Secretin

Last updated
SCT
Identifiers
Aliases SCT , entrez:6343, secretin
External IDs OMIM: 182099 HomoloGene: 137358 GeneCards: SCT
Orthologs
SpeciesHumanMouse
Entrez

6343

n/a

Ensembl

ENSG00000070031
ENSG00000274473

n/a

UniProt

P09683

n/a

RefSeq (mRNA)

NM_021920

n/a

RefSeq (protein)

NP_068739

n/a

Location (UCSC) Chr 11: 0.63 – 0.63 Mb n/a
PubMed search [2] n/a
Wikidata
View/Edit Human

Secretin is a hormone that regulates water homeostasis throughout the body and influences the environment of the duodenum by regulating secretions in the stomach, pancreas, and liver. It is a peptide hormone produced in the S cells of the duodenum, which are located in the intestinal glands. [3] In humans, the secretin peptide is encoded by the SCT gene. [4]

Contents

Secretin helps regulate the pH of the duodenum by inhibiting the secretion of gastric acid from the parietal cells of the stomach and stimulating the production of bicarbonate from the ductal cells of the pancreas. [5] [6] It also stimulates the secretion of bicarbonate and water by cholangiocytes in the bile duct, protecting it from bile acids by controlling the pH and promoting the flow in the duct. [7] Meanwhile, in concert with secretin's actions, the other main hormone simultaneously issued by the duodenum, cholecystokinin (CCK), stimulates the gallbladder to contract, delivering its stored bile.

Prosecretin is a precursor to secretin, which is present in digestion. Secretin is stored in this unusable form, and is activated by gastric acid. This indirectly results in the neutralisation of duodenal pH, thus ensuring no damage is done to the small intestine by the aforementioned acid. [8]

In 2007, secretin was discovered to play a role in osmoregulation by acting on the hypothalamus, pituitary gland, and kidney. [9] [10]

History

In 1902, William Bayliss and Ernest Starling were studying how the nervous system controls the process of digestion. [11] It was known that the pancreas secreted digestive juices in response to the passage of food (chyme) through the pyloric sphincter into the duodenum. They discovered (by cutting all the nerves to the pancreas in their experimental animals) that this process was not, in fact, governed by the nervous system. They determined that a substance secreted by the intestinal lining stimulates the pancreas after being transported via the bloodstream. They named this intestinal secretion secretin. This type of 'chemical messenger' substance is now called a hormone, a term coined by Starling in 1905. [12]

Secretin is frequently erroneously stated to have been the first hormone identified. [13] However, British researchers George Oliver and Edward Albert Schäfer had already published their findings of an adrenal extract increasing blood pressure and heart rate in brief reports in 1894 and a full publication in 1895, making adrenaline the first discovered hormone. [14] [15]

Structure

Secretin is initially synthesized as a 120 amino acid precursor protein known as prosecretin. This precursor contains an N-terminal signal peptide, spacer, secretin itself (residues 28–54), and a 72-amino acid C-terminal peptide. [4]

The mature secretin peptide is a linear peptide hormone, which is composed of 27 amino acids and has a molecular weight of 3055. A helix is formed in the amino acids between positions 5 and 13. The amino acids sequences of secretin have some similarities to that of glucagon, vasoactive intestinal peptide (VIP), and gastric inhibitory peptide (GIP). Fourteen of 27 amino acids of secretin reside in the same positions as in glucagon, 7 the same as in VIP, and 10 the same as in GIP. [16]

Secretin also has an amidated carboxyl-terminal amino acid which is valine. [17] The sequence of amino acids in secretin is H–His-Ser-Asp-Gly-Thr-Phe-Thr-Ser-Glu-Leu-Ser-Arg-Leu-Arg-Asp-Ser-Ala-Arg-Leu-Gln-Arg-Leu-Leu-Gln-Gly-Leu-Val–NH2. [17]

Physiology

Production and secretion

Secretin is synthesized in cytoplasmic secretory granules of S-cells, which are found mainly in the mucosa of the duodenum, and in smaller numbers in the jejunum of the small intestine. [18]

Secretin is released into circulation and/or intestinal lumen in response to low duodenal pH that ranges between 2 and 4.5 depending on species; the acidity is due to hydrochloric acid in the chyme that enters the duodenum from the stomach via the pyloric sphincter. [19] Also, the secretion of secretin is increased by the products of protein digestion bathing the mucosa of the upper small intestine. [20]

Secretin release is inhibited by H2 antagonists, which reduce gastric acid secretion. As a result, if the pH in the duodenum increases above 4.5, secretin cannot be released. [21]

Function

pH regulation

Secretin primarily functions to neutralize the pH in the duodenum, allowing digestive enzymes from the pancreas (e.g., pancreatic amylase and pancreatic lipase) to function optimally. [22]

Secretin targets the pancreas; pancreatic centroacinar cells have secretin receptors in their plasma membrane. As secretin binds to these receptors, it stimulates adenylate cyclase activity and converts ATP to cyclic AMP. [23] Cyclic AMP acts as second messenger in intracellular signal transduction and causes the organ to secrete a bicarbonate-rich fluid that flows into the intestine. Bicarbonate is a base that neutralizes the acid, thus establishing a pH favorable to the action of other digestive enzymes in the small intestine. [24]

Secretin also increases water and bicarbonate secretion from duodenal Brunner's glands to buffer the incoming protons of the acidic chyme, [22] and also reduces acid secretion by parietal cells of the stomach. [25] It does this through at least three mechanisms: 1) By stimulating release of somatostatin, 2) By inhibiting release of gastrin in the pyloric antrum, and 3) By direct downregulation of the parietal cell acid secretory mechanics. [26] [19]

It counteracts blood glucose concentration spikes by triggering increased insulin release from pancreas, following oral glucose intake. [27]

Osmoregulation

Secretin modulates water and electrolyte transport in pancreatic duct cells, [28] liver cholangiocytes, [29] and epididymis epithelial cells. [30] It is found [31] to play a role in the vasopressin-independent regulation of renal water reabsorption. [9]

Secretin is found in the magnocellular neurons of the paraventricular and supraoptic nuclei of the hypothalamus and along the neurohypophysial tract to neurohypophysis. During increased osmolality, it is released from the posterior pituitary. In the hypothalamus, it activates vasopressin release. [10] It is also needed to carry out the central effects of angiotensin II. In the absence of secretin or its receptor in the gene knockout animals, central injection of angiotensin II was unable to stimulate water intake and vasopressin release. [32]

It has been suggested that abnormalities in such secretin release could explain the abnormalities underlying type D syndrome of inappropriate antidiuretic hormone hypersecretion (SIADH). [10] In these individuals, vasopressin release and response are normal, although abnormal renal expression, translocation of aquaporin 2, or both are found. [10] It has been suggested that "Secretin as a neurosecretory hormone from the posterior pituitary, therefore, could be the long-sought vasopressin independent mechanism to solve the riddle that has puzzled clinicians and physiologists for decades." [10]

Food intake

Secretin and its receptor are found in discrete nuclei of the hypothalamus, including the paraventricular nucleus and the arcuate nucleus, which are the primary brain sites for regulating body energy homeostasis. It was found that both central and peripheral injection of Sct reduce food intake in mouse, indicating an anorectic role of the peptide. This function of the peptide is mediated by the central melanocortin system. [33]

Uses

Secretin is used in a diagnostic tests for pancreatic function; secretin is injected and the pancreatic output can then be imaged with magnetic resonance imaging, a noninvasive procedure, or secretions generated as a result can gathered either through an endoscope or through tubes inserted through the mouth, down into the duodenum. [34] [35] [36]

A recombinant human secretin has been available since 2004 for these diagnostic purposes. [37] There were problems with the availability of this agent from 2012 to 2015. [38]

Research

A wave of enthusiasm for secretin as a possible treatment for autism arose in the 1990s based on a hypothetical gut-brain connection; as a result the NIH ran a series of clinical trials that showed that secretin was not effective, which brought an end to popular interest. [39] [40] [41]

A high-affinity and optimized secretin receptor antagonist (Y10,c[E16,K20],I17,Cha22,R25)sec(6-27) has been designed and developed which has allowed the structural characterization of secreting inactive conformation. [42]

See also

Related Research Articles

<span class="mw-page-title-main">Pancreas</span> Organ of the digestive system and endocrine system of vertebrates

The pancreas is an organ of the digestive system and endocrine system of vertebrates. In humans, it is located in the abdomen behind the stomach and functions as a gland. The pancreas is a mixed or heterocrine gland, i.e., it has both an endocrine and a digestive exocrine function. 99% of the pancreas is exocrine and 1% is endocrine. As an endocrine gland, it functions mostly to regulate blood sugar levels, secreting the hormones insulin, glucagon, somatostatin and pancreatic polypeptide. As a part of the digestive system, it functions as an exocrine gland secreting pancreatic juice into the duodenum through the pancreatic duct. This juice contains bicarbonate, which neutralizes acid entering the duodenum from the stomach; and digestive enzymes, which break down carbohydrates, proteins and fats in food entering the duodenum from the stomach.

<span class="mw-page-title-main">Glucagon</span> Peptide hormone

Glucagon is a peptide hormone, produced by alpha cells of the pancreas. It raises the concentration of glucose and fatty acids in the bloodstream and is considered to be the main catabolic hormone of the body. It is also used as a medication to treat a number of health conditions. Its effect is opposite to that of insulin, which lowers extracellular glucose. It is produced from proglucagon, encoded by the GCG gene.

<span class="mw-page-title-main">Cholecystokinin</span> Hormone of the gastrointestinal system

Cholecystokinin is a peptide hormone of the gastrointestinal system responsible for stimulating the digestion of fat and protein. Cholecystokinin, formerly called pancreozymin, is synthesized and secreted by enteroendocrine cells in the duodenum, the first segment of the small intestine. Its presence causes the release of digestive enzymes and bile from the pancreas and gallbladder, respectively, and also acts as a hunger suppressant.

<span class="mw-page-title-main">Gastrin</span> Mammalian protein found in Homo sapiens

Gastrin is a peptide hormone that stimulates secretion of gastric acid (HCl) by the parietal cells of the stomach and aids in gastric motility. It is released by G cells in the pyloric antrum of the stomach, duodenum, and the pancreas.

<span class="mw-page-title-main">Gastric acid</span> Digestive fluid formed in the stomach

Gastric acid, gastric juice, or stomach acid is a digestive fluid formed within the stomach lining. With a pH between 1 and 3, gastric acid plays a key role in digestion of proteins by activating digestive enzymes, which together break down the long chains of amino acids of proteins. Gastric acid is regulated in feedback systems to increase production when needed, such as after a meal. Other cells in the stomach produce bicarbonate, a base, to buffer the fluid, ensuring a regulated pH. These cells also produce mucus – a viscous barrier to prevent gastric acid from damaging the stomach. The pancreas further produces large amounts of bicarbonate and secretes bicarbonate through the pancreatic duct to the duodenum to neutralize gastric acid passing into the digestive tract.

<span class="mw-page-title-main">Digestive enzyme</span> Class of enzymes

Digestive enzymes are a group of enzymes that break down polymeric macromolecules into their smaller building blocks, in order to facilitate their absorption into the cells of the body. Digestive enzymes are found in the digestive tracts of animals and in the tracts of carnivorous plants, where they aid in the digestion of food, as well as inside cells, especially in their lysosomes, where they function to maintain cellular survival. Digestive enzymes of diverse specificities are found in the saliva secreted by the salivary glands, in the secretions of cells lining the stomach, in the pancreatic juice secreted by pancreatic exocrine cells, and in the secretions of cells lining the small and large intestines.

<span class="mw-page-title-main">Vasoactive intestinal peptide</span> Hormone that affects blood pressure / heart rate

Vasoactive intestinal peptide, also known as vasoactive intestinal polypeptide or VIP, is a peptide hormone that is vasoactive in the intestine. VIP is a peptide of 28 amino acid residues that belongs to a glucagon/secretin superfamily, the ligand of class II G protein–coupled receptors. VIP is produced in many tissues of vertebrates including the gut, pancreas, cortex, and suprachiasmatic nuclei of the hypothalamus in the brain. VIP stimulates contractility in the heart, causes vasodilation, increases glycogenolysis, lowers arterial blood pressure and relaxes the smooth muscle of trachea, stomach and gallbladder. In humans, the vasoactive intestinal peptide is encoded by the VIP gene.

<span class="mw-page-title-main">Incretin</span> Group of gastrointestinal hormones

Incretins are a group of metabolic hormones that stimulate a decrease in blood glucose levels. Incretins are released after eating and augment the secretion of insulin released from pancreatic beta cells of the islets of Langerhans by a blood-glucose–dependent mechanism.

<span class="mw-page-title-main">Glucose-dependent insulinotropic polypeptide</span> Mammalian protein found in Homo sapiens

Glucose-dependent insulinotropic polypeptide, abbreviated as GIP, is an inhibiting hormone of the secretin family of hormones. While it is a weak inhibitor of gastric acid secretion, its main role, being an incretin, is to stimulate insulin secretion.

<span class="mw-page-title-main">Motilin</span>

Motilin is a 22-amino acid polypeptide hormone in the motilin family that, in humans, is encoded by the MLN gene.

<span class="mw-page-title-main">Gastrinoma</span> Medical condition

Gastrinomas are neuroendocrine tumors (NETs), usually located in the duodenum or pancreas, that secrete gastrin and cause a clinical syndrome known as Zollinger–Ellison syndrome (ZES). A large number of gastrinomas develop in the pancreas or duodenum, with near-equal frequency, and approximately 10% arise as primary neoplasms in lymph nodes of the pancreaticoduodenal region.

Pancreatic juice is a liquid secreted by the pancreas, which contains a number of digestive enzymes, including trypsinogen, chymotrypsinogen, elastase, carboxypeptidase, pancreatic lipase, nucleases and amylase. The pancreas is located in the visceral region, and is a major part of the digestive system required for proper digestion and subsequent assimilation of macronutrient substances required for living.

<span class="mw-page-title-main">Glucagon-like peptide-1</span> Gastrointestinal peptide hormone Involved in glucose homeostasis

Glucagon-like peptide-1 (GLP-1) is a 30- or 31-amino-acid-long peptide hormone deriving from the tissue-specific posttranslational processing of the proglucagon peptide. It is produced and secreted by intestinal enteroendocrine L-cells and certain neurons within the nucleus of the solitary tract in the brainstem upon food consumption. The initial product GLP-1 (1–37) is susceptible to amidation and proteolytic cleavage, which gives rise to the two truncated and equipotent biologically active forms, GLP-1 (7–36) amide and GLP-1 (7–37). Active GLP-1 protein secondary structure includes two α-helices from amino acid position 13–20 and 24–35 separated by a linker region.

<span class="mw-page-title-main">Peptide YY</span> Peptide released from cells in the ileum and colon in response to feeding

Peptide YY (PYY) also known as peptide tyrosine tyrosine is a peptide that in humans is encoded by the PYY gene. Peptide YY is a short peptide released from cells in the ileum and colon in response to feeding. In the blood, gut, and other elements of periphery, PYY acts to reduce appetite; similarly, when injected directly into the central nervous system, PYY is also anorexigenic, i.e., it reduces appetite.

<span class="mw-page-title-main">Enteroendocrine cell</span>

Enteroendocrine cells are specialized cells of the gastrointestinal tract and pancreas with endocrine function. They produce gastrointestinal hormones or peptides in response to various stimuli and release them into the bloodstream for systemic effect, diffuse them as local messengers, or transmit them to the enteric nervous system to activate nervous responses. Enteroendocrine cells of the intestine are the most numerous endocrine cells of the body. They constitute an enteric endocrine system as a subset of the endocrine system just as the enteric nervous system is a subset of the nervous system. In a sense they are known to act as chemoreceptors, initiating digestive actions and detecting harmful substances and initiating protective responses. Enteroendocrine cells are located in the stomach, in the intestine and in the pancreas. Microbiota play key roles in the intestinal immune and metabolic responses in these enteroendocrine cells via their fermentation product, acetate.

<span class="mw-page-title-main">Secretin receptor</span> Protein-coding gene in the species Homo sapiens

The secretin receptor is a protein that in humans is encoded by the SCTR gene. This protein is a G protein-coupled receptor which binds secretin and is the leading member of the secretin receptor family, also called class B GPCR subfamily.

<span class="mw-page-title-main">Gastric inhibitory polypeptide receptor</span> Protein-coding gene in the species Homo sapiens

The gastric inhibitory polypeptide receptor (GIP-R), also known as the glucose-dependent insulinotropic polypeptide receptor, is a protein that in humans is encoded by the GIPR gene.

<span class="mw-page-title-main">Secretin family</span>

Glucagon/gastric inhibitory polypeptide/secretin/vasoactive intestinal peptide hormones are a family of evolutionarily related peptide hormones that regulate activity of G-protein-coupled receptors from the secretin receptor family.

The nervous system, and endocrine system collaborate in the digestive system to control gastric secretions, and motility associated with the movement of food throughout the gastrointestinal tract, including peristalsis, and segmentation contractions.

Local hormones are a large group of signaling molecules that do not circulate within the blood. Local hormones are produced by nerve and gland cells and bind to either neighboring cells or the same type of cell that produced them. Local hormones are activated and inactivated quickly. They are released during physical work and exercise. They mainly control smooth and vascular muscle dilation. Strength of response is dependent upon the concentration of receptors of target cell and the amount of ligand.

References

  1. 1 2 3 ENSG00000274473 GRCh38: Ensembl release 89: ENSG00000070031, ENSG00000274473 - Ensembl, May 2017
  2. ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ↑ Häcki WH (September 1980). "Secretin". Clinics in Gastroenterology. 9 (3): 609–632. doi:10.1016/S0300-5089(21)00474-0. PMID   7000396.
  4. 1 2 Kopin AS, Wheeler MB, Leiter AB (March 1990). "Secretin: structure of the precursor and tissue distribution of the mRNA". Proceedings of the National Academy of Sciences of the United States of America. 87 (6): 2299–2303. Bibcode:1990PNAS...87.2299K. doi: 10.1073/pnas.87.6.2299 . JSTOR   2354038. PMC   53674 . PMID   2315322.
  5. ↑ Whitmore TE, Holloway JL, Lofton-Day CE, Maurer MF, Chen L, Quinton TJ, et al. (2000). "Human secretin (SCT): gene structure, chromosome location, and distribution of mRNA". Cytogenetics and Cell Genetics. 90 (1–2): 47–52. doi:10.1159/000015658. PMID   11060443. S2CID   12850155.
  6. ↑ Costanzo, Linda S. (2006). Physiology (3rd ed.). Philadelphia, PA: Saunders Elsevier. ISBN   9781416023203. OCLC   62326921.
  7. ↑ Banales JM, Huebert RC, Karlsen T, Strazzabosco M, LaRusso NF, Gores GJ (May 2019). "Cholangiocyte pathobiology". Nature Reviews. Gastroenterology & Hepatology. 16 (5): 269–281. doi:10.1038/s41575-019-0125-y. PMC   6563606 . PMID   30850822.
  8. ↑ Gafvelin G, Jörnvall H, Mutt V (September 1990). "Processing of prosecretin: isolation of a secretin precursor from porcine intestine". Proceedings of the National Academy of Sciences of the United States of America. 87 (17): 6781–6785. Bibcode:1990PNAS...87.6781G. doi: 10.1073/pnas.87.17.6781 . PMC   54621 . PMID   2395872.
  9. 1 2 Chu JY, Chung SC, Lam AK, Tam S, Chung SK, Chow BK (April 2007). "Phenotypes developed in secretin receptor-null mice indicated a role for secretin in regulating renal water reabsorption". Molecular and Cellular Biology. 27 (7): 2499–2511. doi:10.1128/MCB.01088-06. PMC   1899889 . PMID   17283064.
  10. 1 2 3 4 5 Chu JY, Lee LT, Lai CH, Vaudry H, Chan YS, Yung WH, Chow BK (September 2009). "Secretin as a neurohypophysial factor regulating body water homeostasis". Proceedings of the National Academy of Sciences of the United States of America. 106 (37): 15961–15966. Bibcode:2009PNAS..10615961C. doi: 10.1073/pnas.0903695106 . JSTOR   40484830. PMC   2747226 . PMID   19805236.
  11. ↑ Bayliss WM, Starling EH (September 1902). "The mechanism of pancreatic secretion". The Journal of Physiology. 28 (5): 325–353. doi:10.1113/jphysiol.1902.sp000920. PMC   1540572 . PMID   16992627.
  12. ↑ Hirst BH (October 2004). "Secretin and the exposition of hormonal control". The Journal of Physiology. 560 (Pt 2): 339. doi:10.1113/jphysiol.2004.073056. PMC   1665254 . PMID   15308687.
  13. ↑ Henriksen JH, Schaffalitzky de Muckadell OB (January 2002). "[Secretin--the first hormone]" [Secretin--the first hormone]. Ugeskrift for Laeger (in Danish). 164 (3): 320–325. PMID   11816326. INIST   13419424.
  14. ↑ Oliver G, Schäfer EA (July 1895). "The Physiological Effects of Extracts of the Suprarenal Capsules". The Journal of Physiology. 18 (3): 230–276. doi:10.1113/jphysiol.1895.sp000564. PMC   1514629 . PMID   16992252.
  15. ↑ Oliver G, Schäfer EA (July 1895). "The Physiological Effects of Extracts of the Suprarenal Capsules". The Journal of Physiology. 18 (3): 230–276. doi:10.1113/jphysiol.1895.sp000564. PMC   1514629 . PMID   16992252.
  16. ↑ Williams RL (1981). Textbook of Endocrinology. Philadelphia: Saunders. p.  697. ISBN   978-0-7216-9398-9.
  17. 1 2 DeGroot LJ (1989). McGuigan JE (ed.). Endocrinology. Philadelphia: Saunders. pp.  2748. ISBN   978-0-7216-2888-2.
  18. ↑ Polak JM, Coulling I, Bloom S, Pearse AG (1971). "Immunofluorescent localization of secretin and enteroglucagon in human intestinal mucosa". Scandinavian Journal of Gastroenterology. 6 (8): 739–744. doi:10.3109/00365527109179946. PMID   4945081.
  19. 1 2 Frohman LA, Felig P (2001). "Gastrointestinal Hormones and Carcinoid Syndrome". In Ghosh PK, O'Dorisio TM (eds.). Endocrinology & metabolism. New York: McGraw-Hill, Medical Pub. Div. pp. 1675–701. ISBN   978-0-07-022001-0.
  20. ↑ Ganong WF (2003). "Regulation of Gastrointestinal Function". Review of Medical Physiology (21st ed.). New York: McGraw-Hill, Medical Pub. Div. ISBN   978-0-07-140236-1.[ page needed ]
  21. ↑ Rominger JM, Chey WY, Chang TM (July 1981). "Plasma secretin concentrations and gastric pH in healthy subjects and patients with digestive diseases". Digestive Diseases and Sciences. 26 (7): 591–597. doi:10.1007/BF01367670. PMID   7249893. S2CID   7039025.
  22. 1 2 Hall JE, Guyton AC (2006). Textbook of medical physiology. St. Louis, Mo: Elsevier Saunders. pp. 800–1. ISBN   978-0-7216-0240-0.
  23. ↑ Gardner JD (1978). "Receptors and gastrointestinal hormones". In Sleisenger MH, Fordtran JS (eds.). Gastrointestinal Disease (2nd ed.). Philadelphia: WB Saunders Company. pp. 179–95.
  24. ↑ Osnes M, Hanssen LE, Flaten O, Myren J (March 1978). "Exocrine pancreatic secretion and immunoreactive secretin (IRS) release after intraduodenal instillation of bile in man". Gut. 19 (3): 180–184. doi:10.1136/gut.19.3.180. PMC   1411891 . PMID   631638.
  25. ↑ Palmer KR, Penman ID (2010). "Alimentary track and pancreatic disease". In Colledge NR, Walker BR, Ralston SH (eds.). Davidson's Principles and Practice of Medicine (20th ed.). Edinburgh: Churchill Livingstone. p. 844. ISBN   978-0-7020-3085-7.
  26. ↑ Boron WF, Boulpaep EL (2012). "Acid secretion". Medical Physiology (2nd ed.). Philadelphia: Saunders. p. 1352. ISBN   978-1-4377-1753-2.
  27. ↑ Kraegen EW, Chisholm DJ, Young JD, Lazarus L (March 1970). "The gastrointestinal stimulus to insulin release. II. A dual action of secretin". The Journal of Clinical Investigation. 49 (3): 524–529. doi:10.1172/JCI106262. PMC   322500 . PMID   5415678.
  28. ↑ Villanger O, Veel T, Raeder MG (March 1995). "Secretin causes H+/HCO3- secretion from pig pancreatic ductules by vacuolar-type H(+)-adenosine triphosphatase". Gastroenterology. 108 (3): 850–859. doi: 10.1016/0016-5085(95)90460-3 . PMID   7875488.
  29. ↑ Marinelli RA, Pham L, Agre P, LaRusso NF (May 1997). "Secretin promotes osmotic water transport in rat cholangiocytes by increasing aquaporin-1 water channels in plasma membrane. Evidence for a secretin-induced vesicular translocation of aquaporin-1". The Journal of Biological Chemistry. 272 (20): 12984–12988. doi: 10.1074/jbc.272.20.12984 . PMID   9148905.
  30. ↑ Chow BK, Cheung KH, Tsang EM, Leung MC, Lee SM, Wong PY (June 2004). "Secretin controls anion secretion in the rat epididymis in an autocrine/paracrine fashion". Biology of Reproduction. 70 (6): 1594–1599. doi:10.1095/biolreprod.103.024257. PMID   14749298. S2CID   1189550.
  31. ↑ Cheng CY, Chu JY, Chow BK (September 2009). "Vasopressin-independent mechanisms in controlling water homeostasis". Journal of Molecular Endocrinology. 43 (3): 81–92. doi: 10.1677/JME-08-0123 . PMID   19318428.
  32. ↑ Lee VH, Lee LT, Chu JY, Lam IP, Siu FK, Vaudry H, Chow BK (December 2010). "An indispensable role of secretin in mediating the osmoregulatory functions of angiotensin II". FASEB Journal. 24 (12): 5024–5032. doi:10.1096/fj.10-165399. PMC   2992369 . PMID   20739612.
  33. ↑ Cheng CY, Chu JY, Chow BK (January 2011). "Central and peripheral administration of secretin inhibits food intake in mice through the activation of the melanocortin system". Neuropsychopharmacology. 36 (2): 459–471. doi:10.1038/npp.2010.178. PMC   3055665 . PMID   20927047.
  34. ↑ Lieb JG, Draganov PV (May 2008). "Pancreatic function testing: here to stay for the 21st century". World Journal of Gastroenterology. 14 (20): 3149–3158. doi: 10.3748/WJG.14.3149 . PMC   2712845 . PMID   18506918.
  35. ↑ Domínguez Muñoz JE (June 2010). "Diagnosis of chronic pancreatitis: Functional testing". Best Practice & Research. Clinical Gastroenterology. 24 (3): 233–241. doi:10.1016/j.bpg.2010.03.008. PMID   20510825.
  36. ↑ "Secretin stimulation test". MedlinePlus Medical Encyclopedia. United States National Library of Medicine. Retrieved 2008-11-01.
  37. ↑ "Human Secretin". Patient Information Sheets. United States Food and Drug Administration. 2004-07-13. Archived from the original on May 11, 2009. Retrieved 2008-11-01.
  38. ↑ American Society of Health-System Pharmacists (5 August 2015). "Secretin Injection". Current Drug Shortage Bulletin. Archived from the original on 9 November 2016. Retrieved 9 November 2016.
  39. ↑ Stokstad E (18 July 2008). "News this Week: Stalled Trial for Autism Highlights Dilemma of Alternative Treatments". Science. p. 324.
  40. ↑ "The Use of Secretin to Treat Autism". NIH News Alert. United States National Institutes of Health. 1998-10-16. Retrieved 2008-11-30.
  41. ↑ Sandler AD, Sutton KA, DeWeese J, Girardi MA, Sheppard V, Bodfish JW (December 1999). "Lack of benefit of a single dose of synthetic human secretin in the treatment of autism and pervasive developmental disorder". The New England Journal of Medicine. 341 (24): 1801–1806. doi: 10.1056/NEJM199912093412404 . PMID   10588965.
  42. ↑ Dong M, Harikumar KG, Raval SR, Milburn JE, Clark C, Alcala-Torano R, et al. (July 2020). "Rational development of a high-affinity secretin receptor antagonist". Biochemical Pharmacology. 177: 113929. doi:10.1016/j.bcp.2020.113929. PMC   7299832 . PMID   32217097.

Further reading

This page is based on this Wikipedia article
Text is available under the CC BY-SA 4.0 license; additional terms may apply.
Images, videos and audio are available under their respective licenses.