The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Gene Review

SCT  -  secretin

Sus scrofa

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of SCT


High impact information on SCT

  • The two forms of pituitary adenylyl cyclase-activating polypeptide (PACAP-27 and -38) are neuropeptides of the secretin/glucagon/vasoactive intestinal polypeptide/growth-hormone-releasing hormone family and regulate hormone release from the pituitary and adrenal gland [5].
  • Under the stimulation with secretin, 5-HT decreased the intracellular pH (pH(i)) and reduced the rate of pH(i) recovery after acid loading with NH(4)(+), suggesting that 5-HT inhibits the intracellular accumulation of HCO3(-) [6].
  • Thus, 5-HT, acting through basolateral 5-HT(3) receptors, strongly inhibits spontaneous, secretin-, and ACh-stimulated fluid secretion by guinea pig pancreatic ducts [6].
  • Basolateral applications of 5-HT strongly but reversibly reduced HCO(3)-dependent, as well as secretin- and acetylcholine- (ACh-) stimulated, fluid secretion, whereas 5-HT applied into the lumen had no such effects [6].
  • Secretin, glucagon, and vasoactive intestinal peptide, at concentrations as high as 10(-5) M, failed to alter calcium outflux and did not affect stimulation by CCK-octapeptide or by carbamycholine [7].

Chemical compound and disease context of SCT


Biological context of SCT

  • The two secretin preparations were found to be equipotent with respect to pancreatic secretion and plasma kinetics [11].
  • The remarkable sequence homology of PHI to the vasoactive intestinal peptide, secretin, glucagon, and gastric inhibitory polypeptide indicates that this peptide is a member of the glucagon-secretin family [12].
  • The difference between the relative affinities of VIP and secretin for the high affinity VIP binding sites appears to be primarily attributable to the NH2-terminal portions of these molecules since synthetic COOH-terminal fragments VIP 14-28, VIP 15-28, and secretin 14-27 were equipotent in inhibiting 125I-VIP binding [13].
  • A low-affinity VIP binding protein (IC50 0.7 microM) was detected in a fraction eluting later and exhibited a peptide specificity: rGRF > VIP > VIP(10-28) > secretin > PHI [14].
  • Gastrin, secretin, cholecystokinin, and motilin concentrations were determined by radioimmunoassay during fasting and postprandial periods (15, 30, 45, 120, 180, and 240 min) [15].

Anatomical context of SCT

  • In LLC-PK1 porcine epithelial cells, the urokinase-type plasminogen activator (u-PA) mRNA and protein can be induced either by stimulation of the protein kinase C (PKC) pathway using a tumor promoter (PMA) or by stimulation of the protein kinase A (PKA) pathway with calcitonin (SCT) [16].
  • Effects of the peripheral and central administration of porcine (PCT) and salmon (SCT) calcitonin on the gastric acid secretion stimulated by various secretagogues were studied in the perfused stomach of anaesthetized rats [17].
  • The present study indicates that PCT and SCT may in part suppress gastric acid secretion due to an interaction with TRH in the hypothalamus [17].
  • BACKGROUND/AIMS: Secretin stimulates pancreatic ductules to secrete HCO3- into pancreatic juice and H+ into interstitial fluid [18].
  • Effects of alcohols on the actions of VIP and secretin on acinar cells from guinea pig pancreas [19].

Associations of SCT with chemical compounds

  • The intracerebroventricular PCT and SCT blocked TRH-induced acid secretion [17].
  • Incubation with SCT resulted in a dose-dependent accumulation of adenosine 3',5'-cyclic monophosphate (cAMP) [50% effective concentration (EC50) = 0.02 nM] in transfected cells (referred to as PC-1 cells) [20].
  • SCT also increased inositol trisphosphate production in PC-1 cells [20].
  • Vasoactive intestinal peptide or secretin, each of which increases cellular cyclic AMP, caused endogenous activation of protein kinase and inhibition of cyclic [3H]AMP binding but did not alter bindings of cyclic [3H]GMP or cyclic [3H]AMP [21].
  • In dispersed acini prepared from guinea pig pancreas, ethanol inhibited the increase in amylase secretion caused by cholecystokinin, carbachol, secretin, or vasoactive intestinal peptide [19].

Regulatory relationships of SCT

  • Somatostatin inhibited secretin- and prostaglandin E1-induced Isc, but was ineffective in tissues stimulated with 8-Br-cyclic AMP [22].
  • Substance P (SP) inhibits secretin-stimulated HCO(3)(-) secretion by modulating a Cl(-)-dependent HCO(3)(-) efflux step at the apical membrane of the duct cell (Hegyi P, Gray MA, and Argent BE. Am J Physiol Cell Physiol 285: C268-C276, 2003) [23].
  • When we assayed the hormonal interaction on amylase release from dispersed pancreatic acini, we found that secretin (32 nM) failed to influence the secretory response to cholecystokinin (1 pM-10 nM) [24].
  • It is concluded that AVP directly inhibits secretin-stimulated ductal fluid secretion in the guinea pig pancreas [25].

Other interactions of SCT

  • Binding of 125I-labeled PYY was rapid (70% maximal within 10 min) and specific (not inhibited by secretin, vasoactive intestinal peptide, cholecystokinin, carbachol, prostaglandin E2, forskolin, or cholera toxin) [26].
  • The increases in cyclic AMP levels evoked by exposure to either 0.1 nM or 0.1 microM secretin were not significantly different in pancreatic ducts isolated from healthy and diabetic guinea pigs nor were levels of CFTR or Na+, K(+)-ATPase expression [27].
  • Calmodulin exhibits high-affinity, calcium-dependent binding of 1 mol/mol of the vasoactive intestinal peptide (VIP), secretin, and either the 42- or 43-residue gastric inhibitory peptide (GIP) with dissociation constants of 0.05-0.14 microM [28].
  • Secretin caused a 10-fold rise of luminal efflux of cyclic AMP that was mitigated by somatostatin, added at 6 x 10(-7) M to the serosal bath [22].
  • In addition, bisindolylmaleimide I (1 nM to 1 microM), an inhibitor of PKC, relieved the inhibitory effect of SP on secretin-stimulated HCO(3)(-) secretion and also reversed the inhibitory effect of PDBu [23].

Analytical, diagnostic and therapeutic context of SCT


  1. Comparison of biologic porcine secretin, synthetic porcine secretin, and synthetic human secretin in pancreatic function testing. Somogyi, L., Ross, S.O., Cintron, M., Toskes, P.P. Pancreas (2003) [Pubmed]
  2. Current concepts on physiological control of gastric acid secretion. Clinical applications. Ivey, K.J. Am. J. Med. (1975) [Pubmed]
  3. Isolation and NH2-terminal sequence of a novel porcine anterior pituitary polypeptide. Homology to proinsulin, secretin and Rous sarcoma virus transforming protein TVFV60. Hsi, K.L., Seidah, N.G., De Serres, G., Chrétien, M. FEBS Lett. (1982) [Pubmed]
  4. The effect of acute ethanol administration on the exocrine pancreatic secretion of the pig. Wheatley, I.C., Barbezat, G.O., Hickman, R., Terblanche, J. The British journal of surgery. (1975) [Pubmed]
  5. Differential signal transduction by five splice variants of the PACAP receptor. Spengler, D., Waeber, C., Pantaloni, C., Holsboer, F., Bockaert, J., Seeburg, P.H., Journot, L. Nature (1993) [Pubmed]
  6. 5-hydroxytryptamine strongly inhibits fluid secretion in guinea pig pancreatic duct cells. Suzuki, A., Naruse, S., Kitagawa, M., Ishiguro, H., Yoshikawa, T., Ko, S.B., Yamamoto, A., Hamada, H., Hayakawa, T. J. Clin. Invest. (2001) [Pubmed]
  7. Action of cholecystokinin and cholinergic agents on calcium transport in isolated pancreatic acinar cells. Gardner, J.D., Conlon, T.P., Kleveman, H.L., Adams, T.D., Ondetti, M.A. J. Clin. Invest. (1975) [Pubmed]
  8. Mechanism of hepatic bicarbonate secretion and bile acid independent bile secretion. Mathisen, O., Raeder, M. Eur. J. Clin. Invest. (1983) [Pubmed]
  9. Amino acid- and glucose-induced cholestasis before and during secretin stimulation. Mathisen, O., Omland, E. Scand. J. Gastroenterol. (1989) [Pubmed]
  10. Characteristics of inhibition of pancreatic secretion by the beta-adrenergic agonist, terbutaline. Joehl, R.J. Pancreas (1986) [Pubmed]
  11. Human secretin. Biologic effects and plasma kinetics in humans. Christ, A., Werth, B., Hildebrand, P., Gyr, K., Stalder, G.A., Beglinger, C. Gastroenterology (1988) [Pubmed]
  12. Isolation and characterization of the intestinal peptide porcine PHI (PHI-27), a new member of the glucagon--secretin family. Tatemoto, K., Mutt, V. Proc. Natl. Acad. Sci. U.S.A. (1981) [Pubmed]
  13. Interaction of porcine vasoactive intestinal peptide with dispersed pancreatic acinar cells from the guinea pig. Binding of radioiodinated peptide. Christophe, J.P., Conlon, T.P., Gardner, J.D. J. Biol. Chem. (1976) [Pubmed]
  14. Simultaneous solubilization of high-affinity receptors for VIP and glucagon and of a low-affinity binding protein for VIP, shown to be identical to calmodulin. Andersson, M., Carlquist, M., Maletti, M., Marie, J.C. FEBS Lett. (1993) [Pubmed]
  15. Hyperosmolal formula in neonatal piglets: effects on gastrointestinal hormone concentrations, enteric bacterial titers, and small intestinal histology. Szabo, J.S., Rayford, P.L., Uthman, E., Lobe, T.E. J. Pediatr. Gastroenterol. Nutr. (1990) [Pubmed]
  16. Staurosporine stimulates expression of the urokinase-type (u-PA) plasminogen activator in LLC-PK1 cells. Dierks-Ventling, C., Knesel, J., Nagamine, Y., Hemmings, B.A., Pehling, G., Fischer, F., Fabbro, D. Int. J. Cancer (1989) [Pubmed]
  17. Inhibitory effects of intrahypothalamic injection of calcitonin on TRH-stimulated gastric acid secretion in rats. Maeda-Hagiwara, M., Watanabe, H. Jpn. J. Pharmacol. (1985) [Pubmed]
  18. Secretin causes H+/HCO3- secretion from pig pancreatic ductules by vacuolar-type H(+)-adenosine triphosphatase. Villanger, O., Veel, T., Raeder, M.G. Gastroenterology (1995) [Pubmed]
  19. Effects of alcohols on the actions of VIP and secretin on acinar cells from guinea pig pancreas. Uhlemann, E.R., Robberecht, P., Gardner, J.D. Gastroenterology (1979) [Pubmed]
  20. A cloned porcine renal calcitonin receptor couples to adenylyl cyclase and phospholipase C. Force, T., Bonventre, J.V., Flannery, M.R., Gorn, A.H., Yamin, M., Goldring, S.R. Am. J. Physiol. (1992) [Pubmed]
  21. Cyclic nucleotide-dependent protein kinase activity in acinar cells from guinea pig pancreas. Jensen, R.T., Gardner, J.D. Gastroenterology (1978) [Pubmed]
  22. Secretin and somatostatin as modulators of electrolyte transport in guinea pig gallbladder epithelium. Sprakties, G., Macherey, H.J., Petersen, K.U. J. Pharmacol. Exp. Ther. (1993) [Pubmed]
  23. Protein kinase C mediates the inhibitory effect of substance P on HCO3- secretion from guinea pig pancreatic ducts. Hegyi, P., Rakonczay, Z., Tiszlavicz, L., Varró, A., Tóth, A., Rácz, G., Varga, G., Gray, M.A., Argent, B.E. Am. J. Physiol., Cell Physiol. (2005) [Pubmed]
  24. Secretin potentiates guinea pig pancreatic response to cholecystokinin by a cholinergic mechanism. Alcón, S., Rosado, J.A., García, L.J., Pariente, J.A., Salido, G.M., Pozo, M.J. Can. J. Physiol. Pharmacol. (1996) [Pubmed]
  25. Arginine vasopressin inhibits fluid secretion in guinea pig pancreatic duct cells. Ko, S.B., Naruse, S., Kitagawa, M., Ishiguro, H., Murakami, M., Hayakawa, T. Am. J. Physiol. (1999) [Pubmed]
  26. Y2 receptors for peptide YY and neuropeptide Y on dispersed chief cells from guinea pig stomach. Singh, G., Singh, L., Raufman, J.P. Am. J. Physiol. (1992) [Pubmed]
  27. Sodium, potassium-activated adenosine triphosphatase activity is impaired in the guinea pig pancreatic duct system in streptozotocin-induced diabetes. Hootman, S.R., Jones, J.E., Kapoor, R., Nguyen, K.L., de Ondarza, J. Biochem. Biophys. Res. Commun. (1998) [Pubmed]
  28. Binding of hormones and neuropeptides by calmodulin. Malencik, D.A., Anderson, S.R. Biochemistry (1983) [Pubmed]
  29. Processing of prosecretin: isolation of a secretin precursor from porcine intestine. Gafvelin, G., Jörnvall, H., Mutt, V. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  30. Synthesis of phenolic group containing analogues of porcine secretin and their immunological properties. Yanaihara, N., Kubota, M., Sakagami, M., Sato, H., Mochizuki, T. J. Med. Chem. (1977) [Pubmed]
  31. Exocrine pancreatic dysfunction in guinea pigs with diabetes mellitus. Balk, M.W., Lang, C.M., White, W.J., Munger, B.L. Lab. Invest. (1975) [Pubmed]
WikiGenes - Universities