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Receptors for Gut Peptides and Other Secretagogues on Pancreatic Acinar Cells

Jerry D. Gardner, Robert T. Jensen

10.1002/cphy.cp060209

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 Receptors for Secretagogues that Mobilize Cellular Calcium
1.1 Receptors for Cholecystokinin and Structurally Related Peptides
1.2 Receptors for Bombesin and Structurally Related Peptides
1.3 Receptors for Muscarinic‐Cholinergic Agents
1.4 Receptors for Physalaemin and Structurally Related Peptides
2 Receptors for Secretagogues that Increase Cellular Camp
2.1 Receptors for Vasoactive Intestinal Peptide and Secretin
2.2 Receptors for Cholera Toxin
2.3 Receptors for Calcitonin Gene‐Related Peptide
2.4 Receptors for Natural Glucagon Contaminant
Figure 1. Figure 1.

Ability of CCK(CCK‐8) to increase amylase release and Ca2+ outflux and to inhibit binding of 125I‐CCK in dispersed acini from guinea pig pancreas. Results are expressed as the percentage of maximal effect of CCK‐26–33.

From Jensen et al. 63
Figure 2. Figure 2.

Structure of N2,O2'‐dibutyryl cGMP (Bt2cGMP), D,L‐4‐benzamido‐N,N‐dipropylglutaramic acid (proglumide), N‐p‐chlorobenzoyl‐L‐tryptophan (benzotript), and COOH‐terminal octapeptide of cholecystokinin (CCK‐8 or CCK‐26–33).
Figure 3. Figure 3.

Effects of Bt2cGMP, O2'BtcGMP, and N2BtcGMP on amylase release stimulated by CCK‐26–33 (CCK‐8) (left panel) and on binding of 125I‐CCK (right panel).

From Barlas et al. 5) and Jensen et al. 63
Figure 4. Figure 4.

Effects of proglumide and benzotript on amylase release stimulated by CCK‐26–33 (CCK‐8) (left panel) and on binding of 125I‐CCK (right panel).

From Hahne et al. 44
Figure 5. Figure 5.

Structure of L‐tryptophan and various N‐acyl derivatives of L‐tryptophan.
Figure 6. Figure 6.

Effects of L‐tryptophan and various N‐acyl derivatives of L‐tryptophan on amylase release stimulated by CCK‐26–33 (CCK‐8) (left panel) and on binding of 125I‐CCK (right panel). For abbreviations, see legend to Fig. 5.

From Jensen et al. 61
Figure 7. Figure 7.

Effects of L‐ and D‐tryptophan and their Boc and Ac derivatives on amylase release stimulated by CCK‐26–33 (CCK‐8) (left panel) and on binding of 125I‐CCK (right panel). Open symbols represent results obtained with compounds containing D‐tryptophan, and closed symbols represent results obtained with compounds containing L‐tryptophan. For abbreviations, see legend to Fig. 5.

From Jensen et al. 61
Figure 8. Figure 8.

Relationship between the ability of a Cbz‐amino acid to inhibit binding of 125I‐CCK and the hydrophobicity of the amino acid side chain. Logarithm of the concentration of Cbz‐amino acid that inhibited binding of 125I‐CCK by 20% (IC 20) obtained from measurements of binding of 125I‐CCK. Hydrophobicity of the amino acid side chain (R group) was obtained from Rekker 102). Open symbols, amino acid derivatives with aromatic side chains; closed symbols, amino acid derivatives with aliphatic side chains. Single letter next to each symbol is one‐letter notation for amino acids; N‐V and N‐L, norvaline and norleucine, respectively.

From Maton et al. 80
Figure 9. Figure 9.

Effect of proglumide analogue 10 on amylase release stimulated by CCK‐26–33 (CCK‐8) (left panel) and on binding of 125I‐CCK (right panel).

From Jensen et al. 68
Figure 10. Figure 10.

Effects of CCK‐32–33, CCK‐31–33, and their Boc derivatives on amylase release stimulated by CCK‐26–33 (CCK‐8) (left panel) and on binding of 125I‐CCK (right panel).

From Jensen et al. 60
Figure 11. Figure 11.

Effect of CCK‐27–32‐NH2 on amylase release stimulated by CCK‐26–33 (CCK‐8) (left panel) and on binding of 125I‐CCK (right panel).

From Spanarkel et al. 115
Figure 12. Figure 12.

Effect of various derivatives ofCCK‐26–32 on amylase release stimulated by CCK‐26–33 (CCK‐8) (left panel) and on binding of 125I‐CCK (right panel).

From Gardner et al. 38
Figure 13. Figure 13.

Effect of various NH2‐terminal fragments of CCK‐26–33 (CCK‐8) on amylase release stimulated by CCK‐26–33 (left panel) and on binding of 125I‐CCK (right panel).

From Gardner et al. 37
Figure 14. Figure 14.

Structure of asperlicin and L‐364, 718.
Figure 15. Figure 15.

Effect of asperlicin on amylase release stimulated by CCK‐26–33 (CCK‐8) (left panel) and on binding of 125I‐CCK (right panel) in guinea pig pancreatic acini. Results are means from 5 separate experiments.

Methods from Jensen et al. 63
Figure 16. Figure 16.

Effect of L‐364, 718 on amylase release stimulated by CCK‐26–33 (CCK‐8) (left panel) and on binding of 125I‐CCK (right panel) in guinea pig pancreatic acini. Results are means from at least 6 separate experiments.

Methods from Jensen et al. 63
Figure 17. Figure 17.

Ability of bombesin to increase amylase secretion and Ca2+ outflux and its ability to inhibit binding of 125I‐[Tyr4]bombesin in dispersed acini from guinea pig pancreas. Results are expressed as percentage of maximal effect caused by bombesin.

From Jensen et al. 65) and Uhlemann et al. 118
Figure 18. Figure 18.

Effect of [D‐Arg1,D‐Pro2,D‐Trp7,9,Leu11]substance P on binding of 125I‐[Tyr4]bombesin (left panel) and on amylase release stimulated by bombesin (right panel).

From Jensen et al. 59
Figure 19. Figure 19.

Effect of [D‐Phe12]bombesin on bombesin‐stimulated amylase release (left panel) and on binding of 125I‐[Tyr4]bombesin (right panel).

From Heinz‐Erian et al. 46
Figure 20. Figure 20.

Ability of carbachol to increase amylase secretion and Ca2+ outflux and to inhibit binding of [3H]N‐methyl scopolamine in dispersed acini from guinea pig pancreas. Results are expressed as the percentage of the maximal effect produced by carbachol.

From Jensen and Gardner 58) and McArthur et al. 82
Figure 21. Figure 21.

Ability of physalaemin to increase amylase secretion and Ca2+ outflux and to inhibit binding of 125I‐physalaemin in dispersed acini from guinea pig pancreas. Results are expressed as percentage of maximal effect caused by physalaemin.

From Jensen and Gardner 57) and Uhlemann et al. 118
Figure 22. Figure 22.

Effect of 3 analogues of substance P on binding of 125I‐physalaemin (left panel) and on amylase release stimulated by physalaemin (right panel). The 3 analogues tested were [D‐Arg1,D‐Pro2,D‐Trp7,9,Leu11]substance P (analogue A), [D‐Pro2,D‐Trp7,9]substance P (analogue B), and [D‐Pro2,D‐Phe7, D‐Trp9]substance P (analogue C).

From Jensen et al. 62
Figure 23. Figure 23.

Ability of VIP to interact with VIP‐preferring receptors to increase amylase secretion and cAMP and to inhibit binding of 125I‐VIP in dispersed acini from guinea pig pancreas. Results are expressed as percentage of maximal effect caused by VIP.

From Jensen and Gardner 58
Figure 24. Figure 24.

Ability of secretin to interact with secretin‐preferring receptors to increase cAMP and to inhibit binding of 125I‐secretin in dispersed acini from guinea pig pancreas. Results are expressed as percentage of maximal effect caused by secretin.

From Jensen et al. 56
Figure 25. Figure 25.

Ability of cholera toxin to increase amylase secretion and cAMP and to inhibit binding of 125I‐cholera toxin in dispersed acini from guinea pig pancreas. Results are expressed as percentage of maximal effect caused by cholera toxin.

From Gardner and Rottman 40
Figure 26. Figure 26.

Ability of calcitonin gene‐related peptide (CGRP) to increase amylase secretion and cAMP and to inhibit binding of 125I‐CGRP in dispersed acini from guinea pig pancreas. Results are expressed as percentage of maximal effect caused by CGRP.

From Zhou et al. 124


Figure 1.

Ability of CCK(CCK‐8) to increase amylase release and Ca2+ outflux and to inhibit binding of 125I‐CCK in dispersed acini from guinea pig pancreas. Results are expressed as the percentage of maximal effect of CCK‐26–33.

From Jensen et al. 63


Figure 2.

Structure of N2,O2'‐dibutyryl cGMP (Bt2cGMP), D,L‐4‐benzamido‐N,N‐dipropylglutaramic acid (proglumide), N‐p‐chlorobenzoyl‐L‐tryptophan (benzotript), and COOH‐terminal octapeptide of cholecystokinin (CCK‐8 or CCK‐26–33).



Figure 3.

Effects of Bt2cGMP, O2'BtcGMP, and N2BtcGMP on amylase release stimulated by CCK‐26–33 (CCK‐8) (left panel) and on binding of 125I‐CCK (right panel).

From Barlas et al. 5) and Jensen et al. 63


Figure 4.

Effects of proglumide and benzotript on amylase release stimulated by CCK‐26–33 (CCK‐8) (left panel) and on binding of 125I‐CCK (right panel).

From Hahne et al. 44


Figure 5.

Structure of L‐tryptophan and various N‐acyl derivatives of L‐tryptophan.



Figure 6.

Effects of L‐tryptophan and various N‐acyl derivatives of L‐tryptophan on amylase release stimulated by CCK‐26–33 (CCK‐8) (left panel) and on binding of 125I‐CCK (right panel). For abbreviations, see legend to Fig. 5.

From Jensen et al. 61


Figure 7.

Effects of L‐ and D‐tryptophan and their Boc and Ac derivatives on amylase release stimulated by CCK‐26–33 (CCK‐8) (left panel) and on binding of 125I‐CCK (right panel). Open symbols represent results obtained with compounds containing D‐tryptophan, and closed symbols represent results obtained with compounds containing L‐tryptophan. For abbreviations, see legend to Fig. 5.

From Jensen et al. 61


Figure 8.

Relationship between the ability of a Cbz‐amino acid to inhibit binding of 125I‐CCK and the hydrophobicity of the amino acid side chain. Logarithm of the concentration of Cbz‐amino acid that inhibited binding of 125I‐CCK by 20% (IC 20) obtained from measurements of binding of 125I‐CCK. Hydrophobicity of the amino acid side chain (R group) was obtained from Rekker 102). Open symbols, amino acid derivatives with aromatic side chains; closed symbols, amino acid derivatives with aliphatic side chains. Single letter next to each symbol is one‐letter notation for amino acids; N‐V and N‐L, norvaline and norleucine, respectively.

From Maton et al. 80


Figure 9.

Effect of proglumide analogue 10 on amylase release stimulated by CCK‐26–33 (CCK‐8) (left panel) and on binding of 125I‐CCK (right panel).

From Jensen et al. 68


Figure 10.

Effects of CCK‐32–33, CCK‐31–33, and their Boc derivatives on amylase release stimulated by CCK‐26–33 (CCK‐8) (left panel) and on binding of 125I‐CCK (right panel).

From Jensen et al. 60


Figure 11.

Effect of CCK‐27–32‐NH2 on amylase release stimulated by CCK‐26–33 (CCK‐8) (left panel) and on binding of 125I‐CCK (right panel).

From Spanarkel et al. 115


Figure 12.

Effect of various derivatives ofCCK‐26–32 on amylase release stimulated by CCK‐26–33 (CCK‐8) (left panel) and on binding of 125I‐CCK (right panel).

From Gardner et al. 38


Figure 13.

Effect of various NH2‐terminal fragments of CCK‐26–33 (CCK‐8) on amylase release stimulated by CCK‐26–33 (left panel) and on binding of 125I‐CCK (right panel).

From Gardner et al. 37


Figure 14.

Structure of asperlicin and L‐364, 718.



Figure 15.

Effect of asperlicin on amylase release stimulated by CCK‐26–33 (CCK‐8) (left panel) and on binding of 125I‐CCK (right panel) in guinea pig pancreatic acini. Results are means from 5 separate experiments.

Methods from Jensen et al. 63


Figure 16.

Effect of L‐364, 718 on amylase release stimulated by CCK‐26–33 (CCK‐8) (left panel) and on binding of 125I‐CCK (right panel) in guinea pig pancreatic acini. Results are means from at least 6 separate experiments.

Methods from Jensen et al. 63


Figure 17.

Ability of bombesin to increase amylase secretion and Ca2+ outflux and its ability to inhibit binding of 125I‐[Tyr4]bombesin in dispersed acini from guinea pig pancreas. Results are expressed as percentage of maximal effect caused by bombesin.

From Jensen et al. 65) and Uhlemann et al. 118


Figure 18.

Effect of [D‐Arg1,D‐Pro2,D‐Trp7,9,Leu11]substance P on binding of 125I‐[Tyr4]bombesin (left panel) and on amylase release stimulated by bombesin (right panel).

From Jensen et al. 59


Figure 19.

Effect of [D‐Phe12]bombesin on bombesin‐stimulated amylase release (left panel) and on binding of 125I‐[Tyr4]bombesin (right panel).

From Heinz‐Erian et al. 46


Figure 20.

Ability of carbachol to increase amylase secretion and Ca2+ outflux and to inhibit binding of [3H]N‐methyl scopolamine in dispersed acini from guinea pig pancreas. Results are expressed as the percentage of the maximal effect produced by carbachol.

From Jensen and Gardner 58) and McArthur et al. 82


Figure 21.

Ability of physalaemin to increase amylase secretion and Ca2+ outflux and to inhibit binding of 125I‐physalaemin in dispersed acini from guinea pig pancreas. Results are expressed as percentage of maximal effect caused by physalaemin.

From Jensen and Gardner 57) and Uhlemann et al. 118


Figure 22.

Effect of 3 analogues of substance P on binding of 125I‐physalaemin (left panel) and on amylase release stimulated by physalaemin (right panel). The 3 analogues tested were [D‐Arg1,D‐Pro2,D‐Trp7,9,Leu11]substance P (analogue A), [D‐Pro2,D‐Trp7,9]substance P (analogue B), and [D‐Pro2,D‐Phe7, D‐Trp9]substance P (analogue C).

From Jensen et al. 62


Figure 23.

Ability of VIP to interact with VIP‐preferring receptors to increase amylase secretion and cAMP and to inhibit binding of 125I‐VIP in dispersed acini from guinea pig pancreas. Results are expressed as percentage of maximal effect caused by VIP.

From Jensen and Gardner 58


Figure 24.

Ability of secretin to interact with secretin‐preferring receptors to increase cAMP and to inhibit binding of 125I‐secretin in dispersed acini from guinea pig pancreas. Results are expressed as percentage of maximal effect caused by secretin.

From Jensen et al. 56


Figure 25.

Ability of cholera toxin to increase amylase secretion and cAMP and to inhibit binding of 125I‐cholera toxin in dispersed acini from guinea pig pancreas. Results are expressed as percentage of maximal effect caused by cholera toxin.

From Gardner and Rottman 40


Figure 26.

Ability of calcitonin gene‐related peptide (CGRP) to increase amylase secretion and cAMP and to inhibit binding of 125I‐CGRP in dispersed acini from guinea pig pancreas. Results are expressed as percentage of maximal effect caused by CGRP.

From Zhou et al. 124
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Article Title: Receptors for Gut Peptides and Other Secretagogues on Pancreatic Acinar Cells
 

How to Cite

Jerry D. Gardner, Robert T. Jensen. Receptors for Gut Peptides and Other Secretagogues on Pancreatic Acinar Cells. Compr Physiol 2011, Supplement 17: Handbook of Physiology, The Gastrointestinal System, Neural and Endocrine Biology: 171-192. First published in print 1989. doi: 10.1002/cphy.cp060209