Actions of peptides isolated from amphibian skin on amylase release from dispersed pancreatic acini.

Uhlemann, Edward R.; Rottman, Alvin J.; Gardner, Jerry D.

doi:10.1152/ajpendo.1979.236.5.e571

Cited by 14 publications

(12 citation statements)

References 4 publications

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“…These results are comparable to those observed in other species (22). Several authors have re ported that bombesin nonapeptide is a direct stimulant of enzyme secretion by the guinea pig or rat pancreas acting through mecha nisms similar to those of CCK (8,14,16,21). Assuming that the isolation procedure did not selectively destroy the bombesin recep tors present on the dog pancreatic acinar cell surface, the present results show that bombe sin nonapeptide had no direct effect on secre tion by canine pancreatic acinar cells, thus confirming previous indirect evidence against a direct secretagogues effect of bom besin reported by other workers in different in vivo studies (10.…”

Section: Discussionsupporting

confidence: 86%

Action of Secretagogues on Amylase Release from Dog Pancreatic Acini

et al. 1981

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This work describes a new preparation of dog pancreatic acini which were used to study amylase release in response to various secretagogues. Neither secretin nor vasoactive intestinal peptide stimulated amylase release from acini. Caerulein, carbachol and human synthetic gastrin G17 stimulated amylase release with the same efficacy, but with different potencies. Bombesin nonapeptide did not show any evidence of a direct stimulatory effect on amylase release. These species-related peculiarities stress the necessity of using the same species when comparing pancreatic cell behaviour in vivo and in vitro.

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Section: Discussionsupporting

confidence: 86%

Action of Secretagogues on Amylase Release from Dog Pancreatic Acini

et al. 1981

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“…In addition to stimulating amylase release, physalaemin and eledoisin have been shown to increase 45Ca outflux as well as cellular cyclic GMP in pancreatic acini (1)(2)(3). We compared the ability of physalaemin to alter these functions with its ability to inhibit the binding of '25I-physalaemin (Fig.…”

Section: Resultsmentioning

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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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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“…Furthermore, bombesin has been reported to stimulate amylase release in the rat pancreas in vitro (Deschodt-Lankman, Robberecht, De Neef, Lammens & Christophe, 1976;Jwatsuki & Peterson, 1976;Uhleman, Rottman & Gardner, 1979) via specific and separate plasma membrane receptors (Jensen, Moody, Pert, Rivier & Gardner, 1978;Jensen & Gardner, 1981).…”

Section: Discussionmentioning

confidence: 99%

Cholecystokinin receptor antagonism by peptidergic and non‐peptidergic agents in rat pancreas.

Dembiński¹,

Jaworek²,

Konturek³

et al. 1989

The Journal of Physiology

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SUMMARY1. Graded doses of bombesin infused I.v. into conscious rats with chronic pancreatic fistulae induced a dose-dependent stimulation of protein secretion, similar to that obtained with caerulein. This stimulation does not appear to be mediated by cholecystokinin (CCK) receptors because peptidergic (CR-1409) and non-peptidergic (L-364 718) CCK antagonists failed to affect protein secretion at a dose range which caused almost complete suppression of caerulein-induced pancreatic secretion.2. Studies in vitro on isolated rat pancreatic acini revealed that caerulein, pentagastrin and bombesin all showed the same efficacy in their ability to stimulate amylase release. In contrast, CCK antagonists competitively inhibited amylase release induced by caerulein and pentagastrin but not by bombesin or urecholine, indicating that the latter two agents act directly on acinar cells via receptors which are separate from those involved in stimulation induced by caerulein and pentagastrin.3. DNA synthesis, measured by the incorporation of [3H]thymidine into DNA, was significantly stimulated by caerulein, soybean trypsin inhibitor (FOY 305), pentagastrin and by bombesin in a dose-dependent manner. CCK receptor antagonists prevented stimulation of DNA synthesis induced by caerulein, FOY 305 and pentagastrin but not by bombesin.4. This study indicates that bombesin strongly stimulates pancreatic enzyme secretion, with an efficacy similar to that of caerulein, and also exerts a potent growth-promoting action on the pancreas, both effects appearing to be mediated by mechanisms independent of the CCK receptors.

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Actions of peptides isolated from amphibian skin on amylase release from dispersed pancreatic acini.

Cited by 14 publications

References 4 publications

Action of Secretagogues on Amylase Release from Dog Pancreatic Acini

Action of Secretagogues on Amylase Release from Dog Pancreatic Acini

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

Cholecystokinin receptor antagonism by peptidergic and non‐peptidergic agents in rat pancreas.

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