Efficacy of octreotide (Octrade) for prevention of pancreatitis after endoscopic retrograde cholangiopancreatography

The article presents the results of a study of the effectiveness of the use of an inhibitor of pancreatic enzyme secretion of octreotide (Octrade) for the prevention of pancreatitis after endoscopic retrograde cholangiopancreatography (ERCP). It was shown that the administration of Octrade at a dose of 0.3 mg in 500 ml of 0.9 % NaCl by continuous intravenous infusion for 7 hours and then 0.1 mg of Octrade subcutaneously at 6 and 12 hours after the end of intravenous infusion significantly reduced the frequency of pancreatitis (4.0 % and 22.2 %; p < 0.05) and hyperamylasemia (8.0 % and 25.9 %; p < 0.05) after ERCP. It is concluded that Octrade is effective in preventing the development of pancreatitis and hyperamilasemia after ERCP.

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Cholecystokinin mediates feedback regulation of pancreatic enzyme secretion in rats

AJP Gastrointestinal and Liver Physiology ◽

10.1152/ajpgi.1986.250.2.g252 ◽

1986 ◽

Vol 250 (2) ◽

pp. G252-G259 ◽

Cited By ~ 10

Author(s):

D. S. Louie ◽

D. May ◽

P. Miller ◽

C. Owyang

Keyword(s):

Negative Feedback ◽

Intravenous Infusion ◽

Pancreatic Secretion ◽

Pancreatic Enzyme ◽

Feedback Regulation ◽

Enzyme Secretion ◽

Negative Feedback Regulation ◽

Plasma Cholecystokinin ◽

Pancreatic Enzyme Secretion ◽

Protein Output

Previous studies have shown that trypsin and chymotrypsin in the duodenum exert a negative-feedback regulation on pancreatic enzyme secretion in the rat. The mechanism responsible for this physiological phenomenon is unknown. By use of a specific and sensitive bioassay based on amylase release from isolated pancreatic acini, the role of cholecystokinin in the negative-feedback regulation of exocrine pancreatic secretion was examined. Rats were prepared with duodenal cannulas and pancreaticobiliary cannulas. Diversion of pancreaticobiliary juice resulted in a threefold increase in pancreatic protein output and an increase of plasma cholecystokinin from a basal level of 0.5 +/- 0.08 pM cholecystokinin octapeptide (CCK-8) to 16 +/- 4 pM CCK-8. Perfusion of trypsin (2 mg/h) or pancreaticobiliary juice returned pancreatic protein output to basal levels and plasma cholecystokinin to 2.1 +/- 1.2 and 0.33 +/- 0.1 pM, respectively. The inhibitory effect of trypsin on cholecystokinin release was enzyme and site specific, since inhibition of cholecystokinin release was not observed with perfusion of amylase into the duodenum or with trypsin into the ileum. Intravenous infusion of proglumide abolished the increase in pancreatic secretion following diversion of pancreaticobiliary juice. Intraduodenal perfusion of lidocaine, infusion of tetrodotoxin into the superior mesenteric artery, or intravenous infusion of atropine inhibited the rise in plasma cholecystokinin seen with diversion of pancreaticobiliary juice. These studies suggest that feedback regulation of pancreatic enzyme secretion in the rat is mediated by release of cholecystokinin. Furthermore, the feedback mechanism is neurally mediated, involving a cholinergic pathway.

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MELATONIN METABOLITE; N1-ACETYL-N2-FORMYL-5-METHOXYKYNURAMINE STIMULATES PANCREATIC ENZYME SECRETION VIA CCK RELEASE. STUDY ON THE RATS.

10.26226/morressier.59a6b342d462b80290b53f8f ◽

2017 ◽

Author(s):

Jolanta Maria Jaworek

Keyword(s):

Pancreatic Enzyme ◽

Enzyme Secretion ◽

Pancreatic Enzyme Secretion ◽

Release Study ◽

Cck Release

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Mechanism of galanin's inhibitory action on pancreatic enzyme secretion: modulation of cholinergic transmission--studies in vivo and in vitro.

Gut ◽

10.1136/gut.34.11.1616 ◽

1993 ◽

Vol 34 (11) ◽

pp. 1616-1621 ◽

Cited By ~ 17

Author(s):

K H Herzig ◽

G Brunke ◽

I Schon ◽

M Schaffer ◽

U R Folsch

Keyword(s):

Inhibitory Action ◽

Pancreatic Enzyme ◽

Enzyme Secretion ◽

Cholinergic Transmission ◽

Pancreatic Enzyme Secretion ◽

Transmission Studies

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Pancreatic polypeptide inhibits pancreatic enzyme secretion via a cholinergic pathway

AJP Gastrointestinal and Liver Physiology ◽

10.1152/ajpgi.1987.253.5.g706 ◽

1987 ◽

Vol 253 (5) ◽

pp. G706-G710 ◽

Cited By ~ 3

Author(s):

G. Jung ◽

D. S. Louie ◽

C. Owyang

Keyword(s):

Pancreatic Polypeptide ◽

Acetylcholine Release ◽

Pancreatic Enzyme ◽

Enzyme Secretion ◽

Dependent Manner ◽

Amylase Release ◽

Opioid Receptor Antagonists ◽

Cholinergic Pathway ◽

Pancreatic Enzyme Secretion ◽

Dose Dependent

In rat pancreatic slices, rat pancreatic polypeptide (PP) or C-terminal hexapeptide of PP [PP-(31-36)] inhibited potassium-stimulated amylase release in a dose-dependent manner. The inhibition was unaffected by addition of hexamethonium but blocked by atropine. In contrast, PP(31-36) did not have any effect on acetylcholine- or cholecystokinin octapeptide-stimulated amylase release. In addition, when pancreatic slices were incubated with [3H] choline, PP(31-36) inhibited the potassium-evoked release of synthesized [3H] acetylcholine in a dose-dependent manner. The inhibitory action of PP was unaffected by adrenergic, dopaminergic, or opioid receptor antagonists. Thus PP inhibits pancreatic enzyme secretion via presynaptic modulation of acetylcholine release. This newly identified pathway provides a novel mechanism for hormonal inhibition of pancreatic enzyme secretion via modulation of the classic neurotransmitter function.

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