
  • 21
    • 0037417984 scopus 로고    scopus 로고
    • Lower blood glucose, hyperglucagonemia, and pancreatic alpha cell hyperplasia in glucagon receptor knockout mice
    • Gelling RW, Du XQ, Dichmann DS et al (2003) Lower blood glucose, hyperglucagonemia, and pancreatic alpha cell hyperplasia in glucagon receptor knockout mice. Proc Natl Acad Sci USA 100:1438-1443
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 1438-1443
    • Gelling, R.W.1    Du, X.Q.2    Dichmann, D.S.3
  • 22
    • 32544451924 scopus 로고    scopus 로고
    • Variant of transcription factor 7-like 2 (TCF7L2) gene confers risk of type 2 diabetes
    • Grant SF, Thorleifsson G, Reynisdottir I et al (2006) Variant of transcription factor 7-like 2 (TCF7L2) gene confers risk of type 2 diabetes. Nat Genet 38:320-323
    • (2006) Nat Genet , vol.38 , pp. 320-323
    • Grant, S.F.1    Thorleifsson, G.2    Reynisdottir, I.3
  • 23
    • 0017284469 scopus 로고
    • Cytochemical and ultrastructural differentiation of enteroglucagon and pancreatic-type glucagon cells of the gastrointestinal tract
    • Grimelius L, Capella C, Buffa R et al (1976) Cytochemical and ultrastructural differentiation of enteroglucagon and pancreatic-type glucagon cells of the gastrointestinal tract. Virchows Arch B Cell Pathol 20:217-228
    • (1976) Virchows Arch B Cell Pathol , vol.20 , pp. 217-228
    • Grimelius, L.1    Capella, C.2    Buffa, R.3
  • 24
    • 0033303516 scopus 로고    scopus 로고
    • Glucagon-like peptide-1-(7-36)amide is transformed to glucagon-like peptide-1-(9-36)amide by dipeptidyl peptidase IV in the capillaries supplying the L cells of the porcine intestine [In Process Citation]
    • Hansen L, Deacon CF, Orskov C et al (1999) Glucagon-like peptide-1-(7-36)amide is transformed to glucagon-like peptide-1-(9-36)amide by dipeptidyl peptidase IV in the capillaries supplying the L cells of the porcine intestine [In Process Citation]. Endocrinology 140:5356-5363
    • (1999) Endocrinology , vol.140 , pp. 5356-5363
    • Hansen, L.1    Deacon, C.F.2    Orskov, C.3
  • 25
    • 0033921741 scopus 로고    scopus 로고
    • Somatostatin restrains the secretion of glucagonlike peptide-1 and 2 from isolated perfused porcine ileum
    • Hansen L, Hartmann B, Bisgaard T et al (2000) Somatostatin restrains the secretion of glucagonlike peptide-1 and 2 from isolated perfused porcine ileum. Am J Physiol 278:E1010-E1018
    • (2000) Am J Physiol , vol.278
    • Hansen, L.1    Hartmann, B.2    Bisgaard, T.3
  • 26
    • 0842346386 scopus 로고    scopus 로고
    • Glucagon-like peptide-1 secretion is influenced by perfusate glucose concentration and by a feedback mechanism involving somatostatin in isolated perfused porcine ileum
    • Hansen L, Hartmann B, Mineo H et al (2004) Glucagon-like peptide-1 secretion is influenced by perfusate glucose concentration and by a feedback mechanism involving somatostatin in isolated perfused porcine ileum. Regul Pept 118:11-18
    • (2004) Regul Pept , vol.118 , pp. 11-18
    • Hansen, L.1    Hartmann, B.2    Mineo, H.3
  • 27
    • 0034457973 scopus 로고    scopus 로고
    • In vivo and in vitro degradation of glucagonlike peptide-2 in humans
    • Hartmann B, Harr MB, Jeppesen PB et al (2000a) In vivo and in vitro degradation of glucagonlike peptide-2 in humans. J Clin Endocrinol Metab 85:2884-2888
    • (2000) J Clin Endocrinol Metab , vol.85 , pp. 2884-2888
    • Hartmann, B.1    Harr, M.B.2    Jeppesen, P.B.3
  • 28
    • 0033993906 scopus 로고    scopus 로고
    • Structure, measurement, and secretion of human glucagon-like peptide-2 [In Process Citation]
    • Hartmann B, Johnsen AH, Orskov C et al (2000b) Structure, measurement, and secretion of human glucagon-like peptide-2 [In Process Citation]. Peptides 21:73-80
    • (2000) Peptides , vol.21 , pp. 73-80
    • Hartmann, B.1    Johnsen, A.H.2    Orskov, C.3
  • 29
    • 0021746964 scopus 로고
    • Glucagon gene sequence. Four of six exons encode separate functional domains of rat pre-proglucagon
    • Heinrich G, Gros P, Habener JF (1984) Glucagon gene sequence. Four of six exons encode separate functional domains of rat pre-proglucagon. J Biol Chem 259:14082-14087
    • (1984) J Biol Chem , vol.259 , pp. 14082-14087
    • Heinrich, G.1    Gros, P.2    Habener, J.F.3
  • 30
    • 0029189516 scopus 로고
    • Intra-islet regulation of hormone secretion by glucagon-like peptide-1- (7-36) amide
    • Heller RS, Aponte GW (1995) Intra-islet regulation of hormone secretion by glucagon-like peptide-1- (7-36) amide. Am J Physiol 269:G852-G860
    • (1995) Am J Physiol , vol.269
    • Heller, R.S.1    Aponte, G.W.2
  • 31
    • 0033305721 scopus 로고    scopus 로고
    • Essential requirement for Pax6 in control of enteroendocrine proglucagon gene transcription
    • Hill ME, Asa SL, Drucker DJ (1999) Essential requirement for Pax6 in control of enteroendocrine proglucagon gene transcription. Mol Endocrinol 13:1474-1486
    • (1999) Mol Endocrinol , vol.13 , pp. 1474-1486
    • Hill, M.E.1    Asa, S.L.2    Drucker, D.J.3
  • 32
    • 0018946923 scopus 로고
    • Evidence that glicentin contains the entire sequence of glucagon
    • Holst JJ (1980) Evidence that glicentin contains the entire sequence of glucagon. Biochem J 187:337-343
    • (1980) Biochem J , vol.187 , pp. 337-343
    • Holst, J.J.1
  • 33
    • 0020456354 scopus 로고
    • Evidence that enteroglucagon (II) is identical with the C- terminal sequence (residues 33-69) of glicentin
    • Holst JJ (1982) Evidence that enteroglucagon (II) is identical with the C- terminal sequence (residues 33-69) of glicentin. Biochem J 207:381-388
    • (1982) Biochem J , vol.207 , pp. 381-388
    • Holst, J.J.1
  • 35
    • 0020696540 scopus 로고
    • Content and gel filtration profiles of glucagon-like and somatostatin- like immunoreactivity in human fundic mucosa
    • Holst JJ, Aggestrup S, Loud FB et al (1983a) Content and gel filtration profiles of glucagon-like and somatostatin- like immunoreactivity in human fundic mucosa. J Clin Endocrinol Metab 56:729-732
    • (1983) J Clin Endocrinol Metab , vol.56 , pp. 729-732
    • Holst, J.J.1    Aggestrup, S.2    Loud, F.B.3
  • 36
    • 0021058005 scopus 로고
    • Circulating glucagon after total pancreatectomy in man
    • Holst JJ, Pedersen JH, Baldissera F et al (1983b) Circulating glucagon after total pancreatectomy in man. Diabetologia 25:396-399
    • (1983) Diabetologia , vol.25 , pp. 396-399
    • Holst, J.J.1    Pedersen, J.H.2    Baldissera, F.3
  • 37
    • 0023104829 scopus 로고
    • Truncated glucagon-like peptide I, an insulin-releasing hormone from the distal gut
    • Holst JJ, Orskov C, Nielsen OV et al (1987) Truncated glucagon-like peptide I, an insulin-releasing hormone from the distal gut. FEBS Lett 211:169-174
    • (1987) FEBS Lett , vol.211 , pp. 169-174
    • Holst, J.J.1    Orskov, C.2    Nielsen, O.V.3
  • 38
    • 0028234355 scopus 로고
    • Proglucagon processing in porcine and human pancreas
    • Holst JJ, Bersani M, Johnsen AH et al (1994) Proglucagon processing in porcine and human pancreas. J BiolChem 269:18827-18833
    • (1994) J BiolChem , vol.269 , pp. 18827-18833
    • Holst, J.J.1    Bersani, M.2    Johnsen, A.H.3
  • 39
    • 0030758090 scopus 로고    scopus 로고
    • Endoproteolysis of glucagon-like peptide (GLP)-1 (7-36) amide by ectopeptidases in RINm5F cells
    • Hupe-Sodmann K, Goke R, Goke B et al (1997) Endoproteolysis of glucagon-like peptide (GLP)-1 (7-36) amide by ectopeptidases in RINm5F cells. Peptides 18:625-632
    • (1997) Peptides , vol.18 , pp. 625-632
    • Hupe-Sodmann, K.1    Goke, R.2    Goke, B.3
  • 40
    • 0028922909 scopus 로고
    • Trout and chicken proglucagon: Alternative splicing generates mRNA transcripts encoding glucagon-like peptide 2
    • Irwin DM, Wong J (1995) Trout and chicken proglucagon: alternative splicing generates mRNA transcripts encoding glucagon-like peptide 2. Mol Endocrinol 9:267-277
    • (1995) Mol Endocrinol , vol.9 , pp. 267-277
    • Irwin, D.M.1    Wong, J.2
  • 41
    • 0346096721 scopus 로고    scopus 로고
    • Small-intestinal dysfunction accompanies the complex endocrinopathy of human proprotein convertase 1 deficiency
    • Jackson RS, Creemers JW, Farooqi IS et al (2003) Small-intestinal dysfunction accompanies the complex endocrinopathy of human proprotein convertase 1 deficiency. J Clin Invest 112:1550-1560
    • (2003) J Clin Invest , vol.112 , pp. 1550-1560
    • Jackson, R.S.1    Creemers, J.W.2    Farooqi, I.S.3
  • 42
    • 0023950336 scopus 로고
    • Distribution of glucagonlike peptide i (GLP-I), glucagon, and glicentin in the rat brain: An immunocytochemical study
    • Jin SL, Han VK, Simmons JG et al (1988) Distribution of glucagonlike peptide I (GLP-I), 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.1    Han, V.K.2    Simmons, J.G.3
  • 43
    • 47849093381 scopus 로고    scopus 로고
    • Mechanisms underlying proglucagon gene expression
    • Jin T (2008) Mechanisms underlying proglucagon gene expression. J Endocrinol 198:17-28
    • (2008) J Endocrinol , vol.198 , pp. 17-28
    • Jin, T.1
  • 44
    • 0023214460 scopus 로고
    • Immunohistochemical localization of glucagon-like peptide 1. Use of poly- and monoclonal antibodies
    • Kauth T, Metz J (1987) Immunohistochemical localization of glucagon-like peptide 1. Use of poly- and monoclonal antibodies. Histochemistry 86:509-515
    • (1987) Histochemistry , vol.86 , pp. 509-515
    • Kauth, T.1    Metz, J.2
  • 45
    • 0033304603 scopus 로고    scopus 로고
    • The glucagon-like peptides
    • Kieffer TJ, 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
  • 46
    • 0016716546 scopus 로고
    • Identification of cells with pancreatic-type and guttype glucagon immunoreactivity in the human colon
    • Knudsen JB, Holst JJ, Asnaes S et al (1975) Identification of cells with pancreatic-type and guttype glucagon immunoreactivity in the human colon. Acta Pathol Microbiol Scand [A] 83:741-743
    • (1975) Acta Pathol Microbiol Scand [A] , vol.83 , pp. 741-743
    • Knudsen, J.B.1    Holst, J.J.2    Asnaes, S.3
  • 47
    • 0030607672 scopus 로고    scopus 로고
    • Glucagon-like peptide-1-( 9-36) amide is a major metabolite of glucagon-like peptide-1-(7-36) amide after in vivo administration to dogs, and it acts as an antagonist on the pancreatic receptor
    • Knudsen LB, Pridal L (1996) Glucagon-like peptide-1-(9-36) amide is a major metabolite of glucagon-like peptide-1-(7-36) amide after in vivo administration to dogs, and it acts as an antagonist on the pancreatic receptor. Eur J Pharmacol 318:429-435
    • (1996) Eur J Pharmacol , vol.318 , pp. 429-435
    • Knudsen, L.B.1    Pridal, L.2
  • 48
    • 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 et al (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
  • 49
    • 0026658127 scopus 로고
    • Glucagon gene 5'-flanking sequences direct expression of simian virus 40 large T antigen to the intestine, producing carcinoma of the large bowel in transgenic mice
    • Lee YC, Asa SL, Drucker DJ (1992) Glucagon gene 5'-flanking sequences direct expression of simian virus 40 large T antigen to the intestine, producing carcinoma of the large bowel in transgenic mice. J Biol Chem 267:10705-10708
    • (1992) J Biol Chem , vol.267 , pp. 10705-10708
    • Lee, Y.C.1    Asa, S.L.2    Drucker, D.J.3
  • 50
    • 0019276946 scopus 로고
    • Neurotransmitters and glucagon release from the isolated, perfused canine stomach
    • Lefebvre PJ, Luyckx AS (1980) Neurotransmitters and glucagon release from the isolated, perfused canine stomach. Diabetes 29:697-701
    • (1980) Diabetes , vol.29 , pp. 697-701
    • Lefebvre, P.J.1    Luyckx, A.S.2
  • 51
    • 33646182645 scopus 로고    scopus 로고
    • Glucagon-like peptide-1 receptor and proglucagon expression in mouse skin
    • List JF, He H, Habener JF (2006) Glucagon-like peptide-1 receptor and proglucagon expression in mouse skin. Regul Pept 134:149-157
    • (2006) Regul Pept , vol.134 , pp. 149-157
    • List, J.F.1    He, H.2    Habener, J.F.3
  • 52
    • 0021032599 scopus 로고
    • Mammalian pancreatic preproglucagon contains three glucagon- related peptides
    • Lopez LC, Frazier ML, Su CJ et al (1983) Mammalian pancreatic preproglucagon contains three glucagon- related peptides. Proc Natl Acad Sci USA 80:5485-5489
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 5485-5489
    • Lopez, L.C.1    Frazier, M.L.2    Su, C.J.3
  • 53
    • 33746076698 scopus 로고    scopus 로고
    • Role of the exchange protein directly activated by cyclic adenosine 5'-monophosphate (Epac) pathway in regulating proglucagon gene expression in intestinal endocrine L cells
    • Lotfi S, Li Z, Sun J et al (2006) Role of the exchange protein directly activated by cyclic adenosine 5'-monophosphate (Epac) pathway in regulating proglucagon gene expression in intestinal endocrine L cells. Endocrinology 147:3727-3736
    • (2006) Endocrinology , vol.147 , pp. 3727-3736
    • Lotfi, S.1    Li, Z.2    Sun, J.3
  • 54
    • 0020026919 scopus 로고
    • Pancreatic preproglucagon cDNA contains two glucagonrelated coding sequences arranged in tandem
    • Lund PK, Goodman RH, Dee PC et al (1982) Pancreatic preproglucagon cDNA contains two glucagonrelated 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
  • 55
    • 19944427738 scopus 로고    scopus 로고
    • Glucagon stimulates exocytosis in mouse and rat pancreatic alpha-cells by binding to glucagon receptors
    • Ma X, Zhang Y, Gromada J et al (2005) Glucagon stimulates exocytosis in mouse and rat pancreatic alpha-cells by binding to glucagon receptors. Mol Endocrinol 19:198-212
    • (2005) Mol Endocrinol , vol.19 , pp. 198-212
    • Ma, X.1    Zhang, Y.2    Gromada, J.3
  • 56
    • 17844404229 scopus 로고    scopus 로고
    • Basal receptor activation by locally produced glucagonlike peptide-1 contributes to maintaining beta-cell function
    • Masur K, Tibaduiza EC, Chen C et al (2005) Basal receptor activation by locally produced glucagonlike peptide-1 contributes to maintaining beta-cell function. Mol Endocrinol 19:1373-1382
    • (2005) Mol Endocrinol , vol.19 , pp. 1373-1382
    • Masur, K.1    Tibaduiza, E.C.2    Chen, C.3
  • 57
    • 33845999607 scopus 로고    scopus 로고
    • FoxO1 is required for the regulation of preproglucagon gene expression by insulin in pancreatic alphaTC1-9 cells
    • McKinnon CM, Ravier MA, Rutter GA (2006) FoxO1 is required for the regulation of preproglucagon gene expression by insulin in pancreatic alphaTC1-9 cells. J Biol Chem 281:39358-39369
    • (2006) J Biol Chem , vol.281 , pp. 39358-39369
    • McKinnon, C.M.1    Ravier, M.A.2    Rutter, G.A.3
  • 58
    • 1442350411 scopus 로고    scopus 로고
    • Secretion, degradation, and elimination of glucagonlike peptide 1 and gastric inhibitory polypeptide in patients with chronic renal insufficiency and healthy control subjects
    • Meier JJ, Nauck MA, Kranz D et al (2004) Secretion, degradation, and elimination of glucagonlike peptide 1 and gastric inhibitory polypeptide in patients with chronic renal insufficiency and healthy control subjects. Diabetes 53:654-662
    • (2004) Diabetes , vol.53 , pp. 654-662
    • Meier, J.J.1    Nauck, M.A.2    Kranz, D.3
  • 59
    • 0023008693 scopus 로고
    • Preproglucagon gene expression in pancreas and intestine diversifies at the level of post-translational processing
    • Mojsov S, Heinrich G, Wilson IB et al (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
  • 60
    • 0023107555 scopus 로고
    • Insulinotropin: Glucagon-like peptide i (7-37) co-encoded in the glucagon gene is a potent stimulator of insulin release in the perfused rat pancreas
    • Mojsov S, Weir GC, Habener JF (1987) Insulinotropin: glucagon-like peptide I (7-37) co-encoded in the glucagon gene is a potent stimulator of insulin release in the perfused rat pancreas. J Clin Invest 79:616-619
    • (1987) J Clin Invest , vol.79 , pp. 616-619
    • Mojsov, S.1    Weir, G.C.2    Habener, J.F.3
  • 61
    • 0025343831 scopus 로고
    • Both amidated and nonamidated forms of glucagon-like peptide i are synthesized in the rat intestine and the pancreas
    • Mojsov S, Kopczynski MG, Habener JF (1990) Both amidated and nonamidated forms of glucagon-like peptide I are synthesized in the rat intestine and the pancreas. J Biol Chem 265:8001-8008
    • (1990) J Biol Chem , vol.265 , pp. 8001-8008
    • Mojsov, S.1    Kopczynski, M.G.2    Habener, J.F.3
  • 62
    • 0019379796 scopus 로고
    • Relationship of glicentin to proglucagon and glucagon in the porcine pancreas
    • Moody AJ, Holst JJ, Thim L et al (1981) Relationship of glicentin to proglucagon and glucagon in the porcine pancreas. Nature 289:514-516
    • (1981) Nature , vol.289 , pp. 514-516
    • Moody, A.J.1    Holst, J.J.2    Thim, L.3
  • 63
    • 0037784011 scopus 로고    scopus 로고
    • GLP-1 and GIP are colocalized in a subset of endocrine cells in the small intestine
    • Mortensen K, Christensen LL, Holst JJ et al (2003) GLP-1 and GIP are colocalized in a subset of endocrine cells in the small intestine. Regul Pept 114:189-196
    • (2003) Regul Pept , vol.114 , pp. 189-196
    • Mortensen, K.1    Christensen, L.L.2    Holst, J.J.3
  • 64
    • 0004981389 scopus 로고
    • Aqueous extracts of the pancreas. I. Influence on the carbohydrate metabolism of depancreatized animals
    • Murlin JR, Clough HD, Gibbs CBF et al (1923) Aqueous extracts of the pancreas. I. Influence on the carbohydrate metabolism of depancreatized animals. J Biol Chem 56:253-296
    • (1923) J Biol Chem , vol.56 , pp. 253-296
    • Murlin, J.R.1    Clough, H.D.2    Gibbs, C.B.F.3
  • 65
    • 0032698718 scopus 로고    scopus 로고
    • Divergent regulation of human and rat proglucagon gene promoters in vivo
    • Nian M, Drucker DJ, Irwin D (1999) Divergent regulation of human and rat proglucagon gene promoters in vivo. Am J Physiol 277:G829-G837
    • (1999) Am J Physiol , vol.277
    • Nian, M.1    Drucker, D.J.2    Irwin, D.3
  • 66
    • 0036084248 scopus 로고    scopus 로고
    • Human glucagon gene promoter sequences regulating tissuespecific versus nutrient-regulated gene expression
    • Nian M, Gu J, Irwin DM et al (2002) Human glucagon gene promoter sequences regulating tissuespecific versus nutrient-regulated gene expression. Am J Physiol Regul IntegrComp Physiol 282:R173-R183
    • (2002) Am J Physiol Regul IntegrComp Physiol , vol.282
    • Nian, M.1    Gu, J.2    Irwin, D.M.3
  • 67
    • 0034129091 scopus 로고    scopus 로고
    • Regulation of pancreatic PC1 and PC2 associated with increased glucagon-like peptide 1 in diabetic rats
    • Nie Y, Nakashima M, Brubaker PL et al (2000) Regulation of pancreatic PC1 and PC2 associated with increased glucagon-like peptide 1 in diabetic rats. J Clin Invest 105:955-965
    • (2000) J Clin Invest , vol.105 , pp. 955-965
    • Nie, Y.1    Nakashima, M.2    Brubaker, P.L.3
  • 68
    • 0023161473 scopus 로고
    • Identical mRNA for preproglucagon in pancreas and gut
    • Novak U, Wilks A, Buell G et al (1987) Identical mRNA for preproglucagon in pancreas and gut. Eur J Biochem 164:553-558
    • (1987) Eur J Biochem , vol.164 , pp. 553-558
    • Novak, U.1    Wilks, A.2    Buell, G.3
  • 69
    • 4243207903 scopus 로고
    • Glucagon- and glicentin-producing cells
    • Lefebvre PJ (ed), Springer, Berlin
    • Orci L, Bordi C, Unger RH et al (1983) Glucagon- and glicentin-producing cells. In: Lefebvre PJ (ed) Glucagon. Springer, Berlin
    • (1983) Glucagon
    • Orci, L.1    Bordi, C.2    Unger, R.H.3
  • 70
    • 0014226137 scopus 로고
    • Structural evidence for glucagon producing cells in the intestinal mucosa of the rat
    • Orci L, Pictet R, Forssmann WG et al (1968) Structural evidence for glucagon producing cells in the intestinal mucosa of the rat. Diabetologia 4:56-67
    • (1968) Diabetologia , vol.4 , pp. 56-67
    • Orci, L.1    Pictet, R.2    Forssmann, W.G.3
  • 71
    • 0024359370 scopus 로고
    • Complete sequences of glucagon-like peptide-1 from human and pig small intestine
    • Orskov C, Bersani M, Johnsen AH et al (1989) Complete sequences of glucagon-like peptide-1 from human and pig small intestine. J Biol Chem 264:12826-12829
    • (1989) J Biol Chem , vol.264 , pp. 12826-12829
    • Orskov, C.1    Bersani, M.2    Johnsen, A.H.3
  • 72
    • 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 et al (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
  • 73
    • 0023470507 scopus 로고
    • Pancreatic and intestinal processing of proglucagon in man
    • Orskov C, Holst JJ, Poulsen SS et al (1987) Pancreatic and intestinal processing of proglucagon in man. Diabetologia 30:874-881
    • (1987) Diabetologia , vol.30 , pp. 874-881
    • Orskov, C.1    Holst, J.J.2    Poulsen, S.S.3
  • 74
    • 0028281773 scopus 로고
    • Tissue and plasma concentrations of amidated and glycine- extended glucagon-like peptide i in humans
    • Orskov C, Rabenhoj L, Wettergren A et al (1994) Tissue and plasma concentrations of amidated and glycine- extended glucagon-like peptide I in humans. Diabetes 43:535-539
    • (1994) Diabetes , vol.43 , pp. 535-539
    • Orskov, C.1    Rabenhoj, L.2    Wettergren, A.3
  • 75
    • 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, 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
  • 76
    • 0019853170 scopus 로고
    • The major proglucagon fragment: An abundant islet protein and secretory product
    • Patzelt C, Schug G (1981) The major proglucagon fragment: an abundant islet protein and secretory product. FEBS Lett 129:127-130
    • (1981) FEBS Lett , vol.129 , pp. 127-130
    • Patzelt, C.1    Schug, G.2
  • 77
    • 38349193088 scopus 로고    scopus 로고
    • Porcine glucagon-like peptide-2: Structure, signaling, metabolism and effects
    • Pedersen NB, Hjollund KR, Johnsen AH et al (2008) Porcine glucagon-like peptide-2: structure, signaling, metabolism and effects. Regul Pept 146:310-320
    • (2008) Regul Pept , vol.146 , pp. 310-320
    • Pedersen, N.B.1    Hjollund, K.R.2    Johnsen, A.H.3
  • 78
    • 0025740672 scopus 로고
    • Insulin regulation of the glucagon gene is mediated by an insulin-responsive DNA element
    • Philippe J (1991) Insulin regulation of the glucagon gene is mediated by an insulin-responsive DNA element. Proc Natl Acad Sci USA 88:7224-7227
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 7224-7227
    • Philippe, J.1
  • 79
    • 67349102328 scopus 로고    scopus 로고
    • The T allele of rs7903146 TCF7L2 is associated with impaired insulinotropic action of incretin hormones, reduced 24 h profiles of plasma insulin and glucagon, and increased hepatic glucose production in young healthy men
    • Pilgaard K, Jensen CB, Schou JH et al (2009) The T allele of rs7903146 TCF7L2 is associated with impaired insulinotropic action of incretin hormones, reduced 24 h profiles of plasma insulin and glucagon, and increased hepatic glucose production in young healthy men. Diabetologia 52:1298-1307
    • (2009) Diabetologia , vol.52 , pp. 1298-1307
    • Pilgaard, K.1    Jensen, C.B.2    Schou, J.H.3
  • 80
    • 24944436267 scopus 로고    scopus 로고
    • Neutral endopeptidase 24.11 and dipeptidyl peptidase IV are both mediators of the degradation of glucagon-like peptide 1 in the anaesthetised pig
    • Plamboeck A, Holst JJ, Carr RD et al (2005) Neutral endopeptidase 24.11 and dipeptidyl peptidase IV are both mediators of the degradation of glucagon-like peptide 1 in the anaesthetised pig. Diabetologia 48:1882-1890
    • (2005) Diabetologia , vol.48 , pp. 1882-1890
    • Plamboeck, A.1    Holst, J.J.2    Carr, R.D.3
  • 81
    • 0031455165 scopus 로고    scopus 로고
    • Role of the prohormone convertase PC3 in the processing of proglucagon to glucagon-like peptide 1
    • Rouille Y, Kantengwa S, Irminger JC et al (1997) Role of the prohormone convertase PC3 in the processing of proglucagon to glucagon-like peptide 1. J Biol Chem 272:32810-32816
    • (1997) J Biol Chem , vol.272 , pp. 32810-32816
    • Rouille, Y.1    Kantengwa, S.2    Irminger, J.C.3
  • 82
    • 0028294866 scopus 로고
    • Proglucagon is processed to glucagon by prohormone convertase PC2 in alpha TC1-6 cells
    • Rouille Y, Westermark G, Martin SK et al (1994) Proglucagon is processed to glucagon by prohormone convertase PC2 in alpha TC1-6 cells. Proc Natl Acad Sci USA 91:3242-3246
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 3242-3246
    • Rouille, Y.1    Westermark, G.2    Martin, S.K.3
  • 83
    • 35848942800 scopus 로고    scopus 로고
    • Impaired glucagon-like peptide-1-induced insulin secretion in carriers of transcription factor 7-like 2 (TCF7L2) gene polymorphisms
    • Schafer SA, Tschritter O, Machicao F et al (2007) Impaired glucagon-like peptide-1-induced insulin secretion in carriers of transcription factor 7-like 2 (TCF7L2) gene polymorphisms. Diabetologia 50:2443-2450
    • (2007) Diabetologia , vol.50 , pp. 2443-2450
    • Schafer, S.A.1    Tschritter, O.2    MacHicao, F.3
  • 84
    • 14844324460 scopus 로고    scopus 로고
    • Protein kinase B activity is sufficient to mimic the effect of insulin on glucagon gene transcription
    • Schinner S, Barthel A, Dellas C et al (2005) Protein kinase B activity is sufficient to mimic the effect of insulin on glucagon gene transcription. J Biol Chem 280:7369-7376
    • (2005) J Biol Chem , vol.280 , pp. 7369-7376
    • Schinner, S.1    Barthel, A.2    Dellas, C.3
  • 85
    • 0033857422 scopus 로고    scopus 로고
    • Elimination of glucagon-like peptide 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 et al (2000) Elimination of glucagon-like peptide 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
  • 86
    • 67249096093 scopus 로고    scopus 로고
    • Decreased TCF7L2 protein levels in type 2 diabetes mellitus correlate with downregulation of GIP- and GLP-1 receptors and impaired beta-cell function
    • Shu L, Matveyenko AV, Kerr-Conte J et al (2009) Decreased TCF7L2 protein levels in type 2 diabetes mellitus correlate with downregulation of GIP- and GLP-1 receptors and impaired beta-cell function. Hum Mol Genet 18:2388-2399
    • (2009) Hum Mol Genet , vol.18 , pp. 2388-2399
    • Shu, L.1    Matveyenko, A.V.2    Kerr-Conte, J.3
  • 87
    • 0017168179 scopus 로고
    • Purification and characterization of a protein from porcine gut with glucagon-like immunoreactivity
    • Sundby F, Jacobsen H, Moody AJ (1976) Purification and characterization of a protein from porcine gut with glucagon-like immunoreactivity. Horm Metab Res 8:366-371
    • (1976) Horm Metab Res , vol.8 , pp. 366-371
    • Sundby, F.1    Jacobsen, H.2    Moody, A.J.3
  • 88
    • 0017369322 scopus 로고
    • Ultrastructural identification of cells storing pancreatictype glucagon in dog stomach
    • Sundler F, Alumets J, Holst J et al (1976) Ultrastructural identification of cells storing pancreatictype glucagon in dog stomach. Histochemistry 50:33-37
    • (1976) Histochemistry , vol.50 , pp. 33-37
    • Sundler, F.1    Alumets, J.2    Holst, J.3
  • 89
    • 84957890116 scopus 로고
    • Origin and distribution of the hyperglycemic-glycogenolytic factor of the pancreas
    • Sutherland EW, De Duve C (1948) Origin and distribution of the hyperglycemic-glycogenolytic factor of the pancreas. J Biol Chem 175:663-674
    • (1948) J Biol Chem , vol.175 , pp. 663-674
    • Sutherland, E.W.1    De Duve, C.2
  • 90
    • 0019804078 scopus 로고
    • The amino acid sequence of porcine glicentin
    • Thim L, Moody AJ (1981) The amino acid sequence of porcine glicentin. Peptides 2(Suppl 2):37-39
    • (1981) Peptides , vol.2 , Issue.SUPPL. 2 , pp. 37-39
    • Thim, L.1    Moody, A.J.2
  • 91
    • 0020318408 scopus 로고
    • Purification and chemical characterization of a glicentin- related pancreatic peptide (proglucagon fragment) from porcine pancreas
    • Thim L, Moody AJ (1982) Purification and chemical characterization of a glicentin- related pancreatic peptide (proglucagon fragment) from porcine pancreas. Biochim Biophys Acta 703:134-141
    • (1982) Biochim Biophys Acta , vol.703 , pp. 134-141
    • Thim, L.1    Moody, A.J.2
  • 92
    • 4143138571 scopus 로고    scopus 로고
    • Neutral endopeptidase 24.11 is important for the degradation of both endogenous and exogenous glucagon in anesthetized pigs
    • Trebbien R, Klarskov L, Olesen M et al (2004) Neutral endopeptidase 24.11 is important for the degradation of both endogenous and exogenous glucagon in anesthetized pigs. Am J Physiol Endocrinol Metab 287:E431-E438
    • (2004) Am J Physiol Endocrinol Metab , vol.287
    • Trebbien, R.1    Klarskov, L.2    Olesen, M.3
  • 93
    • 0037312830 scopus 로고    scopus 로고
    • Pax-6 activates endogenous proglucagon gene expression in the rodent gastrointestinal epithelium
    • Trinh DK, Zhang K, Hossain M et al (2003) Pax-6 activates endogenous proglucagon gene expression in the rodent gastrointestinal epithelium. Diabetes 52:425-433
    • (2003) Diabetes , vol.52 , pp. 425-433
    • Trinh, D.K.1    Zhang, K.2    Hossain, M.3
  • 94
    • 1442274636 scopus 로고    scopus 로고
    • Impaired intestinal proglucagon processing in mice lacking prohormone convertase 1
    • Ugleholdt R, Zhu X, Deacon CF et al (2004) Impaired intestinal proglucagon processing in mice lacking prohormone convertase 1. Endocrinology 145:1349-1355
    • (2004) Endocrinology , vol.145 , pp. 1349-1355
    • Ugleholdt, R.1    Zhu, X.2    Deacon, C.F.3
  • 95
    • 0000847723 scopus 로고
    • Glucagon antibodies and an immunoassay for glucagon
    • Unger RH, Eisentraut AM, McCall RH et al (1961) Glucagon antibodies and an immunoassay for glucagon. J Clin Invest 40:1280-1289
    • (1961) J Clin Invest , vol.40 , pp. 1280-1289
    • Unger, R.H.1    Eisentraut, A.M.2    McCall, R.H.3
  • 96
    • 0013962416 scopus 로고
    • Distribution of immunoassayable glucagon in gastrointestinal tissues
    • Unger RH, Ketterer H, Eisentraut AM (1966) Distribution of immunoassayable glucagon in gastrointestinal tissues. Metabolism 15:865-867
    • (1966) Metabolism , vol.15 , pp. 865-867
    • Unger, R.H.1    Ketterer, H.2    Eisentraut, A.M.3
  • 97
    • 0014242412 scopus 로고
    • Characterization of the responses of circulating glucagon-like immunoreactivity to intraduodenal and intravenous administration of glucose
    • Unger RH, Ohneda A, Valverde I et al (1968) Characterization of the responses of circulating glucagon-like immunoreactivity to intraduodenal and intravenous administration of glucose. J Clin Invest 47:48-65
    • (1968) J Clin Invest , vol.47 , pp. 48-65
    • Unger, R.H.1    Ohneda, A.2    Valverde, I.3
  • 98
    • 0014299659 scopus 로고
    • Demonstration and characterization of a second fraction of glucagon- like immunoreactivity in jejunal extracts
    • Valverde I, Rigopoulou D, Exton J et al (1968) Demonstration and characterization of a second fraction of glucagon- like immunoreactivity in jejunal extracts. Am J Med Sci 255:415-420
    • (1968) Am J Med Sci , vol.255 , pp. 415-420
    • Valverde, I.1    Rigopoulou, D.2    Exton, J.3
  • 99
    • 0021849270 scopus 로고
    • Localization of glucagon-like peptide (GLP) immunoreactants in human gut and pancreas using light and electron microscopic immunocytochemistry
    • Varndell IM, Bishop AE, Sikri KL et al (1985) Localization of glucagon-like peptide (GLP) immunoreactants in human gut and pancreas using light and electron microscopic immunocytochemistry. J Histochem Cytochem 33:1080-1086
    • (1985) J Histochem Cytochem , vol.33 , pp. 1080-1086
    • Varndell, I.M.1    Bishop, A.E.2    Sikri, K.L.3
  • 100
    • 0037241085 scopus 로고    scopus 로고
    • Similar elimination rates of glucagon-like peptide-1 in obese type 2 diabetic patients and healthy subjects
    • Vilsboll T, Agerso H, Krarup T et al (2003) Similar elimination rates of glucagon-like peptide-1 in obese type 2 diabetic patients and healthy subjects. J Clin Endocrinol Metab 88:220-224
    • (2003) J Clin Endocrinol Metab , vol.88 , pp. 220-224
    • Vilsboll, T.1    Agerso, H.2    Krarup, T.3
  • 102
    • 0001095690 scopus 로고    scopus 로고
    • Reduced concentrations of intact and total GIP and GLP-1 in type 2 diabetic patients
    • Vilsbøll T, Krarup T, Deacon CD, Madsbad S, Holst JJ (2001) Reduced concentrations of intact and total GIP and GLP-1 in type 2 diabetic patients. Diabetes 50:609-613
    • (2001) Diabetes , vol.50 , pp. 609-613
    • Vilsbøll, T.1    Krarup, T.2    Deacon, C.D.3    Madsbad, S.4    Holst, J.J.5
  • 103
    • 0032538344 scopus 로고    scopus 로고
    • Amidated and non-amidated glucagonlike peptide-1 (GLP-1): Non-pancreatic effects (cephalic phase acid secretion) and stability in plasma in humans
    • Wettergren A, Pridal L, Wojdemann M, Holst JJ (1998) Amidated and non-amidated glucagonlike peptide-1 (GLP-1): non-pancreatic effects (cephalic phase acid secretion) and stability in plasma in humans. Regul Pept 77:83-87
    • (1998) Regul Pept , vol.77 , pp. 83-87
    • Wettergren, A.1    Pridal, L.2    Wojdemann, M.3    Holst, J.J.4
  • 104
    • 33748603481 scopus 로고    scopus 로고
    • Improving function and survival of pancreatic islets by endogenous production of glucagon-like peptide 1 (GLP-1)
    • Wideman RD, Yu IL, Webber TD et al (2006) Improving function and survival of pancreatic islets by endogenous production of glucagon-like peptide 1 (GLP-1). Proc Natl Acad Sci USA 103: 13468-13473
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 13468-13473
    • Wideman, R.D.1    Yu, I.L.2    Webber, T.D.3
  • 105
    • 0036269003 scopus 로고    scopus 로고
    • Expression pattern of IAPP and prohormone convertase 1/3 reveals a distinctive set of endocrine cells in the embryonic pancreas
    • Wilson ME, Kalamaras JA, German MS (2002) Expression pattern of IAPP and prohormone convertase 1/3 reveals a distinctive set of endocrine cells in the embryonic pancreas. Mech Dev 115:171-176
    • (2002) Mech Dev , vol.115 , pp. 171-176
    • Wilson, M.E.1    Kalamaras, J.A.2    German, M.S.3
  • 106
    • 12544254474 scopus 로고    scopus 로고
    • TCF-4 mediates cell type-specific regulation of proglucagon gene expression by beta-catenin and glycogen synthase kinase-3beta
    • Yi F, Brubaker PL, Jin T (2005) TCF-4 mediates cell type-specific regulation of proglucagon gene expression by beta-catenin and glycogen synthase kinase-3beta. J Biol Chem 280:1457-1464
    • (2005) J Biol Chem , vol.280 , pp. 1457-1464
    • Yi, F.1    Brubaker, P.L.2    Jin, T.3
  • 107
    • 31844433106 scopus 로고    scopus 로고
    • The metabolite generated by dipeptidyl-peptidase 4 metabolism of glucagon-like peptide-1 has no influence on plasma glucose levels in patients with type 2 diabetes
    • Zander M, Madsbad S, Deacon CF et al (2006) The metabolite generated by dipeptidyl-peptidase 4 metabolism of glucagon-like peptide-1 has no influence on plasma glucose levels in patients with type 2 diabetes. Diabetologia 49:369-374
    • (2006) Diabetologia , vol.49 , pp. 369-374
    • Zander, M.1    Madsbad, S.2    Deacon, C.F.3
  • 108
    • 33645413882 scopus 로고    scopus 로고
    • Intron 1 sequences are required for pancreatic expression of the human proglucagon gene
    • Zhou L, Nian M, Gu J et al (2006) Intron 1 sequences are required for pancreatic expression of the human proglucagon gene. Am J Physiol Regul Integr Comp Physiol 290:R634-R641
    • (2006) Am J Physiol Regul Integr Comp Physiol , vol.290
    • Zhou, L.1    Nian, M.2    Gu, J.3
  • 109
    • 0036679173 scopus 로고    scopus 로고
    • Disruption of PC1/3 expression in mice causes dwarfism and multiple neuroendocrine peptide processing defects
    • Zhu X, Zhou A, Dey A et al (2002) Disruption of PC1/3 expression in mice causes dwarfism and multiple neuroendocrine peptide processing defects. Proc Natl Acad Sci USA 99:10293-10298
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 10293-10298
    • Zhu, X.1    Zhou, A.2    Dey, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.