Serum trypsin, α-amylase and lipase during bombesin stimulation in normal subjects and patients with pancreatic insufficiency

Hafkenscheid, J. C. M.; Hessels, M.; Jansen, J. B. M. J.; Lamers, C. B. H. W.

doi:10.1016/0009-8981(84)90297-3

Cited by 13 publications

(6 citation statements)

References 11 publications

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“…The present study confirms previous re ports, indicating that infusion of bombesin stimulates plasma immunoreactive trypsin secretion in man [2,3]. However, the mech anism of this stimulatory action of bombesin on plasma trypsin is unknown.…”

Section: Discussionsupporting

confidence: 81%

“…Infusion of bombesin, a gastrointestinal neuropeptide, stimulates the secretion of trypsin not only into the duodenum but also into the circulation [1][2][3]. The stimulatoryeffect of bombesin on intraduodenal enzyme secretion is, at least in part, mediated by cholecystokinin [4], However, cholecystoki-1 Supported by grant 13-37-43 from the Nether lands Foundation for Medical Research FUNGO. nin does not seem to be involved in the stim ulation of immunoreactive trypsin release into the plasma by bombesin [5][6][7], In order to delineate the mechanism of the stimula tory' effect of bombesin on plasma immuno reactive trypsin, we have determined the ef fects of atropine and somatostatin, two in hibitors of intraduodenal pancreatic enzyme secretion, on bombesin-stimulated release of immunoreactive trypsin into the plasma of healthy human subjects.…”

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confidence: 99%

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Effect of Atropine and Somatostatin on Bombesin-Stimulated Plasma Immunoreactive Trypsin Release in Man

Jong

Klamer²,

Lamers³

1987

Digestion

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This study was undertaken to determine the effect of atropine and somatostatin, two inhibitors of intraduodenal pancreatic enzyme secretion, on bombesin-stimulated release of plasma immunoreactive trypsin in 6 healthy volunteers. Infusion of 5 ng/kg·min bombesin during 30 min induced significant increases in plasma trypsin from 206 ± 20 to 334 ± 44 ng/ml (p < 0.01). Atropine (15 ng/kg as i.v. bolus followed by 5 ng/kg•h) had no influence on the bombesin-stimulated increase in plasma immunoreactive trypsin (207 ± 20 to 326 ± 54 ng/ml). Somatostatin (125 μg as i.v. bolus followed by 125 μg/h) also failed to inhibit the plasma trypsin response to bombesin (207 ± 18 to 663 ± 166 ng/ml). These results point to major differences in the regulation of plasma and intraduodenal trypsin secretion.

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Section: Discussionsupporting

confidence: 81%

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confidence: 99%

Effect of Atropine and Somatostatin on Bombesin-Stimulated Plasma Immunoreactive Trypsin Release in Man

Jong

Klamer²,

Lamers³

1987

Digestion

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“…This effect agrees with previous reports that bom besin increased plasma 1RT in humans [4][5][6][7], Bombesin did not change plasma amylase in humans [5]. In the present study using dogs, plasma amylase was also increased by bombesin.…”

Section: Discussionsupporting

confidence: 82%

“…It stimu lates gastric and pancreatic exocrine secre tion in several species, including humans and dogs [1][2][3]. Bombesin also increases plasma immunoreactive trypsin (IRT) con centration in humans [4][5][6][7] plasma trypsin release to bombesin seems to vary according to the degree of pancreatic dysfunction and reflects the residual capac ity of acinar cell mass in humans [4,5]. The stimulatory effects of bombesin on exocrine pancreatic secretion are considered to be mediated by cholecystokinin (CCK) release [2], The mechanism of the effect of bombe sin on plasma trypsin is poorly understood.…”

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confidence: 99%

Stimulatory Effects of Bombesin on Plasma Trypsin Release and Exocrine Pancreatic Secretion in Dogs

et al. 1990

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We examined the effect of bombesin on plasma trypsin release and exocrine pancreatic secretion in dogs. Bombesin significantly increased plasma immunoreactive trypsin (IRT). Atropine significantly inhibited the response of plasma IRT to bombesin. Pancreatic trypsin secretion was also increased by bombesin, as well as bicarbonate and protein outputs. Atropine failed to inhibit pancreatic trypsin secretion. In conclusion, bombesin has a stimulatory effect on plasma trypsin release mediated by a cholinergic mechanism and different from pancreatic secretion.

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“…Recent reports [24,25] on bombesin-induced changes in se rum levels of ICT, lipase, total amylase and pancreatic isoamylase in humans have also shown a similar sensitivity pattern. Infusion of bombesin, a secretagogue which exerts similar electrophysiological and biochemical effects on the exocrine pancreas, caused the marked increases in serum ICT levels, but there was either no increase [25] or slight but insignificant increases [24] in serum levels of both total amylase and pancreatic isoamy lase. Furthermore, serum lipase levels were found to be moderately sensitive to bombe sin stimulation with a modest but significant rise [25].…”

Section: Responses Associated With Intake O F Noncaloric Fiber Pelletsmentioning

confidence: 94%

Effects of Cholecystokinin, Food Intake and Cephalic Stimuli on Plasma Levels of Amylase, Lipase, and Immunoreactive Cationic Trypsinogen in Rats

et al. 1986

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Plasma levels of amylase, lipase, and immunoreactive cationic trypsinogen (ICT) were monitored in conscious rats to study the effects of cholecystokinin octapeptide (CCK-8) plus secretin administration, cephalic stimuli, and food intake. Stepwise increasing doses of CCK-8 (1, 5, 15, 30 Ivy dog units: IDU/kg/h) caused significant dose-related increases in plasma levels of each enzyme in a similar manner as those previously observed for response patterns of CCK-induced exocrine protein secretion in the same species. ICT showed the greatest response to CCK-8 with a maximal concentration 30 times above basal levels resulting in the steepest slope of the dose-response curve. Plasma lipase showed a maximal response that was 5 times above the basal level, while the plasma amylase level was increased only by 50% at the maximal response. Computed ED₅₀ of CCK-8 for each enzyme confirmed this relative sensitivity of the response: 3.0, 8.7, 11.0 IDU/kg/h for ICT, lipase, and amylase, respectively. Plasma levels of amylase and lipase did not change significantly in response to the intake of either a liquid diet or fiber pellets containing no caloric value. Plasma ICT levels, however, were elevated significantly by 23 and 53% at the time when the liquid diet or fiber pellets were given and when cephalic stimulation appeared maximally induced. The increased levels declined thereafter and were no longer significantly different from the basal levels for postprandial 2 h. These results indicate that the response patterns of plasma ICT, amylase, and lipase to CCK-8 appear to parallel that of exocrine protein secretion and that plasma ICT levels provide superior sensitivity over amylase and lipase determination as a plasma parameter for either pharmacological or physiological stimulation of the exocrine pancreas. Furthermore, cephalic stimuli have been shown to mediate the response to food intake.

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Serum trypsin, α-amylase and lipase during bombesin stimulation in normal subjects and patients with pancreatic insufficiency

Cited by 13 publications

References 11 publications

Effect of Atropine and Somatostatin on Bombesin-Stimulated Plasma Immunoreactive Trypsin Release in Man

Effect of Atropine and Somatostatin on Bombesin-Stimulated Plasma Immunoreactive Trypsin Release in Man

Stimulatory Effects of Bombesin on Plasma Trypsin Release and Exocrine Pancreatic Secretion in Dogs

Effects of Cholecystokinin, Food Intake and Cephalic Stimuli on Plasma Levels of Amylase, Lipase, and Immunoreactive Cationic Trypsinogen in Rats

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