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Secretin

William Y. Chey, Ta‐Min Chang

10.1002/cphy.cp060217

Source: Supplement 17: Handbook of Physiology, The Gastrointestinal System, Neural and Endocrine Biology

Originally published: 1989

Published online: January 2011

Full Article on Wiley Online Library



Abstract

The sections in this article are:

1 Discovery of Secretin
1.1 Historical Background
1.2 Isolation and Purification of Secretin
1.3 Structure, Chemical Properties, and Structure‐Activity Relationship
1.4 Synthesis of Secretin
2 Assay for Secretin
2.1 Bioassay of Secretin
2.2 Immunoassays
3 Distribution of Secretin‐Containing Cells
4 Physiology and Pharmacology of Secretin
4.1 Release of Secretin
4.2 Action of Secretin
4.3 Plasma Half‐Life and Catabolism of Secretin
4.4 Luminal Secretin and Its Biological Action
5 Mechanism of Action of Secretin
5.1 Mechanism in Pancreas
5.2 Mechanism on Stomach
6 Pathophysiology of Secretin
6.1 Hypersecretinemia
6.2 Hyposecretinemia
Figure 1. Figure 1.

Sequence of peptides or proteins of secretin family. SEC, secretin; VIP, vasoactive intestinal polypeptide; PHI, peptide histidine‐isoleucine amide; PHM, peptide histidine‐methionine amide; Glue, glucagon; GLP, glucagon‐like peptide; HSP‐I, helospectin‐I; HDM, helodermin; GIP, gastric inhibitory peptide; GRF, growth hormone‐releasing factor; Pre, prealbumin. *Indiates a COOH‐terminal amino acid amide. aPrefixes denote species: h, human; b, bovine; p, porcine; c, chicken. bChicken VIP differs by having S, F, V, and T COOH‐terminal amino acid amide at residues 11, 13, 26, and 28, respectively. cRat, rabbit, golden hamster, Arabian camel, and porcine glycentin33–61 have same sequence as human glucagon. Duck glucagon differs by having T at residue 16 and S at residue 28. Turkey and chicken glucagon differ by S at residue 28. Angler fish glucagon differs by having S, R, E, K, E, R, and N at residues 7, 8, 15, 18, 21, 24, and 29, respectively. dGlucagon‐like peptides are found to be encoded in structures of bovine, hamster, and angler fish preproglucagons with some differences in sequence. eHelospectin‐II differs from helospectin I by lacking COOH‐terminal amino acid of latter. fSequence of porcine, caprine, bovine, ovine, and rat GRF are now known; they differ from hGRF by 3–10 residues.
Figure 2. Figure 2.

Sequence specificity of antisecretin serum R‐1–6, determined by cross‐reaction study with various fragments of secretin and vesecretin, which is VIP‐1–12 linked to secretin‐12–27. ○, Natural porcine secretin; •, secretin‐1–12; □, secretin‐14–27; ▄, secretin‐4–27; Δ, vesecretin.
Figure 3. Figure 3.

Ion‐exchange chromatogram of secretin from various sources. Upper panel, natural porcine secretin; lower panel, synthetic porcine secretin from Peninsula Laboratories. Synthetic secretin from following sources exhibited similar chromatograms to one shown in upper panel: Sigma, Cambridge, Squibb, Dr. Coy 112), and Professor Beyerman 30).
Figure 4. Figure 4.

Secretin cells in canine duodenal mucosa stained by peroxidase‐antiperoxidase (PAP) staining method. A, × 530; B, × 1,400.
Figure 5. Figure 5.

Mean values of plasma secretin concentration and pancreatic bicarbonate output in response to intraduodenal infusion of 0.05 N HCl (1.1 ml/min) with and without concomitant intravenous administration of deoxyglucose (2‐DG) (mg · kg−1 · h−1) in 4 dogs with pancreatic fistula. Values are means ± SE of 8 experiments (2 experiments per dog). Statistical significance of differences from control value expressed as ▴, P < 0.001; •, P < 0.01.

From Chey et al. 87
Figure 6. Figure 6.

Linear relationship between acid load in duodenum and increment in plasma secretin concentration. In 5 dogs with intraduodenal infusion of HCl, increase in plasma secretin concentration is compared with acid load in duodenum by linear regression analysis. •, Mean values.

From Chen et al. 82
Figure 7. Figure 7.

Effect of liver extract (LE) meals adjusted to various pH values on plasma immunoreactive secretin concentration and pancreatic bicarbonate secretion. Values are means ± SE of 2 tests on each of 5 dogs.

From Chey and Konturek 90
Figure 8. Figure 8.

Effectiveness of various foodstuffs in stimulating volume secretion of transplanted pancreas in 6 dogs (secretin effect). Bars are arranged in groups of 3 representing 3 consecutive 20‐min collection periods after administration of substances indicated above each group.

From Wang and Grossman 487
Figure 9. Figure 9.

Plasma secretin concentrations in response to intraduodenal Lipomul in 7 dogs with chronic pancreatic fistulas. Lipomul, 15 mmol, was infused under 2 experimental conditions of diversion or intraduodenal reinfusion of pancreatic juice or saline at a rate of 2 ml/min for 10 min. Values are means ± SE from 7 dogs.

From Watanabe et al. 489
Figure 10. Figure 10.

The pH profile of duodenum at 3 different levels and plasma secretin concentration in 4 dogs in which a 5% liver extract (LE) meal with pH adjusted by intragastric titration to 6.0, 4.0, and 2.0 was infused in stomach. Values are means obtained from 4 dogs with 3 implanted pH electrodes in duodenum and gastric cannula.

From W. Y. Chey, H. J. Park, and K. Y. Lee, unpublished data
Figure 11. Figure 11.

Plasma secretin concentrations after standard meat meal in 30 healthy subjects and during intravenous infusion of 0.03 CU · kg−1 · h−1 (2.8 pmol · kg−1 · h−1) of GIH secretin, dissolved in 0.2% albumin, in 15 healthy subjects. Two separate groups of volunteers are comparable in age and sex. Meat meal was given at time zero. Secretin was administered intravenously 60 min after intravenous infusion of saline. Shaded area, means ± SE of plasma secretin concentration after meal. Each point and bar represent mean ± SE.

From You et al. 517
Figure 12. Figure 12.

Pancreatic bicarbonate outputs (means ± SE) in response to intravenous secretin alone in 3 graded doses and intravenous secretin plus intravenous atropine in 5 subjects. Symbols represent statistical significance of difference between values of each corresponding time period of 2 experiments.

From You et al. 516
Figure 13. Figure 13.

Effect of rabbit antisecretin serum on plasma immunoreactive secretin concentrations in response to meat meal. Values are means ± SE of 4 experiments in 4 dogs with pancreatic fistula. Solid line, values obtained during intravenous administration of normal rabbit serum; dashed line, those during administration of antisecretin serum.

From Chey et al. 88
Figure 14. Figure 14.

Effects of normal rabbit serum (solid line) and anti‐secretin serum (dashed line) on concentration and output of pancreatic bicarbonate in response to meat meal. Values represent means ± SE of 9 experiments in 9 dogs with pancreatic fistula.

From Chey et al. 88
Figure 15. Figure 15.

Pancreatic bicarbonate output in response to graded doses of CCK‐8 with or without secretin background in dose of 0.03 CU · kg−1 · h−1 (2.8 pmol · kg−1 · h−1). •, Bicarbonate output produced by simultaneous infusion of secretin and varying doses of CCK‐8; □, calculated sum of bicarbonate output produced by 2 individual hormones; ○, bicarbonate output produced by varying doses of CCK‐8 alone. Points with vertical bars represent means ± SE of 5 subjects.

From You et al. 517
Figure 16. Figure 16.

Effects of normal rabbit serum or rabbit antisecretin serum on plasma immunoreactive gastrin concentrations in 4 dogs. Values are means ± SE of 8 experiments in 4 dogs.

From Chey et al. 89
Figure 17. Figure 17.

Effects of intravenous secretin (0.06 and 0.125 U · kg−1 · h−1) on acid secretion from main stomach stimulated by human synthetic gastrin (0.125 and 0.25 μg · kg−1 · h−1). Values are means ± SE of 8 experiments in 4 dogs.

From Chey et al. 89
Figure 18. Figure 18.

Effects of glucagon, secretin, and VIP on gastric somatostatin and gastrin release in isolated perfused rat stomach. After preperfusion for 20 min, all peptides were infused for 15 min at concentrations of 0, 10−8, 10−7, and 10−6 M, respectively, from lowest to highest curve in upper panel and from highest to lowest curves in lower panel. Values are means ± SE.

From Chiba et al. 101
Figure 19. Figure 19.

Plasma half time of secretin determined immediately after 1‐h intravenous infusion of secretin in 8 control subjects and in 7 patients with chronic renal failure. Equilibrium concentration equaled plasma secretin increment over basal at end of 1‐h infusion. All values were normalized so that equilibrium concentration was 100% in each subject. Half times were calculated from elimination constants obtained by linear regression analysis of natural logarithms of mean normalized concentration versus time.

From Chey et al. 98
Figure 20. Figure 20.

Fasting plasma secretin concentrations of normal subjects, patients with duodenal ulcers (DUs), Zollinger‐Ellison syndrome (ZES), and chronic renal failure (CRF).

From Chey et al. 98


Figure 1.

Sequence of peptides or proteins of secretin family. SEC, secretin; VIP, vasoactive intestinal polypeptide; PHI, peptide histidine‐isoleucine amide; PHM, peptide histidine‐methionine amide; Glue, glucagon; GLP, glucagon‐like peptide; HSP‐I, helospectin‐I; HDM, helodermin; GIP, gastric inhibitory peptide; GRF, growth hormone‐releasing factor; Pre, prealbumin. *Indiates a COOH‐terminal amino acid amide. aPrefixes denote species: h, human; b, bovine; p, porcine; c, chicken. bChicken VIP differs by having S, F, V, and T COOH‐terminal amino acid amide at residues 11, 13, 26, and 28, respectively. cRat, rabbit, golden hamster, Arabian camel, and porcine glycentin33–61 have same sequence as human glucagon. Duck glucagon differs by having T at residue 16 and S at residue 28. Turkey and chicken glucagon differ by S at residue 28. Angler fish glucagon differs by having S, R, E, K, E, R, and N at residues 7, 8, 15, 18, 21, 24, and 29, respectively. dGlucagon‐like peptides are found to be encoded in structures of bovine, hamster, and angler fish preproglucagons with some differences in sequence. eHelospectin‐II differs from helospectin I by lacking COOH‐terminal amino acid of latter. fSequence of porcine, caprine, bovine, ovine, and rat GRF are now known; they differ from hGRF by 3–10 residues.



Figure 2.

Sequence specificity of antisecretin serum R‐1–6, determined by cross‐reaction study with various fragments of secretin and vesecretin, which is VIP‐1–12 linked to secretin‐12–27. ○, Natural porcine secretin; •, secretin‐1–12; □, secretin‐14–27; ▄, secretin‐4–27; Δ, vesecretin.



Figure 3.

Ion‐exchange chromatogram of secretin from various sources. Upper panel, natural porcine secretin; lower panel, synthetic porcine secretin from Peninsula Laboratories. Synthetic secretin from following sources exhibited similar chromatograms to one shown in upper panel: Sigma, Cambridge, Squibb, Dr. Coy 112), and Professor Beyerman 30).



Figure 4.

Secretin cells in canine duodenal mucosa stained by peroxidase‐antiperoxidase (PAP) staining method. A, × 530; B, × 1,400.



Figure 5.

Mean values of plasma secretin concentration and pancreatic bicarbonate output in response to intraduodenal infusion of 0.05 N HCl (1.1 ml/min) with and without concomitant intravenous administration of deoxyglucose (2‐DG) (mg · kg−1 · h−1) in 4 dogs with pancreatic fistula. Values are means ± SE of 8 experiments (2 experiments per dog). Statistical significance of differences from control value expressed as ▴, P < 0.001; •, P < 0.01.

From Chey et al. 87


Figure 6.

Linear relationship between acid load in duodenum and increment in plasma secretin concentration. In 5 dogs with intraduodenal infusion of HCl, increase in plasma secretin concentration is compared with acid load in duodenum by linear regression analysis. •, Mean values.

From Chen et al. 82


Figure 7.

Effect of liver extract (LE) meals adjusted to various pH values on plasma immunoreactive secretin concentration and pancreatic bicarbonate secretion. Values are means ± SE of 2 tests on each of 5 dogs.

From Chey and Konturek 90


Figure 8.

Effectiveness of various foodstuffs in stimulating volume secretion of transplanted pancreas in 6 dogs (secretin effect). Bars are arranged in groups of 3 representing 3 consecutive 20‐min collection periods after administration of substances indicated above each group.

From Wang and Grossman 487


Figure 9.

Plasma secretin concentrations in response to intraduodenal Lipomul in 7 dogs with chronic pancreatic fistulas. Lipomul, 15 mmol, was infused under 2 experimental conditions of diversion or intraduodenal reinfusion of pancreatic juice or saline at a rate of 2 ml/min for 10 min. Values are means ± SE from 7 dogs.

From Watanabe et al. 489


Figure 10.

The pH profile of duodenum at 3 different levels and plasma secretin concentration in 4 dogs in which a 5% liver extract (LE) meal with pH adjusted by intragastric titration to 6.0, 4.0, and 2.0 was infused in stomach. Values are means obtained from 4 dogs with 3 implanted pH electrodes in duodenum and gastric cannula.

From W. Y. Chey, H. J. Park, and K. Y. Lee, unpublished data


Figure 11.

Plasma secretin concentrations after standard meat meal in 30 healthy subjects and during intravenous infusion of 0.03 CU · kg−1 · h−1 (2.8 pmol · kg−1 · h−1) of GIH secretin, dissolved in 0.2% albumin, in 15 healthy subjects. Two separate groups of volunteers are comparable in age and sex. Meat meal was given at time zero. Secretin was administered intravenously 60 min after intravenous infusion of saline. Shaded area, means ± SE of plasma secretin concentration after meal. Each point and bar represent mean ± SE.

From You et al. 517


Figure 12.

Pancreatic bicarbonate outputs (means ± SE) in response to intravenous secretin alone in 3 graded doses and intravenous secretin plus intravenous atropine in 5 subjects. Symbols represent statistical significance of difference between values of each corresponding time period of 2 experiments.

From You et al. 516


Figure 13.

Effect of rabbit antisecretin serum on plasma immunoreactive secretin concentrations in response to meat meal. Values are means ± SE of 4 experiments in 4 dogs with pancreatic fistula. Solid line, values obtained during intravenous administration of normal rabbit serum; dashed line, those during administration of antisecretin serum.

From Chey et al. 88


Figure 14.

Effects of normal rabbit serum (solid line) and anti‐secretin serum (dashed line) on concentration and output of pancreatic bicarbonate in response to meat meal. Values represent means ± SE of 9 experiments in 9 dogs with pancreatic fistula.

From Chey et al. 88


Figure 15.

Pancreatic bicarbonate output in response to graded doses of CCK‐8 with or without secretin background in dose of 0.03 CU · kg−1 · h−1 (2.8 pmol · kg−1 · h−1). •, Bicarbonate output produced by simultaneous infusion of secretin and varying doses of CCK‐8; □, calculated sum of bicarbonate output produced by 2 individual hormones; ○, bicarbonate output produced by varying doses of CCK‐8 alone. Points with vertical bars represent means ± SE of 5 subjects.

From You et al. 517


Figure 16.

Effects of normal rabbit serum or rabbit antisecretin serum on plasma immunoreactive gastrin concentrations in 4 dogs. Values are means ± SE of 8 experiments in 4 dogs.

From Chey et al. 89


Figure 17.

Effects of intravenous secretin (0.06 and 0.125 U · kg−1 · h−1) on acid secretion from main stomach stimulated by human synthetic gastrin (0.125 and 0.25 μg · kg−1 · h−1). Values are means ± SE of 8 experiments in 4 dogs.

From Chey et al. 89


Figure 18.

Effects of glucagon, secretin, and VIP on gastric somatostatin and gastrin release in isolated perfused rat stomach. After preperfusion for 20 min, all peptides were infused for 15 min at concentrations of 0, 10−8, 10−7, and 10−6 M, respectively, from lowest to highest curve in upper panel and from highest to lowest curves in lower panel. Values are means ± SE.

From Chiba et al. 101


Figure 19.

Plasma half time of secretin determined immediately after 1‐h intravenous infusion of secretin in 8 control subjects and in 7 patients with chronic renal failure. Equilibrium concentration equaled plasma secretin increment over basal at end of 1‐h infusion. All values were normalized so that equilibrium concentration was 100% in each subject. Half times were calculated from elimination constants obtained by linear regression analysis of natural logarithms of mean normalized concentration versus time.

From Chey et al. 98


Figure 20.

Fasting plasma secretin concentrations of normal subjects, patients with duodenal ulcers (DUs), Zollinger‐Ellison syndrome (ZES), and chronic renal failure (CRF).

From Chey et al. 98
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Article Title: Secretin
 

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William Y. Chey, Ta‐Min Chang. Secretin. Compr Physiol 2011, Supplement 17: Handbook of Physiology, The Gastrointestinal System, Neural and Endocrine Biology: 359-402. First published in print 1989. doi: 10.1002/cphy.cp060217