Effect of extracellular calcium on amylase release from dispersed pancreatic acini.

Gardner, Jerry D.; Costenbader, Cynthia L.; Uhlemann, Edward R.

doi:10.1152/ajpendo.1979.236.6.e754

Cited by 10 publications

(8 citation statements)

References 21 publications

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“…There is the possibility that the concentration of 10-10 M of caerulein is actually submaximal. The biphasic secretory pattern of the pancreatic enzyme was also reported by other workers (FRANDSEN, 1980;GARDNER et al, 1979;GUDERLEY and HEISLER, 1980;KANNO and NISHIMURA, 1976;MATTHEWS et al, 1973;PETERSEN and UEDA,1976;SCHEELE and HAYMOVITS, 1979;SCHREURS et al, 1976;SCHULZ et al, 1981).…”

Section: Discussionsupporting

confidence: 82%

Dynamic analysis of secretagogue-induced amylase secretion from rat pancreatic acini studied by perifusion system.

et al. 1983

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A perifusion system was applied for the study on stimulusenzyme secretion coupling in dispersed pancreatic acini. The system is highly simple, preserves the acini up to more than 3 hr, and makes feasible clear-cut examination on the time course of enzyme secretion caused by secretagogues. Caerulein (10-s M) and carbamylcholine (10-5 M) caused a biphasic amylase secretory pattern consisting of an initial burst secretion and a sustained one. Caerulein induced a persistent amylase release even after cessation of the stimulation, while carbamylcholine-stimulated amylase release returned to basal levels. Atropine inhibited completely carbamylcholine-stimulated amylase release and the successive stimulation by caerulein evoked the amylase secretion with a decreased initial burst secretion. In calcium free medium, caerulein and carbamylcholine induced only a slight secretion, particularly in the sustained secretion phase and a gradual increase occurred with the addition of calcium.

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Section: Discussionsupporting

confidence: 82%

Dynamic analysis of secretagogue-induced amylase secretion from rat pancreatic acini studied by perifusion system.

et al. 1983

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“…Outflux of 'Ca was determined by using the described procedure (24). Acini from the pancreas of one animal were suspended in 10 ml of standard incubation solution and, after the acini were loaded with ',Ca, they were washed and incubated with the appropriate agents for 5 min at 37C.…”

mentioning

confidence: 99%

Proglumide and benzotript: members of a different class of cholecystokinin receptor antagonists.

Hahne¹,

Jensen²,

Lemp³

et al. 1981

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

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175

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In dispersed acini from.guinea pig pancreas, proglumide (DL-4-benzamido-N, N-dipropylglutaramic acid) and benzotript (N-p-chlorobenzoyl-L-tryptophan) caused a rightward shift in the dose-response curve for cholecystokinin-stimulated amylase secretion but did not alter the maximal increase in amylase secretion caused by cholecystoldnin.. At relatively low, concentrations, proglumide did not alter the stimulation ofenzyme secretion caused by secretagogues whose effects are mediated by adenosine 3'5'-monophosphate (e.g., vasoactive intestinal peptide or secretin) and did not alter the stimulation of enzyme secretion caused by secretagogues that have a mode of action similar to that of cholecystokinin but act through different receptors (e.g., bombesin, physalaemin, eledoisin, and ionophore A23187). There was a close correlation between the ability of proglumide or benzotript to inhibit binding of '25I-labeled cholecystokinin to its receptors on pancreatic acini and the abilities ofthese compounds to inhibit the action of cholecystokinin on enzyme secretion and on calcium outflux. These results indicate that proglumide and benzotript are members ofa different class ofcholecystokinin receptor antagonists.Proglumide (Fig.

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“…At the end of the incubation period in the presence (stimulated) or in the absence (basal) of secretagogues, amy lase release from pancreatic acini was determined as previously described by Larose et al [ 12]. Amylase activity was evaluated by the method of Ceska et al [13] using phadebas blue starch reagent as reported by Gardner et al [ 14], Amylase release was expressed as the percentage of initial amylase activity present in the acini released into the medium during 30 min at 37 °C minus basal release giving net amylase release. Total acinar amylase content was determined from each acinar cell suspension by the addition of 500 pi of freshly prepared acini to 5 ml of lysing solution containing 0.01 A/Na phos phate, pH 7.8.…”

Section: Anim Al Model Male Sprague-dawlely Rats (250-260 G) From Thementioning

confidence: 99%

Alterations of the Pancreatic Secretory Responses to Secretin and to the lonophore A23187 by Reserpine: A Calcium-Mediated Phenomenon?

Benrezzak¹,

Bérubé²,

St-Jean³

et al. 1994

Digestion

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This study was undertaken to further characterize the secretory response of the rat pancreas after reserpine treatment. Rats were given reserpine (1 mg kg^-1 day^-1 i.p.) or vehicle for 7 days. To distinguish between specific effects of reserpine and those related to secondary malnutrition caused by the drug, the secretory response of a group of pair-fed (PF) animals to reserpine was also investigated. Amylase release from dispersed pancreatic acini, prepared from control (C), PF and reserpine-treated (R) rats were used to evaluate functional secretory capacity. Reserpine and pair-feeding caused reduced responses of pancreatic acini to secretin. The pair-feeding-altered secretin response was greatly improved by increasing extracellular Ca²⁺ concentration, whereas a slight improvement was noticed in the R group. Reserpine significantly reduced the secretory response to the ionophore A23187 at concentrations above 5 × 10^-7M in 1.25 mM Ca²⁺; in 2.5 mM Ca²⁺, the response to the ionophore was significantly higher in the R group than in C at all ionophore concentrations. Furthermore, at 2 × 10^-7M ionophore, the secretory response to secretin in the R group became significantly higher than that in the C group but comparable to that of the control + ionophore. In conclusion, reserpine affects the secretory response to secretin as did pre-exposure of pancreatic acini to a high concentration of carbamylcholine. The modified secretory response to the ionophore following reserpine treatment indicates that reserpine may act as a ‘Ca²⁺ entry mechanism’ antagonist which may explain the partial reduction in the secretin response.

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Effect of extracellular calcium on amylase release from dispersed pancreatic acini.

Cited by 10 publications

References 21 publications

Dynamic analysis of secretagogue-induced amylase secretion from rat pancreatic acini studied by perifusion system.

Dynamic analysis of secretagogue-induced amylase secretion from rat pancreatic acini studied by perifusion system.

Proglumide and benzotript: members of a different class of cholecystokinin receptor antagonists.

Alterations of the Pancreatic Secretory Responses to Secretin and to the lonophore A23187 by Reserpine: A Calcium-Mediated Phenomenon?

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