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Original Article

Gastrointestinal Endocrinology

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Pages 27-38 | Published online: 08 Jul 2009

References: General

  • Hess Thaysen E. Gastrointestinal hormones and other subjects. Alfred Benzon Publication I. Copenhagen: Munksgaard 1971; 1–306
  • Jorpes J E, Mutt V. Secretin, cholecystokinin, pancreozymin and gastrin. Handb Exp Pharmacol. Berlin, Springer Verlag 1973; 1–376
  • Erspamer V, Melchiorri P. Active polypeptides of the amphibian skin and their synthetic analogs. Pure App Chem 1973; 35: 463–94
  • Tatemoto K, Mutt V. Chemical determination of polypeptide hormones. Proc Natl Acad Sci USA 1978; 75: 4115–9
  • Schwartz T W. Molecular structure of G-protein coupled receptors. Textbook of receptor pharmacology, J C Foreman, T Johansen. Boca Raton, CRC Press 1995; 108–26
  • Bell G I, Santerre R F, Mullenbach G T. Hamster preproglucagon contains the sequence of glucagon and two related peptides. Nature 1983; 302: 716–8
  • Hvidberg A, Toft Nielsen M, Hilsted J, Ørskov C, Hoist J J. Effect of glucagon-like peptide-1 (proglucagon 78–107amide) on hepatic glucose production in healthy man. Metabolism 1994; 43: 104–8
  • Nauck M A, Heimesaat M, Ørskov C, Hoist J J, Ebert R, Creutzfeldt W. Preserved incretin activity of GLP-1 (7–36amide), but not of synthetic human GIP in patients with type 2-diabetes mellitus. J Clin Invest 1993; 91: 301–7
  • Nauck M A, Kleine N, Ørskov C, Hoist J J, Willms B, Creutzfeldt W. Normalization of fasting hyperglycemia by exogenous GLP-1 (7–36amide) in type-2 diabetic patients. Diabetologia 1993; 36: 741–4
  • Schwartz T W. Molecular structure of G-protein coupled receptors. Textbook of receptor pharmacology, J C Foreman, T Johansen. CRC Press, Boca Raton 1995; 108–26
  • Thorens B. Expression cloning of the pancreatic β-cell receptor for the gluco-incretin hormone glucagon-like peptide-1. Proc Natl Acad Sci USA 1992; 89: 8641–5
  • Rehfeld J F, Stadil F, Rubin B. Production and evaluation of antibodies for the radioimmunoassay of gastrin. Scand J Clin Lab Invest 1972; 30: 221–32
  • Stadil F, Rehfeld J F. Preparation of125I-synthetic human gastrin I for radioimmunoanalysis. Scand J Clin Lab Invest 1972; 30: 361–9
  • Rehfeld J F. Three components of gastrin in human serum. Biochim Biophys Acta 1972; 285: 364–72
  • Stadil F, Rehfeld J F. Determination of gastrin in serum. An evaluation of the reliability of a radioimmunoassay of gastrin. Scand J Gastroenterol 1973; 8: 101–13
  • Rehfeld J F. Localization of gastrin to neuro-and adenohypophysis. Nature 1978; 271: 771–3
  • Brand S J, Andersen B N, Rehfeld J F. Complete tyrosyl O-sulfation of gastrin in the neonatal pancreas. Nature 1984; 309: 456–8
  • Bardram L, Hilsted L, Rehfeld J F. Progastrin expression in the mammalian pancreas. Proc Natl Acad Sci USA 1990; 87: 298–302
  • Rehfeld J F, Johnsen A H. Identification of gastrin component I as gastrin-71, the largest possible bioactive progastrin product. Eur J Biochem 1994; 171: 139–42
  • Rehfeld J F, Hansen C P, Johnsen A H. Post(poly)Glu cleavage and degradation modified by O-sulphated tyrosine: a novel posttranslational processing mechanism. EMBO J 1995; 14: 389–96
  • Rehfeld J F, Solinge W W. The tumour biology of gastrin and cholecystokinin [review]. Adv Cancer Res 1994; 63: 295–346
  • Schaffalitzky de Muckadell O B, Fahrenkrug J. Radioimmunoassay of secretin in plasma. Scand J Clin lab Invest 1977; 37: 155–62
  • Schaffalitzky de Muckadell O B, Fahrenkrug J. Secretion pattern of secretin in man: regulation by gastric acid. Gut 1978; 19: 812–8
  • Schaffalitzky de Muckadell O B, Fahrenkrug J, Rune S J. Physiological significance of secretin in the pancreatic bicarbonate secretion. I. Responsiveness of the secretin-releasing system in the upper duodenum. Scand J Gastroenterol 1979; 14: 79–83
  • Schaffalitzky de Muckadell O B, Fahrenkrug J, Matzen P, Rune S J, Worning H. Physiological significance of secretin in the pancreatic bicarbonate secretion. II. Pancreatic bicarbonate response to a physiological increase in plasma secretin concentration. Scand J Gastroenterol 1979; 14: 85–90
  • Rehfeld J F. Immunochemical studies on cholecystokinin. I. Development of sequence-specific radioimmunoassays against porcine tritria contra peptide cholecystokinin. J Biol Chem 1978; 253: 4016–21
  • Rehfeld J F. Immunochemical studies on cholecystokinin. II. Distribution and molecular heterogeneity in the central nervous system and small intestine of man and hog. J Biol Chem 1978; 253: 4022–30
  • Rehfeld J F, Larsson L I, Goltermann N R, et al. Neural regulation of pancreatic hormone secretion by the C-terminal tetrapeptide of CCK. Nature 1980; 284: 33–9
  • Hökfelt T, Rehfeld J F, Skirboll L, et al. Evidence for coexistence of dopamine and CCK in mesolimbic neurons. Nature 1980; 285: 476–8
  • Rehfeld J F, Hansen H F. Characterization of procholecystokinin products in the porcine cerebral cortex. J Biol Chem 1986; 261: 5832–40
  • Rehfeld J F. Accumulation of nonamidated progastrin and procholecystokinin products in the porcine anterior pituitary. J Biol Chem 1986; 261: 58417
  • Rehfeld J F. Cholecystokinin [review]. Handbook of physiology: the gastrointestinal system, vol. II, G M Makhlouf. Am Phys Soc, Bethesda 1989; 337–58
  • Johnsen A H, Rehfeld J F. Cionin, a disulfotyrosyl hybrid of cholecystokinin and gastrin from the protochordate Ciona intestinalis. J Biol Chem 1990; 265: 3054–8
  • Rehfeld J F, Mogensen N W, Bardram L, et al. Expression but failing maturation of procholecystokinin in cerebellum. Brain Res 1992; 576: 111–9
  • Rehfeld J F, Bardram L, Hilsted L. Ontogeny of procholecystokinin maturation in the rat duodenum, jejunum and ileum. Gastroenterology 1992; 103: 424–30
  • Fahrenkrug J, Schaffalitzky de Muckadell O B. Radioimmunoassay of vasoactive intestinal polypeptide (VIP) in plasma. J Lab Clin Med 1977; 89: 1379–88
  • Fahrenkrug J, Schaffalitzky de Muckadell O B, Hoist J J, Jensen S L. Vasoactive intestinal polypeptide in vagally mediated pancreatic secretion of fluid and bicarbonate. Am J Physiol 1979; 237: E535–40
  • Fahrenkrug J. Glycine-extended processing intermediate of pro VIP: a new form of VIP in the rat. Biochim Biophys Res Commun 1991; 178: 173–7
  • Rønnov-Jessen D, Gether U, Fahrenkrug J. PreproVIP derived peptides in tissue and plasma from patient with VIP-producing tumours. Eur J Clin Invest 1991; 21: 154–60
  • Bredkjær H E, Rønnov-Jessen D, Fahrenkrug L, Ekblad E, Fahrenkrug J. Expression of prepro-VIP-derived peptides in the human gastrointestinal tract: a biochemical and immunocyto-chemical study. Regul Pept 1991; 33: 145–64
  • Fahrenkrug J, Galbo H, Hoist J J, Schaffalitzky de Muckadell O B. Influence of the autonomic nervous system on the release of vasoactive intestinal polypeptide from the porcine gastrointestinal tract. J Physiol (Lond) 1978; 280: 405–22
  • Fahrenkrug J, Haglund U, Jodal M, Lundgren O, Olbe L, Schaffalitzky de Muckadell O B. Nervous release of vasoactive intestinal polypeptide in the gastrointestinal tract of cats: possible physiological implications. J Physiol (Lond) 1978; 284: 291–305
  • Fahrenkrug J, Emson P. Characterization and regional distribution of peptides derived from the VIP-precursor in the normal human brain. J Neurochem 1989; 53: 1142–8
  • Larsson L-I, Fahrenkrug J, Schaffalitzky de Muckadell O B, Sundler F, Håkanson R, Rehfeld J. Localization of vasoactive intestinal polypeptide (VIP) to central and peripheral neurons. Proc Natl Acad Sci USA 1976; 73: 3197–200
  • Lundberg J M, Änggård A, Fahrenkrug J, Hökfelt T, Mutt V. Vasoactive intestinal polypeptide (VIP) in cholinergic neurons of exocrine glands: functional significance of coexisting transmitters for vasodilation and secretion. Proc Natl Acad Sci USA 1980; 77: 1651–5
  • Ottesen B, Wagner G, Viraq R, Fahrenkrug J. Penile erection: possible role for vasoactive intestinal polypeptide as a neurotransmitter. Brit Med J 1984; 288: 9–11
  • Pederson R A. Gastric inhibitory polypeptide. Gut peptides, J H Walsh, G J Dockray. Raven Press, New York 1994; 2172–260
  • Nauck M, Schmidt W E, Ebert R, et al. Insulinotropic properties of synthetic human gastric inhibitory polypeptide in man: interactions with glucose, phenylalanine, and cholecystokinin-8. J Clin Endocrinol Metab 1989; 69: 654–61
  • Salera M, Giacomono P, Pironi L, et al. Circadian rhythm of gastric inhibitory polypeptide (GIP) in man. Metabolism 1983; 32: 21–4
  • Walsh J H. Gastrointestinal hormones. Physiology of the gastrointestinal tract.3rd ed., L R Johnson. New York, Raven Press 1994; 1–120
  • Takeda J, Seino Y, Tanaka K, et al. Sequence of an intestinal cDNA encoding human gastric inhibitory polypeptide precursor. Proc Natl Acad Sci USA 1987; 84: 7005–8
  • Usdin T B, Mezey E, Button D C, Brownstein M J, Bonner T I. Gastric inhibitory polypeptide receptor, a member of the secretin-vasoactive intestinal peptide receptor family, is widely distributed in peripheral organs and the brain. Endocrinology 1993; 133: 2861–70
  • Lacroix A, Bolte E, Tremblay J, et al. Gastric inhibitory polypeptide-dependent cortisol hypersecretion—a new cause of Cushing's syndrome. N Engl J Med 1992; 327: 974–80
  • Moody A J, Thim L, Valverde I. The isolation and sequencing of human gastric inhibitory peptide (GIP). FEBS Lett 1984; 172: 142–8
  • Brazeau P, Vale W, Burgut R, et al. Hypothalamic polypeptide that inhibits the secretion of immunoreactive pituitary growth hormones. Science 1973; 179: 77–9
  • Pradayrol L, Jörnvall H, Mutt V, Ribet A. N-terminally extended somatostatin: the primary structure of somatostatin-28. FEBS Lett 1980; 109: 55–9
  • Shen P L, Pictet R L, Rutter W J. Human somatostatin I: sequence of the cDNA. Proc Natl Acad Sci USA 1982; 79: 4575–9
  • Hoist J J, Jørgensen P N, Rasmussen T N, Schmidt P. Somatostatin restraint of gastrin secretion in porcine antrum revealed by monoclonal antibody immunoneutralization. Am J Physiol 1992; 263: G908–12
  • Hoist J J, Ørskov C, Seier Poulsen S. Somatostatin is an essential paracrine link in acid inhibition of gastrin secretion. Digestion 1992; 51: 95–102
  • Bell G I, Reisine T. Molecular biology of somatostatin receptors. Trends Neurosci 1993; 16: 34–8
  • Darcis T, Van Moerbeke D. Digestive applications of somatostatin: liver, alimentary tract and pancreas. Scand J Gastroenterol 1994; 29(Suppl 207)1–44
  • Hoist Pedersen J, Fahrenkrug J. Neurotensin-like immunoreactivities in human plasma: feeding responses and metabolism. Peptides 1986; 7: 15–20
  • Skov Olsen P, Hoist Pedersen J, Kirkegaard P, Stadil F, Fahrenkrug J, Christiansen J. Neurotensin inhibits meal-stimulated gastric acid secretion in man. Scand J Gastroenterol 1983; 18: 1073–6
  • McDonald T J. The gastrin-releasing polypeptide (GRP). Gastrointestinal hormones. Advances in metabolic disorders, V. Mutt. San Diego, Academic Press 1988; vol 11: 199–250
  • Dockray G J. Physiology of the enteric neuropeptides. Physiology of the gastrointestinal tract.3rd ed., L R Johnsen. New York, Raven Press 1994; 169–209
  • Battey J F, Way J M, Corjay M H, et al. Molecular cloning of the bombesin/gastrin-releasing peptide receptor from Swiss 3t3 cells. Biochemistry 1991; 88: 395–9
  • Knigge U, Hoist J J, Knuhtsen S, et al. Pharmacokinetics and effects on gastroentero-pancreatic hormones and gastric secretion in normal men. J Clin Endocrinol Metab 1984; 59: 310–5
  • Hoist J J, Knuhtsen S, Ørskov C, et al. GRP-producing nerves control antral somatostatin and gastrin secretion in pigs. Am J Physiol 1987; 253: G767–74
  • Hoist J J. Neural regulation of pancreatic exocrine function. The pancreas. Biology, pathobiology and disease. 2nd ed., V LW Go, et al. Raven Press, New York 1993; 381–402
  • Hoist J J, Bork E, Sørensen J B, Schwartz T W, Hansen M. Elevated plasma concentrations of GRP C-flanking peptide in small cell cancer. J Clin Oncol 1989; 7: 1831–8
  • Tatemoto K, Mutt V. Chemical determination of polypeptide hormones. Proc Natl Acad Sci USA 1978; 75: 4115–9
  • Larhammar D, Blomquist A G, Yee F, et al. Cloning and functional expression of a human neuropeptide Y/peptide YY receptor of the Y, type. J Biol Chem 1992; 267: 10935–8
  • Fuhlendorff J, Bether U, Aakerlund L, Schwartz T W, et al. [Leu31, Pro34]neuropeptide Y: A specific Y1 receptor agonist. Proc Natl Acad Sci 1990; 87: 182–6
  • Schwartz T W, Fuhlendorff J, Kjems L, et al. Signal epitopes in the three-dimensional structure of neuropeptide Y. Interaction with Y1, Y2 and pancreatic polypeptide receptors. Ann NY Acad Sci 1990; 611: 35–47
  • Tatemoto K, Rökaeus A, Jömvall H, McDonald T, Mutt V. Galanin—a novel biologically active peptide from porcine intestine. FEBS Lett 1983; 164: 124–8
  • Rökaeus A, Brownstein M J. Construction of a porcine adrenal medullary cDNA library and nucleotide sequence analysis of two clones encoding a galanin precursor. Proc Natl Acad Sci USA 1986; 83: 6287–91
  • Bersani M, Johnsen A H, Høirup P, Dunning B E, Andreasen J, Hoist J J. Human galanin: primary structure and identification of two molecular forms. FEBS Lett 1991; 283: 189–94
  • Habert-Ortoli E, Amiranoff A, Loquet I, Laburthe M, Mayaux J F. Molecular cloning of a functional human galanin receptor. Proc Natl Acad Sci USA 1994; 91: 9780–3
  • Hoist J J, Bersani M, Hvidberg A M, et al. On the effects of human galanin in man. Diabetologia 1992; 36: 653–7
  • Hoist J J, Ehrhart-Bornstein M, Messel T, Poulsen S S. Harling H. Release of galanin from isolated perfused porcine adrenal glands. Role of the splanchnic nerves. Am J Physiol 1991; 261: E31–40

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