Dual inhibitory mechanism of secretin action on acid secretion in totally isolated, vascularly perfused rat stomach

Chung, In‐Sik; Li, Ping; Lee, Kaeyol; Chang, Ta‐Min; Chey, William Y.

doi:10.1016/0016-5085(94)90817-6

Cited by 23 publications

(16 citation statements)

References 41 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…the enterogastrone effect of secretin in vivo is abolished by administration of an anti-somatostatin antiserum (42). As S14 potently inhibits acid secretion by the parietal cell (43), the results of the present study lend support to the concept of a feedback loop between the proximal intestine and the parietal cell through secretin-mediated S14 release.…”

Section: Discussionsupporting

confidence: 72%

Nutrient and Peptide Regulation of Somatostatin-28 Secretion from Intestinal Cultures¹

Brubaker

Gronau²,

Sylvia

et al. 1998

Endocrinology

View full text Add to dashboard Cite

Of the two known forms of intestinal somatostatin, somatostatin-28 (S28) and S14, S28 predominates in the distal mucosa, whereas S14 is localized in the foregut. Although S14 release has been well studied, little is known about the factors regulating secretion of S28 from the intestine. Therefore, fetal rat intestinal cultures, which have been previously demonstrated to synthesize and secrete predominantly S28, were treated with potential nutrient, neuromodulator/ transmitter, and peptide secretagogues (n ϭ 4 -6/experiment). Oleic acid dose dependently stimulated the release of somatostatin-like immunoreactivity (SLI) to 272 Ϯ 81% of the control value at 1.5 ϫ 10 Ϫ4 M (P Ͻ 0.01). Gel permeation analysis (n ϭ 3) demonstrated that this increment was accounted for not only by an increase in the release of S28, but also by an increase in that of S14, such that the secretion of both peptides was increased in parallel. Of the neuromodulators tested, only the enteric peptide gastrin-releasing peptide stimulated intestinal SLI secretion, to 386 Ϯ 60% of the control value at 10 Ϫ6 M (P Ͻ 0.001); similar to oleic acid, the effects on S28 and S14 were equivalent. Galanin, vasoactive intestinal peptide, bethanechol, and epinephrine did not affect SLI release. The duodenal hormone secretin also stimulated SLI release to 310 Ϯ 78% of the control value at 10 Ϫ6 M (P Ͻ 0.001); however, secretin caused a preferential release of S14 over that of S28 (S14, 7.8 Ϯ 2.8-fold; S28, 1.5 Ϯ 0.1-fold). In contrast, gastrin, cholecystokinin, glucose-dependent insulinotropic peptide, neurotensin, peptide YY, epidermal growth factor, and transforming growth factor-␣ had no effect on intestinal SLI release. Thus, luminal nutrients and neuro/endocrine peptides exert differential effects on S28 release from the rat intestine compared with those on S14. These findings implicate S28 as a distinct regulatory peptide in the physiological setting. (Endocrinology 139: 148 -155, 1998) A LTHOUGH widely distributed in the brain, pancreas, and peripheral autonomic nervous system, the gastrointestinal tract provides the largest source of somatostatin in the periphery (1-3). Within the gastrointestinal tract, differential posttranslational processing of prosomatostatin generates two major biologically active peptides, somatostatin-14 (S14) and S28, the distribution of which forms a gradient along the aboral axis. In the mucosa of the stomach and duodenum, S14 is the major product of processing, whereas S28 predominates in the D cells of the distal jejunum and ileum (1-4). S14 is also distributed throughout the length of the small intestine within the myenteric plexi. Both peptides have potent inhibitory effects on digestive functions, including gastric and pancreatic exocrine secretion, neuro/endocrine peptide release, and intestinal growth (5). Of particular note are studies suggesting that S28, rather than S14, may be the physiological regulator of postprandial insulin secretion in humans (6, 7). Although regulation of S14 secretion from the st...

show abstract

Section: Discussionsupporting

confidence: 72%

Nutrient and Peptide Regulation of Somatostatin-28 Secretion from Intestinal Cultures¹

Brubaker

Gronau²,

Sylvia

et al. 1998

Endocrinology

View full text Add to dashboard Cite

show abstract

“…8) or a meal. 34 In both isolated and perfused rat stomach 35 and the intact animals, 36 it has been clearly shown that inhibition of gastric acid secretion by secretin is mediated by somatostatin and prostaglandin.…”

Section: Physiological Actions Of Secretinmentioning

confidence: 98%

Secretin, 100 years later

Chey¹,

Chang²

2003

Journal of Gastroenterology

Self Cite

106

View full text Add to dashboard Cite

One hundred years have elapsed since the discovery of secretin by Bayliss and Starling in 1902. In the past century, the research of secretin has gone by many milestones including isolation, purification and structural determination, chemical synthesis, establishment of its hormonal status by radioimmunoassay and immunoneutralization, identification of the specific receptor, cloning of secretin and its receptor, and identification of a secretin-releasing peptide. It has become clear that secretin is a hormone-regulating pancreatic exocrine secretion of fluid and bicarbonate, gastric acid secretion, and gastric motility. The release and actions of secretin is regulated by hormone-hormonal and neurohormonal interactions. The vagus nerve, particularly its afferent pathway, plays an essential role in the physiological actions of secretin. Substantial information about the property of the secretin receptor has been accumulated, but a potent secretin receptor-specific antagonist remains to be formulated. The neural regulatory mechanisms of the release and action of secretin await further elucidation. The physiological role of secretin in intestinal secretions and motility and extragastrointestinal organs remains to be defined. The presence of secretin and its receptor in the central nervous system is well documented, but its function as a neuropeptide has been recognized gradually and requires extensive study in the future.

show abstract

“…In humans (Dinoso et al 1969) and dogs (Chey et al 1981), secretin was reported to delay gastric emptying by inhibiting the gastric motility, in which the contraction force of the antrum is reduced by secretin. Apart from that, secretin was reported to significantly increase endogenous somatostatin in perfused rat (Chung et al 1994) and dog stomachs (Gerber & Payne 1996). Furthermore, secretin stimulates pepsin secretion in dogs and cats (Magee & Nakajima 1968, Stening et al 1969.…”

Section: Secretin Serves As a Gastrointestinal Hormone In Both Nonmammentioning

confidence: 99%

MOLECULAR EVOLUTION OF GPCRS: Secretin/secretin receptors

Tam

Lee

Jin

et al. 2014

Journal of Molecular Endocrinology

View full text Add to dashboard Cite

In mammals, secretin is a 27-amino acid peptide that was first studied in 1902 by Bayliss and Starling from the extracts of the jejunal mucosa for its ability to stimulate pancreatic secretion. To date, secretin has only been identified in tetrapods, with the earliest diverged secretin found in frogs. Despite being the first hormone discovered, secretin's evolutionary origin remains enigmatic, it shows moderate sequence identity in nonmammalian tetrapods but is highly conserved in mammals. Current hypotheses suggest that although secretin has already emerged before the divergence of osteichthyans, it was lost in fish and retained only in land vertebrates. Nevertheless, the cognate receptor of secretin has been identified in both actinopterygian fish (zebrafish) and sarcopterygian fish (lungfish). However, the zebrafish secretin receptor was shown to be nonbioactive. Based on the present information that the earliest diverged bioactive secretin receptor was found in lungfish, and its ability to interact with both vasoactive intestinal peptide and pituitary adenylate cyclase-activating polypeptide potently suggested that secretin receptor was descended from a VPAC-like receptor gene before the Actinopterygii-Sarcopterygii split in the vertebrate lineage. Hence, secretin and secretin receptor have gone through independent evolutionary trajectories despite their concurrent emergence post-2R. A functional secretin-secretin receptor axis has probably emerged in the amphibians. Although the pleiotropic actions of secretin are well documented in the literature, only limited information of its physiological functions in nonmammalian tetrapods have been reported. To decipher the structural and functional divergence of secretin and secretin receptor, functional characterization of the ligandreceptor pair in nonmammals would be the next perspective for investigation.

show abstract

Dual inhibitory mechanism of secretin action on acid secretion in totally isolated, vascularly perfused rat stomach

Cited by 23 publications

References 41 publications

Nutrient and Peptide Regulation of Somatostatin-28 Secretion from Intestinal Cultures¹

Nutrient and Peptide Regulation of Somatostatin-28 Secretion from Intestinal Cultures¹

Secretin, 100 years later

MOLECULAR EVOLUTION OF GPCRS: Secretin/secretin receptors

Contact Info

Product

Resources

About

Dual inhibitory mechanism of secretin action on acid secretion in totally isolated, vascularly perfused rat stomach

Cited by 23 publications

References 41 publications

Nutrient and Peptide Regulation of Somatostatin-28 Secretion from Intestinal Cultures1

Nutrient and Peptide Regulation of Somatostatin-28 Secretion from Intestinal Cultures1

Secretin, 100 years later

MOLECULAR EVOLUTION OF GPCRS: Secretin/secretin receptors

Contact Info

Product

Resources

About

Nutrient and Peptide Regulation of Somatostatin-28 Secretion from Intestinal Cultures¹

Nutrient and Peptide Regulation of Somatostatin-28 Secretion from Intestinal Cultures¹