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Volumn 84, Issue C, 2010, Pages 1-20

Evolution of Genes for Incretin Hormones and their Receptors

Author keywords

Adaptive evolution; Evolution; Glucagon like peptide 1 (GLP 1); Glucose dependent insulinotropic polypeptide (GIP); Phylogeny; Proglucagon; Receptors; Vertebrates

Indexed keywords

GASTRIC INHIBITORY POLYPEPTIDE; GLUCAGON LIKE PEPTIDE 1; GLUCAGON RECEPTOR;

EID: 78649347352     PISSN: 00836729     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-381517-0.00001-1     Document Type: Book
Times cited : (10)

References (80)
  • 1
    • 67349176115 scopus 로고    scopus 로고
    • Islet G protein-coupled receptors as potential targets for treatment of type 2 diabetes
    • Ahrén B. Islet G protein-coupled receptors as potential targets for treatment of type 2 diabetes. Nat. Rev. Drug Discov. 2009, 8:369-385.
    • (2009) Nat. Rev. Drug Discov. , vol.8 , pp. 369-385
    • Ahrén, B.1
  • 2
    • 54049145812 scopus 로고    scopus 로고
    • Accelerated evolution of small serum proteins (SSPs)-The PSP94 family proteins in a Japanese viper
    • Aoki N., Matsuo H., Deshimaru M., Terada S. Accelerated evolution of small serum proteins (SSPs)-The PSP94 family proteins in a Japanese viper. Gene 2008, 426:7-14.
    • (2008) Gene , vol.426 , pp. 7-14
    • Aoki, N.1    Matsuo, H.2    Deshimaru, M.3    Terada, S.4
  • 3
    • 75149143476 scopus 로고    scopus 로고
    • Glucagon-like peptide 1 and glucose-dependent insulinotropic polypeptide: New advances
    • Asmar M., Holst J.J. Glucagon-like peptide 1 and glucose-dependent insulinotropic polypeptide: New advances. Curr. Opin. Endocrinol. Diabetes Obes. 2010, 17:57-62.
    • (2010) Curr. Opin. Endocrinol. Diabetes Obes. , vol.17 , pp. 57-62
    • Asmar, M.1    Holst, J.J.2
  • 4
    • 34248223285 scopus 로고    scopus 로고
    • Biology of incretins: GLP-1 and GIP
    • Baggio L.L., Drucker D.J. Biology of incretins: GLP-1 and GIP. Gastroenterology 2007, 132:2131-2157.
    • (2007) Gastroenterology , vol.132 , pp. 2131-2157
    • Baggio, L.L.1    Drucker, D.J.2
  • 5
    • 34447325119 scopus 로고    scopus 로고
    • Pro-protein convertases in intermediary metabolism: Islet hormones, brain/gut hormones and integrated physiology
    • Bataille D. Pro-protein convertases in intermediary metabolism: Islet hormones, brain/gut hormones and integrated physiology. J. Mol. Med. 2007, 85:673-684.
    • (2007) J. Mol. Med. , vol.85 , pp. 673-684
    • Bataille, D.1
  • 8
    • 0031040794 scopus 로고    scopus 로고
    • Tissue-specific expression of unique mRNAs that encode proglucagon-derived peptides or exendin 4 in the lizard
    • Chen Y.E., Drucker D.J. Tissue-specific expression of unique mRNAs that encode proglucagon-derived peptides or exendin 4 in the lizard. J. Biol. Chem. 1997, 272:4108-4115.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4108-4115
    • Chen, Y.E.1    Drucker, D.J.2
  • 9
    • 33644531918 scopus 로고    scopus 로고
    • Isolation and cloning of exendin precursor cDNAs from single samples of venom from the Mexican beaded lizard (Heloderma horridum) and the Gila monster (Heloderma suspectum)
    • Chen T., Kwok H., Ivanyi C., Shaw C. Isolation and cloning of exendin precursor cDNAs from single samples of venom from the Mexican beaded lizard (Heloderma horridum) and the Gila monster (Heloderma suspectum). Toxicon 2006, 47:288-295.
    • (2006) Toxicon , vol.47 , pp. 288-295
    • Chen, T.1    Kwok, H.2    Ivanyi, C.3    Shaw, C.4
  • 10
    • 3042647279 scopus 로고    scopus 로고
    • Identification and characterization of a glucagon receptor from the goldfish Carassius auratus: Implications for the evolution of the ligand specificity of glucagon receptors in vertebrates
    • Chow B.K., Moon T.W., Hoo R.L., Yeung C.M., Müller M., Christos P.J., Mojsov S. Identification and characterization of a glucagon receptor from the goldfish Carassius auratus: Implications for the evolution of the ligand specificity of glucagon receptors in vertebrates. Endocrinology 2004, 145:3273-3288.
    • (2004) Endocrinology , vol.145 , pp. 3273-3288
    • Chow, B.K.1    Moon, T.W.2    Hoo, R.L.3    Yeung, C.M.4    Müller, M.5    Christos, P.J.6    Mojsov, S.7
  • 11
    • 7044239241 scopus 로고    scopus 로고
    • New insights into the evolution of the GRF superfamily based on sequence similarity between the locust APRPs and human GRF
    • Clynen E., De Loof A., Schoofs L. New insights into the evolution of the GRF superfamily based on sequence similarity between the locust APRPs and human GRF. Gen. Comp. Endocrinol. 2004, 39:173-178.
    • (2004) Gen. Comp. Endocrinol. , vol.39 , pp. 173-178
    • Clynen, E.1    De Loof, A.2    Schoofs, L.3
  • 12
    • 0031730458 scopus 로고    scopus 로고
    • Purification and characterization of insulin, glucagon, and two glucagon-like peptides with insulin-releasing activity from the pancreas of the toad, Bufo marinus
    • Conlon J.M., Abdel-Wahab Y.H., O'Harte F.P., Nielsen P.F., Whittaker J. Purification and characterization of insulin, glucagon, and two glucagon-like peptides with insulin-releasing activity from the pancreas of the toad, Bufo marinus. Endocrinology 1998, 139:3442-3448.
    • (1998) Endocrinology , vol.139 , pp. 3442-3448
    • Conlon, J.M.1    Abdel-Wahab, Y.H.2    O'Harte, F.P.3    Nielsen, P.F.4    Whittaker, J.5
  • 13
    • 33748504146 scopus 로고    scopus 로고
    • Major contributions of comparative endocrinology to the development and exploitation of the incretin concept
    • Conlon J.M., Patterson S., Flatt P.R. Major contributions of comparative endocrinology to the development and exploitation of the incretin concept. J. Exp. Zool. 2006, 305A:781-786.
    • (2006) J. Exp. Zool. , vol.305 A , pp. 781-786
    • Conlon, J.M.1    Patterson, S.2    Flatt, P.R.3
  • 14
    • 0036158954 scopus 로고    scopus 로고
    • Biological actions and therapeutic potential of the glucagon-like peptides
    • Drucker D.J. Biological actions and therapeutic potential of the glucagon-like peptides. Gastroenterology 2002, 122:531-544.
    • (2002) Gastroenterology , vol.122 , pp. 531-544
    • Drucker, D.J.1
  • 15
    • 12344320974 scopus 로고    scopus 로고
    • Glucagon gene expression
    • Academic Press, San Diego, H.L. Henry, A.W. Norman (Eds.)
    • Drucker D.J. Glucagon gene expression. Encyclopaedia of Hormones 2003, 47-55. Academic Press, San Diego. H.L. Henry, A.W. Norman (Eds.).
    • (2003) Encyclopaedia of Hormones , pp. 47-55
    • Drucker, D.J.1
  • 16
    • 77956861832 scopus 로고
    • Molecular aspects of pancreatic peptides
    • Academic Press, San Diego
    • Dugay S.J., Mommsen T.P. Molecular aspects of pancreatic peptides. Fish Physiology 1994, Vol. 13:225-271. Academic Press, San Diego.
    • (1994) Fish Physiology , vol.13 , pp. 225-271
    • Dugay, S.J.1    Mommsen, T.P.2
  • 17
    • 0025242054 scopus 로고
    • Purification and structure of exendin-3, a new pancreatic secretagogue isolated from Heloderma horridum venom
    • Eng J., Andrews P.C., Kleinman W.A., Singh L., Raufman J.P. Purification and structure of exendin-3, a new pancreatic secretagogue isolated from Heloderma horridum venom. J. Biol. Chem. 1990, 265:20259-20262.
    • (1990) J. Biol. Chem. , vol.265 , pp. 20259-20262
    • Eng, J.1    Andrews, P.C.2    Kleinman, W.A.3    Singh, L.4    Raufman, J.P.5
  • 18
    • 0026648961 scopus 로고
    • Isolation and characterization of exendin-4, an exendin-3 analogue, from Heloderma suspectum venom. Further evidence for an exendin receptor on dispersed acini from guinea pig pancreas
    • Eng J., Kleinman W.A., Singh L., Singh G., Raufman J.P. Isolation and characterization of exendin-4, an exendin-3 analogue, from Heloderma suspectum venom. Further evidence for an exendin receptor on dispersed acini from guinea pig pancreas. J. Biol. Chem. 1992, 267:7402-7405.
    • (1992) J. Biol. Chem. , vol.267 , pp. 7402-7405
    • Eng, J.1    Kleinman, W.A.2    Singh, L.3    Singh, G.4    Raufman, J.P.5
  • 19
    • 0038024615 scopus 로고    scopus 로고
    • The G-protein-coupled receptors in the human genome form five main families. Phylogenetic analysis, paralogon groups, and fingerprints
    • Fredriksson F., Lagerström M.C., Lundin L.-G., Schiöth H.B. The G-protein-coupled receptors in the human genome form five main families. Phylogenetic analysis, paralogon groups, and fingerprints. Mol. Pharmacol. 2003, 63:1256-1272.
    • (2003) Mol. Pharmacol. , vol.63 , pp. 1256-1272
    • Fredriksson, F.1    Lagerström, M.C.2    Lundin, L.-G.3    Schiöth, H.B.4
  • 22
    • 40949162025 scopus 로고    scopus 로고
    • Rapid evolution by positive selection and gene gain and loss: PLA(2) venom genes in closely related Sistrurus rattlesnakes with divergent diets
    • Gibbs H.L., Rossiter W. Rapid evolution by positive selection and gene gain and loss: PLA(2) venom genes in closely related Sistrurus rattlesnakes with divergent diets. J. Mol. Evol. 2008, 66:151-166.
    • (2008) J. Mol. Evol. , vol.66 , pp. 151-166
    • Gibbs, H.L.1    Rossiter, W.2
  • 23
    • 0035716295 scopus 로고    scopus 로고
    • Family-B G-protein coupled receptors
    • Harmar A.J. Family-B G-protein coupled receptors. Genome Biol. 2001, 2:3013.1-3013.10.
    • (2001) Genome Biol. , vol.2
    • Harmar, A.J.1
  • 24
    • 35748957503 scopus 로고    scopus 로고
    • The physiology of glucagon-like peptide 1
    • Holst J.J. The physiology of glucagon-like peptide 1. Physiol. Rev. 2007, 87:1409-1439.
    • (2007) Physiol. Rev. , vol.87 , pp. 1409-1439
    • Holst, J.J.1
  • 25
    • 0032472216 scopus 로고    scopus 로고
    • Neuropeptide families: Evolutionary perspective
    • Hoyle C.H.V. Neuropeptide families: Evolutionary perspective. Regul. Pept. 1998, 73:1-33.
    • (1998) Regul. Pept. , vol.73 , pp. 1-33
    • Hoyle, C.H.V.1
  • 26
    • 0033405532 scopus 로고    scopus 로고
    • Neuropeptide families and their receptors: Evolutionary perspectives
    • Hoyle H.H. Neuropeptide families and their receptors: Evolutionary perspectives. Brian Res. 1999, 848:1-25.
    • (1999) Brian Res. , vol.848 , pp. 1-25
    • Hoyle, H.H.1
  • 27
    • 0035795227 scopus 로고    scopus 로고
    • Molecular evolution of proglucagon
    • Irwin D.M. Molecular evolution of proglucagon. Regul. Pept. 2001, 98:1-12.
    • (2001) Regul. Pept. , vol.98 , pp. 1-12
    • Irwin, D.M.1
  • 28
    • 0035700587 scopus 로고    scopus 로고
    • CDNA cloning of proglucagon from the stomach and pancreas of the dog
    • Irwin D.M. cDNA cloning of proglucagon from the stomach and pancreas of the dog. DNA Seq. 2001, 12:253-260.
    • (2001) DNA Seq. , vol.12 , pp. 253-260
    • Irwin, D.M.1
  • 29
    • 0036247428 scopus 로고    scopus 로고
    • Ancient duplications of the human proglucagon gene
    • Irwin D.M. Ancient duplications of the human proglucagon gene. Genomics 2002, 79:741-746.
    • (2002) Genomics , vol.79 , pp. 741-746
    • Irwin, D.M.1
  • 30
    • 21444451573 scopus 로고    scopus 로고
    • Evolution of hormone function: Proglucagon-derived peptides and their receptors
    • Irwin D.M. Evolution of hormone function: Proglucagon-derived peptides and their receptors. Bioscience 2005, 55:583-591.
    • (2005) Bioscience , vol.55 , pp. 583-591
    • Irwin, D.M.1
  • 31
    • 67349171365 scopus 로고    scopus 로고
    • Molecular evolution of mammalian incretin hormone genes
    • Irwin D.M. Molecular evolution of mammalian incretin hormone genes. Regul. Pept. 2009, 155:121-130.
    • (2009) Regul. Pept. , vol.155 , pp. 121-130
    • Irwin, D.M.1
  • 32
    • 0034712819 scopus 로고    scopus 로고
    • Proglucagon cDNAs from the leopard frog, Rana pipiens, encode two GLP-1-like peptides
    • Irwin D.M., Sivarajah P. Proglucagon cDNAs from the leopard frog, Rana pipiens, encode two GLP-1-like peptides. Mol. Cell. Endocrinol. 2000, 162:17-24.
    • (2000) Mol. Cell. Endocrinol. , vol.162 , pp. 17-24
    • Irwin, D.M.1    Sivarajah, P.2
  • 33
    • 0028922909 scopus 로고
    • Trout and chicken proglucagon: Alternative splicing generates mRNA transcripts encoding glucagon-like peptide 2
    • Irwin D.M., Wong J. Trout and chicken proglucagon: Alternative splicing generates mRNA transcripts encoding glucagon-like peptide 2. Mol. Endocrinol. 1995, 9:267-277.
    • (1995) Mol. Endocrinol. , vol.9 , pp. 267-277
    • Irwin, D.M.1    Wong, J.2
  • 34
    • 15944427534 scopus 로고    scopus 로고
    • Evolution of new hormone function: Loss and gain of a receptor
    • Irwin D.M., Wong K. Evolution of new hormone function: Loss and gain of a receptor. J. Hered. 2005, 96:205-211.
    • (2005) J. Hered. , vol.96 , pp. 205-211
    • Irwin, D.M.1    Wong, K.2
  • 35
    • 33751321379 scopus 로고    scopus 로고
    • Evolution of the vertebrate glucose-dependent insulinotropic polypeptide (GIP) gene
    • Irwin D.M., Zhang T. Evolution of the vertebrate glucose-dependent insulinotropic polypeptide (GIP) gene. Comp. Biochem. Physiol. 2006, 1D:385-395.
    • (2006) Comp. Biochem. Physiol. , vol.1 D , pp. 385-395
    • Irwin, D.M.1    Zhang, T.2
  • 37
    • 0032755756 scopus 로고    scopus 로고
    • Lamprey proglucagon and the origin of glucagon-like peptides
    • Irwin D.M., Huner O., Youson J.H. Lamprey proglucagon and the origin of glucagon-like peptides. Mol. Biol. Evol. 1999, 16:1548-1557.
    • (1999) Mol. Biol. Evol. , vol.16 , pp. 1548-1557
    • Irwin, D.M.1    Huner, O.2    Youson, J.H.3
  • 38
    • 67650650957 scopus 로고    scopus 로고
    • The repertoire of G-protein-coupled receptors in Xenopus tropicalis
    • Ji Y., Zhang Z., Hu Y. The repertoire of G-protein-coupled receptors in Xenopus tropicalis. BMC Genomics 2009, 10:263.
    • (2009) BMC Genomics , vol.10 , pp. 263
    • Ji, Y.1    Zhang, Z.2    Hu, Y.3
  • 39
    • 0037376913 scopus 로고    scopus 로고
    • Glucagon and regulation of glucose metabolism
    • Jiang G., Zhang B.B. Glucagon and regulation of glucose metabolism. Am. J. Physiol. 2003, 284:E671-E678.
    • (2003) Am. J. Physiol. , vol.284
    • Jiang, G.1    Zhang, B.B.2
  • 40
    • 47849093381 scopus 로고    scopus 로고
    • Mechanisms underlying proglucagon gene expression
    • Jin T. Mechanisms underlying proglucagon gene expression. J. Endocrinol. 2008, 198:17-28.
    • (2008) J. Endocrinol. , vol.198 , pp. 17-28
    • Jin, T.1
  • 41
    • 0037283601 scopus 로고    scopus 로고
    • The relative contributions of insulin resistance and beta-cell dysfunction to the pathophysiology of type 2 diabetes
    • Kahn S.E. The relative contributions of insulin resistance and beta-cell dysfunction to the pathophysiology of type 2 diabetes. Diabetologia 2003, 26:3-19.
    • (2003) Diabetologia , vol.26 , pp. 3-19
    • Kahn, S.E.1
  • 42
  • 43
    • 0030482313 scopus 로고    scopus 로고
    • Receptors for VIP, PACAP, secretin, GRF, glucagon, GLP-1, and other members of their new family of G protein-linked receptors: Structure-function relationship with special reference to the human VIP-1 receptor
    • Laburthe M., Couvineau A., Gaudin P., Maoret J.J., Rouyer-Fessard C., Nicole P. Receptors for VIP, PACAP, secretin, GRF, glucagon, GLP-1, and other members of their new family of G protein-linked receptors: Structure-function relationship with special reference to the human VIP-1 receptor. Ann. NY Acad. Sci. 1996, 805:94-109.
    • (1996) Ann. NY Acad. Sci. , vol.805 , pp. 94-109
    • Laburthe, M.1    Couvineau, A.2    Gaudin, P.3    Maoret, J.J.4    Rouyer-Fessard, C.5    Nicole, P.6
  • 44
    • 0031029936 scopus 로고    scopus 로고
    • Distribution of glucagon-like peptide-1 and other preproglucagon-derived peptides in the rat hypothalamus and brainstem
    • Larsen P.J., Tang-Christensen M., Holst J.J., Ørskov C. Distribution of glucagon-like peptide-1 and other preproglucagon-derived peptides in the rat hypothalamus and brainstem. Neuroscience 1996, 77:257-270.
    • (1996) Neuroscience , vol.77 , pp. 257-270
    • Larsen, P.J.1    Tang-Christensen, M.2    Holst, J.J.3    Ørskov, C.4
  • 46
    • 67651173077 scopus 로고    scopus 로고
    • Incretin-based therapies for type 2 diabetes mellitus
    • Lovshin J.A., Drucker D.J. Incretin-based therapies for type 2 diabetes mellitus. Nat. Rev. Endocrinol. 2009, 5:262-269.
    • (2009) Nat. Rev. Endocrinol. , vol.5 , pp. 262-269
    • Lovshin, J.A.1    Drucker, D.J.2
  • 47
    • 0019576004 scopus 로고
    • Intestinal glucagon mRNA identified by hybridization to a cloned islet cDNA encoding a precursor
    • Lund P.K., Goodman R.H., Habener J.F. Intestinal glucagon mRNA identified by hybridization to a cloned islet cDNA encoding a precursor. Biochem. Biophys. Res. Commun. 1981, 100:1659-1666.
    • (1981) Biochem. Biophys. Res. Commun. , vol.100 , pp. 1659-1666
    • Lund, P.K.1    Goodman, R.H.2    Habener, J.F.3
  • 48
    • 0020026919 scopus 로고
    • Pancreatic preproglucagon cDNA contains two glucagon-related coding sequences arranged in tandem
    • Lund P.K., Goodman R.H., Dee P.C., Habener J.F. Pancreatic preproglucagon cDNA contains two glucagon-related coding sequences arranged in tandem. Proc. Natl Acad. Sci. 1982, 79:345-349.
    • (1982) Proc. Natl Acad. Sci. , vol.79 , pp. 345-349
    • Lund, P.K.1    Goodman, R.H.2    Dee, P.C.3    Habener, J.F.4
  • 49
    • 0020534249 scopus 로고
    • Anglerfish islet pre-proglucagon II. Nucleotide and corresponding amino acid sequence of the cDNA
    • Lund P.K., Goodman R.H., Montminy M.R., Dee P.C., Habener J.F. Anglerfish islet pre-proglucagon II. Nucleotide and corresponding amino acid sequence of the cDNA. J. Biol. Chem. 1983, 258:3280-3284.
    • (1983) J. Biol. Chem. , vol.258 , pp. 3280-3284
    • Lund, P.K.1    Goodman, R.H.2    Montminy, M.R.3    Dee, P.C.4    Habener, J.F.5
  • 52
    • 61349172037 scopus 로고    scopus 로고
    • Glucose-dependent insulinotropic polypeptide (Gastric inhibitory polypeptide; GIP)
    • McIntosh C.H.S., Widenmaier S., Kim S.-J. Glucose-dependent insulinotropic polypeptide (Gastric inhibitory polypeptide; GIP). Vitam. Horm. 2009, 80:409-471.
    • (2009) Vitam. Horm. , vol.80 , pp. 409-471
    • McIntosh, C.H.S.1    Widenmaier, S.2    Kim, S.-J.3
  • 53
    • 23044518919 scopus 로고    scopus 로고
    • Glucagon-like peptide-1 (GLP-1) and the control of glucose metabolism in mammals and fish
    • Mojsov S. Glucagon-like peptide-1 (GLP-1) and the control of glucose metabolism in mammals and fish. Am. Zool. 2000, 40:246-258.
    • (2000) Am. Zool. , vol.40 , pp. 246-258
    • Mojsov, S.1
  • 54
    • 0035876718 scopus 로고    scopus 로고
    • Amphibian glucagon family peptides: Potent metabolic regulators in fish hepatocytes
    • Mommsen T.P., Conlon J.M., Irwin D.M. Amphibian glucagon family peptides: Potent metabolic regulators in fish hepatocytes. Regul. Pept. 2001, 99:111-118.
    • (2001) Regul. Pept. , vol.99 , pp. 111-118
    • Mommsen, T.P.1    Conlon, J.M.2    Irwin, D.M.3
  • 55
    • 8444251815 scopus 로고    scopus 로고
    • Hormones and fish hepatocyte metabolism: "The good, the bad and the ugly!"
    • Moon T.W. Hormones and fish hepatocyte metabolism: "The good, the bad and the ugly!". Comp. Biochem. Physiol. 2004, 139B:335-345.
    • (2004) Comp. Biochem. Physiol. , vol.139 B , pp. 335-345
    • Moon, T.W.1
  • 57
    • 67049155251 scopus 로고    scopus 로고
    • Unraveling the science of incretin biology
    • Nauck M.A. Unraveling the science of incretin biology. Am. J. Med. 2009, 122:S3-S10.
    • (2009) Am. J. Med. , vol.122
    • Nauck, M.A.1
  • 58
    • 33746565564 scopus 로고    scopus 로고
    • Gastroenteropancreatic hormones and metabolism in fish
    • Nelson L.E., Sheridan M.A. Gastroenteropancreatic hormones and metabolism in fish. Gen. Comp. Endocrinol. 2006, 148:116-124.
    • (2006) Gen. Comp. Endocrinol. , vol.148 , pp. 116-124
    • Nelson, L.E.1    Sheridan, M.A.2
  • 59
    • 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 E.S., Chow L.S., Tse D.L., Du X., Wei Y., Mojsov S., Chow B.K. Functional studies of a glucagon receptor isolated from frog Rana tigrina rugulosa: Implications on the molecular evolution of glucagon receptors in vertebrates. FEBS Lett. 1999, 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
  • 60
    • 77953065317 scopus 로고    scopus 로고
    • Molecular mechanisms underlying Nutrient-stimulated incretin secretion
    • Parker H.E., Reimann F., Gribble F.M. Molecular mechanisms underlying Nutrient-stimulated incretin secretion. Expert Rev. Mol. Med. 2010, 12:e1.
    • (2010) Expert Rev. Mol. Med. , vol.12
    • Parker, H.E.1    Reimann, F.2    Gribble, F.M.3
  • 61
    • 0032540385 scopus 로고    scopus 로고
    • Molecular cloning of the helodermin and exendin-4 cDNAs in the lizard. Relationship to vasoactive intestinal polypeptide/pituitary adenylate cyclase activating polypeptide and glucagon-like peptide 1 and evidence against the existence of mammalian homologues
    • Pohl M., Wank S.A. Molecular cloning of the helodermin and exendin-4 cDNAs in the lizard. Relationship to vasoactive intestinal polypeptide/pituitary adenylate cyclase activating polypeptide and glucagon-like peptide 1 and evidence against the existence of mammalian homologues. J. Biol. Chem. 1998, 273:9778-9784.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9778-9784
    • Pohl, M.1    Wank, S.A.2
  • 62
    • 0030048156 scopus 로고    scopus 로고
    • Bioactive peptides from lizard venoms
    • Raufman J.P. Bioactive peptides from lizard venoms. Regul. Pept. 1996, 61:1-18.
    • (1996) Regul. Pept. , vol.61 , pp. 1-18
    • Raufman, J.P.1
  • 63
    • 0026795135 scopus 로고
    • Truncated glucagon-like peptide-1 interacts with exendin receptors on dispersed acini from guinea pig pancreas. Identification of a mammalian analogue of the reptilian peptide exendin-4
    • Raufman J.P., Singh L., Singh G., Eng J. Truncated glucagon-like peptide-1 interacts with exendin receptors on dispersed acini from guinea pig pancreas. Identification of a mammalian analogue of the reptilian peptide exendin-4. J. Biol. Chem. 1992, 267:21432-21437.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21432-21437
    • Raufman, J.P.1    Singh, L.2    Singh, G.3    Eng, J.4
  • 64
    • 40849139203 scopus 로고    scopus 로고
    • Expression of proglucagon and proglucagon-derived peptide hormone receptor genes in the chicken
    • Richards M.P., McMurtry J.P. Expression of proglucagon and proglucagon-derived peptide hormone receptor genes in the chicken. Gen. Comp. Endocrinol. 2008, 156:323-338.
    • (2008) Gen. Comp. Endocrinol. , vol.156 , pp. 323-338
    • Richards, M.P.1    McMurtry, J.P.2
  • 66
    • 60449090902 scopus 로고    scopus 로고
    • Hormones and receptors in fish: Do duplicates matter?
    • Roch G.J., Wu S., Sherwood N.M. Hormones and receptors in fish: Do duplicates matter?. Gen. Comp. Endocrinol. 2009, 161:3-12.
    • (2009) Gen. Comp. Endocrinol. , vol.161 , pp. 3-12
    • Roch, G.J.1    Wu, S.2    Sherwood, N.M.3
  • 67
    • 0035923717 scopus 로고    scopus 로고
    • Responses of python gastrointestinal regulatory peptides to feeding
    • Secor S.M., Fehsenfeld D., Diamond J., Adria T.E. Responses of python gastrointestinal regulatory peptides to feeding. Proc. Natl Acad. Sci. 2001, 98:13637-13642.
    • (2001) Proc. Natl Acad. Sci. , vol.98 , pp. 13637-13642
    • Secor, S.M.1    Fehsenfeld, D.2    Diamond, J.3    Adria, T.E.4
  • 69
    • 0027499820 scopus 로고
    • Origin of mammalian gonadotropin-releasing hormones
    • Sherwood N.M., Lovejoy D.A., Coe I.R. Origin of mammalian gonadotropin-releasing hormones. Endocr. Rev. 1993, 14:241-254.
    • (1993) Endocr. Rev. , vol.14 , pp. 241-254
    • Sherwood, N.M.1    Lovejoy, D.A.2    Coe, I.R.3
  • 70
    • 0034511574 scopus 로고    scopus 로고
    • The origin and function of the pituitary adenylate cyclase-activating polypeptide (PACAP)/Glucagon superfamily
    • Sherwood N.M., Krueckl S.L., McRory J.E. The origin and function of the pituitary adenylate cyclase-activating polypeptide (PACAP)/Glucagon superfamily. Endocr. Rev. 2000, 21:619-670.
    • (2000) Endocr. Rev. , vol.21 , pp. 619-670
    • Sherwood, N.M.1    Krueckl, S.L.2    McRory, J.E.3
  • 71
    • 26844577365 scopus 로고    scopus 로고
    • Proglucagon-derived peptides: Mechanisms of action and therapeutic potential
    • Sinclair E.M., Drucker D.J. Proglucagon-derived peptides: Mechanisms of action and therapeutic potential. Physiology 2005, 20:357-365.
    • (2005) Physiology , vol.20 , pp. 357-365
    • Sinclair, E.M.1    Drucker, D.J.2
  • 72
    • 0035096907 scopus 로고    scopus 로고
    • Evolution of receptors for proglucagon-derived peptides: Isolation of frog glucagon receptors
    • Sivarajah P., Wheeler M.B., Irwin D.M. Evolution of receptors for proglucagon-derived peptides: Isolation of frog glucagon receptors. Comp. Biochem. Physiol. 2001, 128B:517-527.
    • (2001) Comp. Biochem. Physiol. , vol.128 B , pp. 517-527
    • Sivarajah, P.1    Wheeler, M.B.2    Irwin, D.M.3
  • 73
    • 34548456352 scopus 로고    scopus 로고
    • PACAP-related peptide (PRP)-molecular evolution and potential functions
    • Tam J.K., Lee L.T., Chow B.K. PACAP-related peptide (PRP)-molecular evolution and potential functions. Peptides 2007, 28:1920-1929.
    • (2007) Peptides , vol.28 , pp. 1920-1929
    • Tam, J.K.1    Lee, L.T.2    Chow, B.K.3
  • 75
    • 68149161100 scopus 로고    scopus 로고
    • Mining incretin hormone pathways for novel therapies
    • Wideman R.D., Kieffer T.J. Mining incretin hormone pathways for novel therapies. Trends Endo. Metab. 2009, 20:280-286.
    • (2009) Trends Endo. Metab. , vol.20 , pp. 280-286
    • Wideman, R.D.1    Kieffer, T.J.2
  • 76
    • 0035169502 scopus 로고    scopus 로고
    • Identification of a proglucagon cDNA from Rana tigrina rugulosa that encodes two GLP-1s and that is alternatively spliced in a tissue-specific manner
    • Yeung C.M., Chow B.K. Identification of a proglucagon cDNA from Rana tigrina rugulosa that encodes two GLP-1s and that is alternatively spliced in a tissue-specific manner. Gen. Comp. Endocrinol. 2001, 124:144-151.
    • (2001) Gen. Comp. Endocrinol. , vol.124 , pp. 144-151
    • Yeung, C.M.1    Chow, B.K.2
  • 77
    • 0036892893 scopus 로고    scopus 로고
    • Isolation and structure-function studies of a glucagon-like peptide 1 receptor from goldfish Carassius auratus: Identification of three charged residues in extracellular domains critical for receptor function
    • Yeung C.M., Mojsov S., Mok P.Y., Chow B.K. Isolation and structure-function studies of a glucagon-like peptide 1 receptor from goldfish Carassius auratus: Identification of three charged residues in extracellular domains critical for receptor function. Endocrinology 2002, 143:4646-4654.
    • (2002) Endocrinology , vol.143 , pp. 4646-4654
    • Yeung, C.M.1    Mojsov, S.2    Mok, P.Y.3    Chow, B.K.4
  • 79
    • 12344338519 scopus 로고    scopus 로고
    • Structure and expression of the chicken proglucagon gene
    • Yue S., Irwin D.M. Structure and expression of the chicken proglucagon gene. Mol. Cell. Endocrinol. 2005, 230:69-76.
    • (2005) Mol. Cell. Endocrinol. , vol.230 , pp. 69-76
    • Yue, S.1    Irwin, D.M.2
  • 80
    • 1342342994 scopus 로고    scopus 로고
    • Fish proglucagon genes have differing coding potential
    • Zhou L., Irwin D.M. Fish proglucagon genes have differing coding potential. Comp. Biochem. Physiol. 2004, 137B:255-264.
    • (2004) Comp. Biochem. Physiol. , vol.137 B , pp. 255-264
    • Zhou, L.1    Irwin, D.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.