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Comparative Neuroendocrinology of Gut Peptides

G. J. Dockray

10.1002/cphy.cp060208

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 General and Comparative Aspects of Organization
1.1 Cellular Origins
1.2 Molecular Aspects
1.3 Target Tissues
2 Experimental Approaches
3 Gastrin‐CCK
3.1 Sequences and Genes
3.2 Distribution
3.3 Biological Properties
4 VIP/Secretin Family
4.1 Sequences and Genes
4.2 VIP and PHI
4.3 Glucagon
4.4 Secretin
4.5 GIP
4.6 GH‐RF
4.7 Helodermin and Helospectins
4.8 Distribution
4.9 Biological Actions
5 Bombesins
5.1 Sequences and Genes
5.2 Distribution
5.3 Biological Properties
6 Tachykinins
6.1 Sequences and Genes
6.2 Distribution
6.3 Biological Properties
7 Pancreatic Polypeptide Family
7.1 Sequences and Genes
7.2 Distribution
7.3 Biological Properties
8 Opioid Peptides
8.1 Sequences and Genes
8.2 Distribution
8.3 Biological Properties
9 Neurotensin
9.1 Sequences
9.2 Distribution and Actions
10 Somatostatin
10.1 Sequences and Genes
10.2 Distribution
10.3 Biological Properties
11 Invertebrate Peptides
11.1 Hydra Head Activator Peptide
11.2 FMRF‐Amide
11.3 Other Molluscan Cardioactive Peptides: SCP and LCP
11.4 Proctolin
11.5 Adipokinetic Hormone
12 Overview
Figure 1. Figure 1.

Schematic representation of biosynthetic precursors of cholecystokinin (CCK), gastrin, and caerulein as deduced from cDNA sequencing. Crosshatched area indicates common pentapeptide sequence (Gly‐Trp‐Met‐Asp‐Phe); note 2 copies in preprocaerulein and 1 each in preprogastrin and preproCCK. Stippled areas indicate signal peptides; only a partial sequence is available for preprocaerulein, and signal region is thus far unidentified. Arrows indicate likely sites of cleavage in posttranslational processing; these are at pairs of basic residues in preprogastrin and preprocaerulein and at single arginine residues in proCCK; the additional action of dipeptidyl aminopeptidase is needed to generate caerulein.
Figure 2. Figure 2.

Amino acid sequences of regions of progastrin, proCCK, and procaerulein giving rise to COOH terminus of biologically active peptides. Cleavage occurs at pairs of Arg, and the adjacent Gly is a substrate for generation of Phe‐amide. Note the conserved tripeptide Ser‐Ala‐Glu in progastrin and proCCK, which forms the NH2‐terminal sequence of flanking peptide liberated by cleavage. Elsewhere there are other similarities between progastrin and proCCK but little similarity with procaerulein. The progastrin sequence is common to human and pig, and proCCK sequence is common to rat, mouse, pig, and human. Procaerulein is from Xenopus.
Figure 3. Figure 3.

Inhibition of acid secretion in the cod Gadus morhua by G‐17, given intramuscularly in doses of 1 and 5 μg · kg−1 · h−1. Sulfated G‐17, CCK‐8, and caerulein also inhibit acid secretion, but pentagastrin stimulated acid secretion.

From Holstein 172
Figure 4. Figure 4.

Protein secretion in gut lumen in protochordate Styela clava in response to sulfated (○) and unsulfated (•) CCK‐8 infused into vascular supply. Both peptides increase protein secretion into lumen and were approximately equipotent. Effects of CCK were inhibited by antagonist dibutyryl GMP. Structurally unrelated peptides, physalaemin and bombesin, also stimulate protein secretion in this preparation.

From Thorndyke and Bevis 354
Figure 5. Figure 5.

Inhibition of binding of 125I‐labeled CCK‐33 to membrane preparations of bullfrog pancreas and brain in vitro (22°C, 3 h). Sulfated G‐17 was ˜10 times less potent than sulfated CCK‐8 in both tissues, but unsulfated peptides were 100–1,000 times less active than their sulfated counterparts. There was no difference in rank order of potency in sulfated and unsulfated forms of gastrin and CCK in frog brain and pancreas. In contrast, in mammals the pancreatic receptors discriminate much more than do brain receptors for sulfated CCK‐8 compared with sulfated G‐17.

From Williams et al. 383
Figure 6. Figure 6.

Schematic representation of organization of precursor for human and rat vasoactive intestinal polypeptide (VIP)/PHI; hamster, bovine, and human glucagon; and anglerfish glucagon. Note additional glucagon‐like peptide in anglerfish and 2 in mammalian precursors.
Figure 7. Figure 7.

Amino acid sequences, aligned from NH2 terminus, of representatives of VIP‐secretin family in single‐letter notation. Sequence of porcine VIP is shown; dash indicates residue identical to that in porcine VIP. Similar sequences have been found for human, bovine, and rat VIP; guinea pig has Leu5, Thr9, Met19, and Val21. Sequence of porcine PHI shown here differs from human, which has Lys12 and Met28, and rat (Tyr10, He17). Porcine and bovine secretin have sequence shown here, but human is Glu15Gly16. Porcine glucagon is shown; similar sequences have been found in all other mammals studied except guinea pig (Glu21, Leu23, Lys24, Leu27, and Val19). Partial sequences (1–29) are shown of human growth hormone‐releasing factor (GH‐RF) (44 residues), hamster glucagon‐like peptide (GLP)‐I (37 residues), hamster GLP‐II (35 residues), porcine glucose‐dependent insulinotropic peptide (GIP) (42 residues), helospectin (35 residues), helodermin (38 residues), and anglerfish GLP (31 residues). Human GIP differs in His18 and Asn24, and bovine GIP has He37. Human GH‐RF differs from rat in 14 positions. Asterisk indicates that there are 6 residues to NH2 terminus of hamster GLP‐I that are not shown (His‐Asp‐Glu‐Phe‐Glu‐Arg). Bovine and human GLP are identical to hamster GLP‐I; bovine and human GLP‐II differ in 3 and 2 residues, respectively, from corresponding hamster peptide. Avian peptides are all of chicken origin. Duck glucagon has Thr for Ser at 16 and Ser for Asn at 28; turkey glucagon also has Ser for Asn at 28. The anglerfish glucagon I is shown; glucagon II in anglerfish differs at Thr16, Arg18, Asp21, Glu24, Lys27, and Ser29. Catfish glucagon is identical to anglerfish glucagon II. Anglerfish GLP from proglucagon I is shown. Corresponding peptide from proglucagon II differs in 7 positions. Catfish GLP differs in 7 residues from anglerfish I.
Figure 8. Figure 8.

Stimulation of flow of juice and protein output from pancreas in the urethane‐anesthetized turkey in response to intravenous injections of chicken VIP, chicken secretin, and porcine secretin. Note greater potency of VIP in stimulating flow of juice. Chicken and porcine VIP are of similar potencies. Porcine secretin is a weak stimulant of avian pancreas but strong stimulant in mammals. Chicken secretin is a weak stimulant in both birds and mammals. None of the peptides strongly stimulates protein output.

From Dimaline and Dockray 79
Figure 9. Figure 9.

Inhibition of acid secretion in cod by VIP and stimulation by bombesin.

From Holstein and Humphrey 175
Figure 10. Figure 10.

Amino acid sequence of bombesin/GRP group of peptides. In both mammals and amphibians 2 subgroups can be identified, depending on residue in penultimate position: either Leu (bombesin or GRP) or Phe (litorin and neuromedin B).
Figure 11. Figure 11.

Amino acid sequence of tachykinins from mammals, amphibian skin and gut, and salivary gland of octopus. In mammals there are 3 peptides, 2 of which (substance P and substance K) share common precursor. Substance K is also known as neuromedin L and neurokinin‐α; neurokinin B is also known as neuromedin K. Sequence Phe‐X‐Gly‐Leu‐Met‐NH2 is common to all except enterohylambatin, which has penultimate Met.
Figure 12. Figure 12.

Action of substance P (SP) in contracting trout stomach. Response is blocked by tetrodotoxin (TTX) (A) but resistant to atropine (ATR) and phentolamine (PHENT) (S); serotonin (5‐HT) also contracts stomach (C). Serotonin antagonist methysergide (METH) blocked action of both serotonin and substance P, suggesting the latter acts through serotonin release. There is also direct evidence that substance P releases serotonin from perfused trout stomach.

From Holmgren et al. 166), © 1985, with permission from Pergamon Press, Ltd
Figure 13. Figure 13.

Pancreatic polypeptide (PP) family in single‐letter notation. All the peptides are 36 residues and COOH‐terminally amidated except anglerfish PP, which is 37 and COOH‐terminal Gly. This would normally be a substrate for conversion to COOH‐terminal amide. There are 3 members in mammals (PP, NPY, and PYY). Note NPY resembles anglerfish APY and avian PP more closely than mammalian PP. Porcine NPY has Leu in place of Met at position 17. Following residues are common to all peptides: Pro5, Pro8, Gly9, Ala12, Glu15, Tyr27, Arg23, Arg35.
Figure 14. Figure 14.

Amino acid sequences of neurotensin family in single‐letter notation. In birds and mammals, there are 2 peptides, tridecepeptide and hexapeptide, that share a COOH‐terminal tetrapeptide sequence. Two peptides also occur in chicken.
Figure 15. Figure 15.

Somatostatin‐related peptides. Tetradecapeptide somatostatin‐14 corresponds to COOH‐terminus of somatostatin‐28. It is strongly conserved and occurs in identical form in teleosts, elasmobranchs, birds, and mammals. In addition, in teleosts there are several related peptides, including the urotensins II, 22‐residue somatostatin, and 28‐residue somatostatin. Angler‐fish somatostatin II is shown; asterisk indicates Hyl at position 6 from COOH terminus. In anglerfish somatostatin I, COOH‐terminal tetradecapeptide is identical to mammalian sequence, but there are 6 substitutions in first 14 positions. Sequence shown for somatostatin‐22 is that reported by Andrews et al. 12) and agrees with that deduced from cDNA sequencing 239); it differs from that reported by Oyama et al. 283) in Thr for Arg at position 5 and Arg for Ser at position 19. Several teleost urotensins II are known, including 3 in carp. Hexapeptide C‐F‐W‐K‐Y‐C is common to all of them. In all members of family, Cys residues are joined by disulfide bridge.
Figure 16. Figure 16.

Contraction of cockroach protodeum in response to serotonin (5‐HT), stomodermal nerve stimulation, and proctolin. Glutamate was only weakly active. Tetrodotoxin blocked effect of nerve stimulation but not proctolin or serotonin. However, serotonin antagonists were shown to block effect of serotonin but not proctolin or nerve stimulation, suggesting that proctolin might be neurotransmitter in this system.

From Brown 40), © 1975, with permission from Pergamon Press, Ltd


Figure 1.

Schematic representation of biosynthetic precursors of cholecystokinin (CCK), gastrin, and caerulein as deduced from cDNA sequencing. Crosshatched area indicates common pentapeptide sequence (Gly‐Trp‐Met‐Asp‐Phe); note 2 copies in preprocaerulein and 1 each in preprogastrin and preproCCK. Stippled areas indicate signal peptides; only a partial sequence is available for preprocaerulein, and signal region is thus far unidentified. Arrows indicate likely sites of cleavage in posttranslational processing; these are at pairs of basic residues in preprogastrin and preprocaerulein and at single arginine residues in proCCK; the additional action of dipeptidyl aminopeptidase is needed to generate caerulein.



Figure 2.

Amino acid sequences of regions of progastrin, proCCK, and procaerulein giving rise to COOH terminus of biologically active peptides. Cleavage occurs at pairs of Arg, and the adjacent Gly is a substrate for generation of Phe‐amide. Note the conserved tripeptide Ser‐Ala‐Glu in progastrin and proCCK, which forms the NH2‐terminal sequence of flanking peptide liberated by cleavage. Elsewhere there are other similarities between progastrin and proCCK but little similarity with procaerulein. The progastrin sequence is common to human and pig, and proCCK sequence is common to rat, mouse, pig, and human. Procaerulein is from Xenopus.



Figure 3.

Inhibition of acid secretion in the cod Gadus morhua by G‐17, given intramuscularly in doses of 1 and 5 μg · kg−1 · h−1. Sulfated G‐17, CCK‐8, and caerulein also inhibit acid secretion, but pentagastrin stimulated acid secretion.

From Holstein 172


Figure 4.

Protein secretion in gut lumen in protochordate Styela clava in response to sulfated (○) and unsulfated (•) CCK‐8 infused into vascular supply. Both peptides increase protein secretion into lumen and were approximately equipotent. Effects of CCK were inhibited by antagonist dibutyryl GMP. Structurally unrelated peptides, physalaemin and bombesin, also stimulate protein secretion in this preparation.

From Thorndyke and Bevis 354


Figure 5.

Inhibition of binding of 125I‐labeled CCK‐33 to membrane preparations of bullfrog pancreas and brain in vitro (22°C, 3 h). Sulfated G‐17 was ˜10 times less potent than sulfated CCK‐8 in both tissues, but unsulfated peptides were 100–1,000 times less active than their sulfated counterparts. There was no difference in rank order of potency in sulfated and unsulfated forms of gastrin and CCK in frog brain and pancreas. In contrast, in mammals the pancreatic receptors discriminate much more than do brain receptors for sulfated CCK‐8 compared with sulfated G‐17.

From Williams et al. 383


Figure 6.

Schematic representation of organization of precursor for human and rat vasoactive intestinal polypeptide (VIP)/PHI; hamster, bovine, and human glucagon; and anglerfish glucagon. Note additional glucagon‐like peptide in anglerfish and 2 in mammalian precursors.



Figure 7.

Amino acid sequences, aligned from NH2 terminus, of representatives of VIP‐secretin family in single‐letter notation. Sequence of porcine VIP is shown; dash indicates residue identical to that in porcine VIP. Similar sequences have been found for human, bovine, and rat VIP; guinea pig has Leu5, Thr9, Met19, and Val21. Sequence of porcine PHI shown here differs from human, which has Lys12 and Met28, and rat (Tyr10, He17). Porcine and bovine secretin have sequence shown here, but human is Glu15Gly16. Porcine glucagon is shown; similar sequences have been found in all other mammals studied except guinea pig (Glu21, Leu23, Lys24, Leu27, and Val19). Partial sequences (1–29) are shown of human growth hormone‐releasing factor (GH‐RF) (44 residues), hamster glucagon‐like peptide (GLP)‐I (37 residues), hamster GLP‐II (35 residues), porcine glucose‐dependent insulinotropic peptide (GIP) (42 residues), helospectin (35 residues), helodermin (38 residues), and anglerfish GLP (31 residues). Human GIP differs in His18 and Asn24, and bovine GIP has He37. Human GH‐RF differs from rat in 14 positions. Asterisk indicates that there are 6 residues to NH2 terminus of hamster GLP‐I that are not shown (His‐Asp‐Glu‐Phe‐Glu‐Arg). Bovine and human GLP are identical to hamster GLP‐I; bovine and human GLP‐II differ in 3 and 2 residues, respectively, from corresponding hamster peptide. Avian peptides are all of chicken origin. Duck glucagon has Thr for Ser at 16 and Ser for Asn at 28; turkey glucagon also has Ser for Asn at 28. The anglerfish glucagon I is shown; glucagon II in anglerfish differs at Thr16, Arg18, Asp21, Glu24, Lys27, and Ser29. Catfish glucagon is identical to anglerfish glucagon II. Anglerfish GLP from proglucagon I is shown. Corresponding peptide from proglucagon II differs in 7 positions. Catfish GLP differs in 7 residues from anglerfish I.



Figure 8.

Stimulation of flow of juice and protein output from pancreas in the urethane‐anesthetized turkey in response to intravenous injections of chicken VIP, chicken secretin, and porcine secretin. Note greater potency of VIP in stimulating flow of juice. Chicken and porcine VIP are of similar potencies. Porcine secretin is a weak stimulant of avian pancreas but strong stimulant in mammals. Chicken secretin is a weak stimulant in both birds and mammals. None of the peptides strongly stimulates protein output.

From Dimaline and Dockray 79


Figure 9.

Inhibition of acid secretion in cod by VIP and stimulation by bombesin.

From Holstein and Humphrey 175


Figure 10.

Amino acid sequence of bombesin/GRP group of peptides. In both mammals and amphibians 2 subgroups can be identified, depending on residue in penultimate position: either Leu (bombesin or GRP) or Phe (litorin and neuromedin B).



Figure 11.

Amino acid sequence of tachykinins from mammals, amphibian skin and gut, and salivary gland of octopus. In mammals there are 3 peptides, 2 of which (substance P and substance K) share common precursor. Substance K is also known as neuromedin L and neurokinin‐α; neurokinin B is also known as neuromedin K. Sequence Phe‐X‐Gly‐Leu‐Met‐NH2 is common to all except enterohylambatin, which has penultimate Met.



Figure 12.

Action of substance P (SP) in contracting trout stomach. Response is blocked by tetrodotoxin (TTX) (A) but resistant to atropine (ATR) and phentolamine (PHENT) (S); serotonin (5‐HT) also contracts stomach (C). Serotonin antagonist methysergide (METH) blocked action of both serotonin and substance P, suggesting the latter acts through serotonin release. There is also direct evidence that substance P releases serotonin from perfused trout stomach.

From Holmgren et al. 166), © 1985, with permission from Pergamon Press, Ltd


Figure 13.

Pancreatic polypeptide (PP) family in single‐letter notation. All the peptides are 36 residues and COOH‐terminally amidated except anglerfish PP, which is 37 and COOH‐terminal Gly. This would normally be a substrate for conversion to COOH‐terminal amide. There are 3 members in mammals (PP, NPY, and PYY). Note NPY resembles anglerfish APY and avian PP more closely than mammalian PP. Porcine NPY has Leu in place of Met at position 17. Following residues are common to all peptides: Pro5, Pro8, Gly9, Ala12, Glu15, Tyr27, Arg23, Arg35.



Figure 14.

Amino acid sequences of neurotensin family in single‐letter notation. In birds and mammals, there are 2 peptides, tridecepeptide and hexapeptide, that share a COOH‐terminal tetrapeptide sequence. Two peptides also occur in chicken.



Figure 15.

Somatostatin‐related peptides. Tetradecapeptide somatostatin‐14 corresponds to COOH‐terminus of somatostatin‐28. It is strongly conserved and occurs in identical form in teleosts, elasmobranchs, birds, and mammals. In addition, in teleosts there are several related peptides, including the urotensins II, 22‐residue somatostatin, and 28‐residue somatostatin. Angler‐fish somatostatin II is shown; asterisk indicates Hyl at position 6 from COOH terminus. In anglerfish somatostatin I, COOH‐terminal tetradecapeptide is identical to mammalian sequence, but there are 6 substitutions in first 14 positions. Sequence shown for somatostatin‐22 is that reported by Andrews et al. 12) and agrees with that deduced from cDNA sequencing 239); it differs from that reported by Oyama et al. 283) in Thr for Arg at position 5 and Arg for Ser at position 19. Several teleost urotensins II are known, including 3 in carp. Hexapeptide C‐F‐W‐K‐Y‐C is common to all of them. In all members of family, Cys residues are joined by disulfide bridge.



Figure 16.

Contraction of cockroach protodeum in response to serotonin (5‐HT), stomodermal nerve stimulation, and proctolin. Glutamate was only weakly active. Tetrodotoxin blocked effect of nerve stimulation but not proctolin or serotonin. However, serotonin antagonists were shown to block effect of serotonin but not proctolin or nerve stimulation, suggesting that proctolin might be neurotransmitter in this system.

From Brown 40), © 1975, with permission from Pergamon Press, Ltd
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Article Title: Comparative Neuroendocrinology of Gut Peptides
 

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G. J. Dockray. Comparative Neuroendocrinology of Gut Peptides. Compr Physiol 2011, Supplement 17: Handbook of Physiology, The Gastrointestinal System, Neural and Endocrine Biology: 133-170. First published in print 1989. doi: 10.1002/cphy.cp060208