Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.4.21.1 (chymotrypsin)
10,938 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The mechanisms of pancreatic adaptation to dietary changes and whether these changes are reflected in the serum are not fully understood. The present study investigates secretagogue-induced release of digestive enzymes from dispersed pancreatic acini as well as the concentrations of these enzymes in serum and pancreas after adaptation to a high protein diet. Adult rats were fed an 8.5% casein diet ad libitum. After 14 d the rats were divided into three groups and fed isoenergetic diets constituting 8.5, 24 or 40% protein for an additional 6 d. No significant differences in final body weight or pancreatic weight were observed among the groups of rats. Rats adapted to the 40% protein diet showed significantly higher trypsin and chymotrypsin activity in pancreatic homogenates than rats fed the 8.5% protein diet. These changes in pancreatic enzyme content were not reflected in serum. Pancreatic acini isolated from the 8.5% protein group showed a markedly reduced responsiveness to cholecystokinin (CCK-8), secretin- and carbachol-induced enzyme release in comparison to the other two dietary groups, although basal enzyme release was the same in all groups. These results indicate that the secretion of pancreatic enzymes following a physiological stimulus is affected by a low protein, high carbohydrate diet.
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PMID:Secretagogue-induced enzyme release from the exocrine pancreas of rats following adaptation to a high protein diet. 245 Sep 76

The present study investigates the effects of nicotine treatment on exocrine pancreatic function. Adult male, Sprague-Dawley rats received nicotine via a time-release pellet, at a rate of 1.65 micrograms/min for 3 weeks. At the end of the experimental period, it was observed that although nicotine did not affect final body or pancreatic weight, the activities of amylase, trypsin, and chymotrypsin in pancreatic homogenates from nicotine-treated rats were 51, 29, and 35% higher, respectively, than in controls. Levels of immunoreactive cationic trypsin(ogen) were significantly higher in pancreatic homogenates and serum from nicotine-treated rats as compared with controls. In addition, concentrations of mRNA, encoding for pancreatic amylase, were higher in pancreatic homogenates from the nicotine-treated rats than in controls. In dispersed pancreatic acini isolated from nicotine-treated rats, basal secretion of amylase, trypsinogen, and chymotrypsinogen was 50% higher than controls and enzyme release following CCK-8 (100 pM), secretin (1 microM), and carbachol (7.5 microM) stimulation was also significantly higher. These data indicate that nicotine treatment, at levels comparable to those expected in moderate cigarette smokers, increases the content of digestive enzymes in rat pancreas, as well as their basal and secretagogue-induced release.
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PMID:Altered exocrine pancreatic function in rats treated with nicotine. 246 Sep 70

In order to evaluate impairment of exocrine pancreatic function during aging, 27 subjects (mean age: 36 years +/- 7.8) and 28 subjects (mean age: 72 years +/- 3.2), with no clinical or radiological evidence of digestive disease, were selected. Duodenal aspirates over a 60 min period were obtained during continuous IV infusion of secretin (0.5 U/kg/h) and caerulein (75 ng/kg/h). Bicarbonate, lipase, chymotrypsin amylase concentrations and output were measured. Bicarbonate, lipase, chymotrypsin concentrations in the aged group were significantly reduced by 17%, 15% and 23% respectively (P less than 0.05) as compared with those in the young group. In addition, a significant reduction of approximately 45% in bicarbonate and enzyme output levels was observed. This study provides strong evidence for a marked functional involution of the exocrine pancreatic secretion during aging. The potential consequences of this phenomenon on the nutritional status in the elderly are discussed.
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PMID:Exocrine pancreatic secretion in the elderly. 246 56

In order to investigate whether the human pancreas is capable of adapting to a diet with high-carbohydrate, low-fat, and normal protein content, 10 healthy volunteers were given a defined elemental diet (60% of calories as carbohydrates, 22% as fat, and 18% as protein) for 7 d. For the next 7 d they received an elemental diet with a further increased carbohydrate content (76% of calories) and a decreased fat content (10% of calories). A complete secretin-pancreozymin test was carried out at the end of the first wk and at d 14. The results show that an increase in dietary carbohydrate does not provoke an adaptational response of stimulated secretion rates of amylase, trypsin, and chymotrypsin in humans, as expected from animal experiments.
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PMID:High amount of dietary carbohydrate does not cause an adaptational increase of stimulated human pancreatic amylase secretion. 247 55

In the present study, we examined the interaction between CCK-8 and natural or synthetic secretin on pancreatic enzyme secretion. On anaesthetized rats, a proximal duodenal segment was continuously perfused with saline and amylase, lipase, trypsin, and chymotrypsin were determined in the perfusate. Neither during iv saline nor during iv secretin (natural or synthetic) at doses of 0.01, 0.05, or 0.1 CU/kg/h, any of the four enzymes changed significantly from basal values over a period of 100 min. Iv CCK-8 at stepwise increasing doses of 5, 10, and 20 pmol/kg/h elicited a significant increase of all four enzymes at the medium dose, with a further increase of amylase and trypsin, but not lipase and chymotrypsin at 20 pmol/kg/h. The addition of secretin at all 3 doses potentiated CCK-induced trypsin output. The effects of natural secretin were more pronounced than those of the synthetic peptide. Secretin significantly increased amylase secretion over basal at the lowest dose of CCK-8 (5 pmol/kg/h) that by itself had no effect on amylase release. Only the higher doses of natural but not synthetic secretin augmented lipase secretion during the lowest dose of CCK-8. Both forms of secretin had no further stimulatory effect on CCK-induced chymotrypsin secretion. The present data demonstrate that, first, in rats a potentiation of CCK-8-induced enzyme secretion by low doses of secretin is different for the four enzymes, which suggests a differential regulatory action of these two intestinal hormones on pancreatic enzyme release. Second, the different effects of natural secretin may represent those of contaminants suggesting that only synthetic secretin should be employed in future studies of this peptide on pancreatic enzyme secretion.
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PMID:Effects of CCK-8 in combination with natural or synthetic secretin on amylase, lipase, trypsin, and chymotrypsin secretion in rats. 247 18

Oral pancreatic enzyme replacement therapy generally benefits patients with severe pancreatic deficiency. However, the fate of oral pancreatic supplements in the digestive lumen and their possible effects on circulating gut hormones are only partially known. The purpose of this article is to validate an experimental model that produces total pancreatic insufficiency in pigs, and to study the fate of orally administered Eurobiol, a whole pancreas lyophilized preparation, and its effects on circulating plasma levels of five digestive hormones. Pancreatic insufficiency was created by pancreatic duct ligation, and the duodenal, jejunal and ileal contents were sampled through cannulas before a normal meal and 0.5-24 h later. Blood samples were taken at the same times, and plasma neurotensin, pancreatic polypeptide, secretin, cholecystokinin (CCK), and gastrin were measured. In pigs with pancreatic insufficiency, Eurobiol, given during the meal, induced a significant increase in all enzyme activities in the duodenum and the jejunum, and in the levels of amylase, trypsin, and chymotrypsin in the ileum, relative to placebo. In the duodenum, the peak concentrations of enzyme activities were 19, 11, 17, and 29% (p less than 0.001) of the postprandial peak activities measured in control pigs with an intact pancreas for lipase, amylase, trypsin, and chymotrypsin, respectively. In the jejunum, the same activities were, respectively, 30, 11, 25, and 36% (p less than 0.01-0.001) of normal peaks. In pigs with pancreatic insufficiency, basal and integrated meal-stimulated neurotensin levels were increased; basal, peak, and integrated meal-stimulated pancreatic polypeptide and secretin levels were increased, whereas gastrin and CCK were not different from controls.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Total pancreatic insufficiency in pigs: a model to study intestinal enzymes and plasma levels of digestive hormones after pancreatic supplementation by a whole pancreas preparation. 247 98

The byproducts P-1 and P-2, which were produced during the synthesis of porcine secretin, were isolated in pure form from the crude secretin by HPLC. These were identified by a combination of amino acid analysis, enzymatic digestion, and isocratic or linear gradient reversed-phase (RP)-HPLC. The amino acid compositions of P1 and P2, determined by amino acid analysis after acid hydrolysis, were found to be the same as those of porcine secretin without distinction between L-and D-amino acids. But, HPLC of their digestive fragments with trypsin and alpha-chymotrypsin differed from that of secretin. The fragments, S7-12 of P-1 and S13-21 of P-2 were determined to be different from the corresponding fragments obtained from secretin by HPLC analysis of their digestive fragments. The amino acid composition of each acid hydrolysate, following digestion with D-amino acid oxidase, was found to have less leucine or alanine content than secretin. The HPLC analysis of the fragments from P-1 and P-2 by tryptic and alpha-chymotryptic digestion showed that they are the same as those from synthetic D-Leu10 secretin or D-Ala17 secretin, respectively. Consequently, P-1 and P-2 are concluded to be the secretin diastereoisomers, D-Leu10 and D-Ala17 secretin, respectively.
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PMID:Identification of secretin diastereoisomers produced during synthesis. 256 77

In order to investigate whether the human exocrine pancreas is capable of adapting to a diet with a high-carbohydrate, low-fat, and normal protein content, 10 healthy subjects were given a continuous intraduodenal infusion of such a dietary composition (8760 kJ in 2400 ml/day) via a portable infusion pump over a period of 10 days. The diet consisted of 76% of calories as carbohydrates (80% oligosaccharides, 20% mono- and disaccharides), 10% as fat (more than 90% C18 fatty acids) and 14% as protein (oligo- and polypeptides; 11.8 g nitrogen per day). A complete pancreozymin-secretin test was carried out before and after the experimental period. The results show that the above dietary regimen leads to a significant (P less than 0.05) increase in the stimulated secretion rates of trypsin and chymotrypsin, whereas, in contrast to the findings in animal experiments, no change could be measured in the secretion rates of amylase and lipase.
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PMID:Lack of adaptive changes in human pancreatic amylase and lipase secretion in response to high-carbohydrate, low-fat diet applied by a 10-day continuous intraduodenal infusion. 257 20

Fecal chymotrypsin (FCT) has been measured by a new photometric method (Monotest Chymotrypsin; Boehringer, Mannheim) in 78 patients: 44 with chronic pancreatitis and 34 not affected by any pancreatic disease. The results were compared with those from other tests of pancreatic secretory (secretin-cerulein test) and digestive [serum and urinary p-aminobenzoic acid (PABA) and pancreolauryl] capacity. When FCT values were severely reduced (below 6.7 U/g), from 90 to 100% of the patients also presented abnormal pancreatic secretory and digestive capacity. On the other hand, 87% of the patients with normal FCT (above 20 U/g) presented normal secretory and digestive capacity. Patients with intermediate FCT values (between 6.7 and 20 U/g) showed normal or abnormal pancreatic secretory and digestive capacity with the same probability. Therefore, FCT, carried out as a first test, seems to identify subjects that need no further pancreatic function tests (normal and severely impaired FCT) and patients who need other more complex functional investigations (intermediate FCT values).
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PMID:The fecal chymotrypsin photometric assay in the evaluation of exocrine pancreatic capacity. Comparison with other direct and indirect pancreatic function tests. 273 75

Two groups of biological methods are commonly used to evaluate the exocrine pancreatic function: tests which require tubes for the collection of duodenal juice and the tubeless tests which are indirect tests of pancreatic function. In this study we have attempted to improve a new test: the test of haptocorrin degradation (THD). This test measures the transfer of labelled cobalamin from haptocorrin to the intrinsic factor which is provoked by the degradation of the haptocorrin by proteases in the duodenal juice. We present the results of this test in 90 patients with chronic pancreatitis. THD was first assayed with basal duodenal juice collected by naso duodenal tubing during secretin cerulein stimulation. In this study the sensitivity and specificity of THD was 0.86 and 0.93, respectively. In the second part of this study we demonstrated that the means of collecting duodenal juice had no effect on the results of THD. Duodenal juice was collected during a secretin cerulein test or during a routine upper gastrointestinal endoscopy after pancreatic stimulation with secretin. The sensitivity and specificity of THD was 0.90 and 0.94, respectively, when duodenal juice was collected during endoscopy. THD was significantly correlated with the NBT-PABA test, steatorrhea, and with the activity of trypsin and chymotrypsin in the duodenal juice. In this study, NBT-PABA was less sensitive than THD for the diagnosis of chronic pancreatitis (sensitivity was 0.70 and 0.89, respectively). The specificity of THD was estimated at 0.94. THD seemed to be a valuable adjunct to test pancreatic function. As upper gastrointestinal endoscopy is usually performed in patients with proved or suspected chronic pancreatitis, THD seems to have a place of choice among the other tests of pancreatic exocrine function. Further evaluation of this test by a multicentric prospective trial is now needed.
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PMID:[Evaluation of exocrine pancreatic function by the haptocorrin degradation test of the duodenal fluid collected by endoscopy]. 273 91


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