In vitro action of bombesin on amylase secretion, membrane potential, and membrane resistance in rat and mouse pancreatic acinar cells. A comparison with other secretagogues.

Iwatsuki, Naofumi; Petersen, O. H.

doi:10.1172/jci108923

Cited by 71 publications

(23 citation statements)

References 27 publications

(49 reference statements)

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“…In pancreatic fragments as well as dispersed acinar cells, each of these amphibian peptides increases amylase secretion, cellular cyclic GMP, and outflux of exchangeable cellular calcium but does not alter cellular cyclic AMP (1). These effects of amphibian peptides are not inhibited by atropine (1,4), and therefore are not mediated by muscarinic cholinergic receptors. The effects of caerulein appear to be mediated by receptors that also interact with CCK because the actions of caerulein and CCK, but not those of other pancreatic secretagogues, can be inhibited competitively by dibutyryl cyclic GMP (5).…”

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confidence: 92%

“…We (1, 2) and others (3,4) have found that peptides isolated from amphibian skin (caerulein, bombesin, litorin, and physalaemin) as well as eledoisin, a peptide isolated from the salivary gland of a Mediterranean octopod,t produce changes in the function of pancreatic acinar cells similar to those caused by muscarinic cholinergic agents and cholecystokinin (CCK). In pancreatic fragments as well as dispersed acinar cells, each of these amphibian peptides increases amylase secretion, cellular cyclic GMP, and outflux of exchangeable cellular calcium but does not alter cellular cyclic AMP (1).…”

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confidence: 99%

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Interaction of physalaemin, substance P, and eledoisin with specific membrane receptors on pancreatic acinar cells.

Jensen¹,

Gardner²

1979

Proc. Natl. Acad. Sci. U.S.A.

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We have prepared '251-labeled physalaemin and have examined the kinetics, stoichiometry, and chemical specificity with which the labeled peptide binds to dispersed acini from guinea pig pancreas. Binding of '25I-labeled physalaemin was saturable, temperature-ependent, and reversible and reflected interaction of the labeled peptide with We (1, 2) and others (3, 4) have found that peptides isolated from amphibian skin (caerulein, bombesin, litorin, and physalaemin) as well as eledoisin, a peptide isolated from the salivary gland of a Mediterranean octopod,t produce changes in the function of pancreatic acinar cells similar to those caused by muscarinic cholinergic agents and cholecystokinin (CCK). In pancreatic fragments as well as dispersed acinar cells, each of these amphibian peptides increases amylase secretion, cellular cyclic GMP, and outflux of exchangeable cellular calcium but does not alter cellular cyclic AMP (1). These effects of amphibian peptides are not inhibited by atropine (1, 4), and therefore are not mediated by muscarinic cholinergic receptors. The effects of caerulein appear to be mediated by receptors that also interact with CCK because the actions of caerulein and CCK, but not those of other pancreatic secretagogues, can be inhibited competitively by dibutyryl cyclic GMP (5). The effects of bombesin and litorin on pancreatic acinar cells appear to be mediated by a common receptor that does not interact with other secretagogues. Binding of 125I-labeled [Tyr4] bombesin (125I-[Tyr4]bombesin) to pancreatic acini in vitro can be inhibited by bombesin and litorin but not by other secretagogues (6) and there is a close correlation between the abilities of bombesin and litorin to inhibit binding of 1251-[Tyr4]bombesin and their abilities to alter the function of pancreatic acini (6). Because physalaemin and eledoisin have similar COOHterminal amino acid sequences and do not interact with receptors for other pancreatic secretagogues, we have proposed (1) that these peptides might interact with a common class of receptors.To explore further the interaction of physalaemin and structurally similar peptides with pancreatic acini, we have prepared 125I-labeled physalaemin (125I-physalaemin) and have examined its ability to bind to dispersed pancreatic acini. We have also explored the abilities of various peptides to inhibit this binding, and the relationship between a peptide's ability to inhibit binding of 125I-physalaemin and its ability to alter acinar cell function. Our results indicate that pancreatic acini possess a single class of receptors that interact reversibly with physalaemin, eledoisin, and substance P and that occupation of approximately 45% of these receptors is sufficient to cause a maximal change in acinar cell function.MATERIALS AND METHODS Materials. Male guinea pigs (175-225 g) were obtained from the Small Animals Section, Veterinary Resources Branch, National Institutes of Health. Hepes and cyclic somatostatin were obtained from Calbiochem; synthetic human gastrin was from ...

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confidence: 92%

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confidence: 99%

Interaction of physalaemin, substance P, and eledoisin with specific membrane receptors on pancreatic acinar cells.

Jensen¹,

Gardner²

1979

Proc. Natl. Acad. Sci. U.S.A.

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“…In vitro studies have provided conflicting results. Bombesin, has been found to stimulate amylase release from rat (Iwatsuki & Petersen, 1978;Otsuki et al, 1987), guinea-pig (Jensen et al, 1984), mouse (Iwatsuki & Petersen, 1978) and human (Susini et al, 1986) pancreatic acini, whereas it is ineffective in the same dog preparation (Bommelaer et al, 1981).…”

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confidence: 99%

Effect of a new potent CCK antagonist, lorglumide, on caerulein‐ and bombesin‐induced pancreatic secretion and growth in the rat

Scarpignato

Varga

Dobronyi

et al. 1989

British J Pharmacology

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1 The effect of lorglumide, a new potent cholecystokinin (CCK) antagonist, on pancreatic secretion and growth induced by caerulein and bombesin was studied in the rat. 2 Pancreatic exocrine secretion was studied both in vitro (isolated and perfused pancreatic segments) and in vivo (anaesthetized animals with cannulation of the common bile duct) whereas the trophic effect was investiged after short-term (5 days) administration of the peptides and/or lorglumide. 3 Both caerulein and bombesin stimulated amylase release from in vitro pancreatic segments in a concentration-dependent manner. Although the efficacy of both peptides was virtually identical, the potency of caerulein was higher than that of bombesin. Lorglumide displaced the concentrationresponse curves to caerulein to the right without affecting the maximum response, suggesting a competitive antagonism. The Schild plot analysis of data gave a straight line with a slope not significantly different from unity. The calculated pA2 for lorglumide was 7.31 + 0.45. The antagonist, however, was completely ineffective when tested against bombesin-induced amylase release. 4 In vivo experiments confirmed results from in vitro studies since lorglumide (5 and I0mgkg 1) significantly reduced pancreatic exocrine secretion induced by caerulein without affecting the response to bombesin. 5 Administration of either peptide increased the weight of the pancreas, the total pancreatic protein and DNA, trypsin and amylase content. Lorglumide (10mgkg-1), administered together with caerulein, reduced the peptide-induced increase in pancreatic weight, protein and enzyme content. On the contrary, when lorglumide was given together with bombesin, all the parameters that were examined were not altered by concomitant administration of the antagonist. 6 These results have demonstrated the ability of lorglumide to antagonize the effects on the pancreas of a CCK-analogue, caerulein, and its inability to affect bombesin-induced pancreatic secretion and growth, suggesting that lorglumide is a potent and selective antagonist of CCK-receptors in the pancreas.

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“…It has been shown (1-3) that several peptides isolated from amphibian skin (caerulein, bombesin, litorin, and physalemin) as well as a peptide isolated from the salivary gland of a Mediterranean octopod (eledoisin) can alter the function of acinar cells from rat or guinea pig pancreas. Like cholecystokinin and muscarinic cholinergic agents (1)(2)(3)(4)(5)(6)(7)(8), each of these nonmammalian peptides increased amylase secretion, cyclic GMP (cGMP) accumulation, and outflux of exchangeable cellular calcium but did not alter cellular cyclic AMP (cAMP) (1). These actions of caerulein were not unanticipated because seven of its eight COOH-terminal amino acids are identical to those of the COOH-terminal octapeptide of cholecystokinin (9).…”

mentioning

confidence: 99%

Interaction of bombesin and litorin with specific membrane receptors on pancreatic acinar cells

Jensen¹,

Moody²,

Pert³

et al. 1978

Proc. Natl. Acad. Sci. U.S.A.

172

100

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[Tyr4Jbombesin, bombesin, and litorin and that occupation of 25% of these receptors will cause a maximal biological response. It has been shown (1-3) that several peptides isolated from amphibian skin (caerulein, bombesin, litorin, and physalemin) as well as a peptide isolated from the salivary gland of a Mediterranean octopod (eledoisin) can alter the function of acinar cells from rat or guinea pig pancreas. Like cholecystokinin and muscarinic cholinergic agents (1-8), each of these nonmammalian peptides increased amylase secretion, cyclic GMP (cGMP) accumulation, and outflux of exchangeable cellular calcium but did not alter cellular cyclic AMP (cAMP) (1). These actions of caerulein were not unanticipated because seven of its eight COOH-terminal amino acids are identical to those of the COOH-terminal octapeptide of cholecystokinin (9). The amino acid sequence of bombesin is similar to that of litorin and the amino acid sequence of physalemin is similar to that of eledoisin; however, the structures of each of these peptides differ substantially from those of cholecystokinin and caerulein (10, 11).To explore further the actions of bombesin and structurally similar peptides on pancreatic acinar cells, we have examined the ability of a synthetic radiolabeled analogue of bombesin Research). Bovine pancreatic polypeptide (BPP) was a gift from T. M. Lin (Lilly Research Laboratories). [Tyr4]bombesin was synthesized by the method described (12). In terms of peptide content, this material was >75% pure. Standard incubation solution contained 24.5 mM Hepes (pH 7.4), 98 mM NaCl, 6 mM KCI, 2.5 mM KH2PO4, 1.2 mM MgCl2, 11.5 mM glucose, 5 mM Na fumarate, Na glutamate, and Na pyruvate, 2.0 mM CaC12, 2 mM glutamine, 0.2% albumin, 0.01% soybean trypsin inhibitor, 1% amino acid mixture, and 1% essential vitamin mixture.125I-[Tyr4]Bombesin was prepared by using a modification of the procedure described by Hunter and Greenwood (13). Equimolar amounts (0.5 nmol) of [Tyr4]bombesin, 125I, and chloramine-T were incubated in a total volume of 35 ,u at ambient temperature for 60 sec and then 1.5 nmol of sodium metabisulfite was added. Radiolabeled peptide was separated from free 125I by using Sephadex LH-20 (0.7 X 20 cm) equilibrated and eluted with methanol/acetic acid/water, 10:2:1 (vol/vol), as described (14). Assuming complete recovery of the peptide, the specific activity of 125I-[Try4]bombesin was 150 Ci/mmol.Dispersed acini from guinea pig pancreas were prepared by using the previously described procedure (5) and, unless specAbbreviations: cAMP, cyclic AMP; cGMP, cyclic GMP; CCK-OP, COOH-terminal octapeptide of porcine cholecystokinin; VIP, porcine vasoactive intestinal peptide; BPP, bovine-pancreatic polypeptide; Kd, concentration for half-maximal effect. 6139 The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U. S. C. §1734 solely to indicate this fact.

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In vitro action of bombesin on amylase secretion, membrane potential, and membrane resistance in rat and mouse pancreatic acinar cells. A comparison with other secretagogues.

Cited by 71 publications

References 27 publications

Interaction of physalaemin, substance P, and eledoisin with specific membrane receptors on pancreatic acinar cells.

Interaction of physalaemin, substance P, and eledoisin with specific membrane receptors on pancreatic acinar cells.

Effect of a new potent CCK antagonist, lorglumide, on caerulein‐ and bombesin‐induced pancreatic secretion and growth in the rat

Interaction of bombesin and litorin with specific membrane receptors on pancreatic acinar cells

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