scholarly journals Pancreatic enzyme secretion in response to test meals differing in the quality of dietary fat (olive and sunflowerseed oils) in human subjects

1997 ◽  
Vol 78 (1) ◽  
pp. 27-39 ◽  
Author(s):  
M. D. Yago ◽  
M. V. Gonzalez ◽  
E. Martinez-Victoria ◽  
J. Mataix ◽  
J. Medrano ◽  
...  
Keyword(s):  
Dietary Fat ◽  
Enzyme Activities ◽  
Human Subjects ◽  
Pancreatic Enzyme ◽  
Enzyme Secretion ◽  
Sunflowerseed Oil ◽  
Before And After ◽  
Pancreatic Enzyme Secretion ◽  
Fat Composition

The aim of the present study was to investigate in human subjects whether or not the ingestion of two liquid meals that differed only in their fatty acid composition (due to the addition of olive oil (group O) or sunflowerseed oil (group S) as the source of dietary fat) would lead to differences in the pancreatic enzyme activities secreted into the duodenum. The experiments were performed in eighteen cholecystectomized subjects who, during the 30d period immediately before surgery, modified their habitual diets in such a way that their fat composition would reflect, as far as possible, that of the experimental meals. Lipase (EC3.1.1.3), colipase, amylase (EC3.2.1.1), chymotrypsin (EC3.4.21.1) and trypsin (EC3.4.21.4) activities were measured in duodenal contents aspirated before and after the ingestion of the test meals. The plasma levels of secretin and cholecystokinin (CCK) were also examined. Duodenal enzyme activities were similar in resting conditions. No significant differences were revealed in postprandial enzyme activities, except for lipase activity, which was higher in group O, probably in relation to the greater plasma CCK concentrations observed in this group. In the absence of enzyme output data, we should not exclude the possibility that the type of dietary fat will affect human pancreatic enzyme secretion to a greater extent than is evident from the present study, for instance through a flow-mediated effect, as we previously observed in dogs.

Effect of beer, yeast-fermented glucose, and ethanol on pancreatic enzyme secretion in healthy human subjects

1996 ◽  
Vol 41 (6) ◽  
pp. 1216-1224 ◽  
Author(s):  
S. T. Chari ◽  
H. Harder ◽  
S. Teyssen ◽  
C. Knodel ◽  
R. L. Riepl ◽  
...  
Keyword(s):  
Human Subjects ◽  
Pancreatic Enzyme ◽  
Enzyme Secretion ◽  
Healthy Human ◽  
Healthy Human Subjects ◽  
Pancreatic Enzyme Secretion ◽  
Beer Yeast

Pancreatic enzyme synthesis and turnover in human subjects

1994 ◽  
Vol 266 (5) ◽  
pp. G816-G821 ◽  
Author(s):  
S. J. O'Keefe ◽  
W. M. Bennet ◽  
A. R. Zinsmeister ◽  
M. W. Haymond
Keyword(s):  
Animal Studies ◽  
Turnover Rate ◽  
Human Subjects ◽  
Pancreatic Enzyme ◽  
Enzyme Synthesis ◽  
Enzyme Secretion ◽  
Digestive Process ◽  
Healthy Humans ◽  
Pancreatic Enzyme Secretion ◽  
Secreted Enzymes

Animal studies have shown that pancreatic enzyme secretion is independent of enzyme synthesis. To investigate this relationship in humans, we have coinfused 14C-labeled leucine tracer with cholecystokinin octapeptide in nine healthy adults for 4 h and measured the rate of appearance of secreted and newly labeled enzymes in the duodenum. Enzyme secretion was well maintained throughout, but newly labeled enzymes only appeared in juice between 75 and 101 min (median time, 86 min), indicating that initial secretion was dependent on the release of zymogen stores and that the median production time for new enzymes was 86 min. Between 85 and 225 min there was a curvilinear increase in the enrichment of secreted enzymes with newly synthesized enzymes, suggesting a median turnover rate of zymogen stores of 29%/h (range 12-47%/h). In conclusion, our results suggest that in healthy humans, postprandial pancreatic enzyme secretion is maintained by the export of a large stored pool and is not rate limited by enzyme synthesis, since it takes approximately 86 min for newly synthesized enzymes to take part in the digestive process.

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

2020 ◽  
Vol 1 (30) ◽  
pp. 30-36
Author(s):  
E. A. Krylova ◽  
D. V. Aleinik
Keyword(s):  
Endoscopic Retrograde Cholangiopancreatography ◽  
Intravenous Infusion ◽  
Pancreatic Enzyme ◽  
Enzyme Secretion ◽  
Continuous Intravenous Infusion ◽  
Endoscopic Retrograde ◽  
Pancreatic Enzyme Secretion

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.

Pancreatic polypeptide inhibits pancreatic enzyme secretion via a cholinergic pathway

1987 ◽  
Vol 253 (5) ◽  
pp. G706-G710 ◽  
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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