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:3.4.21.4 (trypsin)
42,187 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We have confirmed again that bile and trypsin injected in dogs under high pressure produce highly lethal necrotizing pancreatitis responsive to fluid resuscitation. Animals undergoing pancreatectomy show a reduction in serum amylase levels and hemoconcentration (reflected in hematocrit levels) after pancreatectomy, an effect that may be related to removal of the source of vasoactive substances liberated in pancreatitis. Qualitatively, survivors of pancreatectomy exhibit accelerated convalescence. Pancreatectomy, however, does not increase survival once the disease process is established and may be harmful. This experimental study does not support the clinical use of pancretectomy but rather emphasizes the utility of adequate fluid resuscitation in the treatment of severe pancreatitis.
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PMID:Ablative surgery for necrotizing pancreatitis. 124 48

Chronic experiments were conducted on dogs with pancreatic fistulae; secretion of the pancreas (basal and stimulated by duodenal perfusion by acid solutions, albumin and its polypeptide hydrolysate) was investigated with consideration to its enzyme (amylase, trypsin, chymotrypsin) secretion. The polypeptide hydrolysate proved to stimulate the pancreatic enzymes more than pure protein. Barbamyl, chlorpromazine and amyzyl inhibited both the basal and the stimulated secretion of the pancreas. The differential character of the pancreatic enzyme secretion was most disturbed by chlorpromazine and amizyl; this served as an evidence of the substantial role of the central adrenergic and cholinergic structures in the adaptation of the pancreatic secretion to food stimuli.
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PMID:[The effect of several neurotropic preparations on the differential character of pancreatic enzyme secretion]. 124 82

The effect of dietary protein intake on abnormal endocrine pancreatic function was studied in five male chronic alcoholic patients with a recent history of heavy alcohol and poor dietary intake. Pancreatic function was assessed by means of the pancreozymin-secretin stimulation test. Immediately on admission and throughout the study, the patients were given ethanol, 250 g/day in divided doses. Initial administration of a low protein (25 g) 1800 calorie diet resulted in no improvement in pancreatic function. Institution of a normal protein (100 g) 2600 calorie diet for 10 days led to a return to normal in the output of bicarbonate, amylase, lipase, and chymotrypsin. Readministration of the low protein diet for 10 days resulted in decreased output of amylase and chymotrypsin. The volumes of secretion and outputs of trypsin and protein remained unchanged throughout the study. This study shows that the transient dysfunction of the exocrine pancreas frequently observed in actively drinking chronic alcoholic patients is caused by deficient dietary protein intake.
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PMID:Changes in endocrine pancreatic function produced by altered dietary protein intake in drinking alcoholics. 124 78

The effect of long-term oral trypsin inhibitor administration on the exocrine pancreas was studied in unoperated rats and in rats operated on by a 30% proximal small intestinal resection. The following observations were made: in unoperated rats sacrificed 18 hours after the last trypsin inhibitor ingestion there was an increase of the wet weight of pancreas, increase of the pancreatic protein, and an increase of pancreatic and intestinal trypsin(ogen) and of pancreatic amylase by comparison with the controls. In operated rats, treated and examined in an identical way, no influences on the exocrine pancreas were found. It is suggested that the abolishment of the trypsin inhibitor effects on the exocrine pancreas in operated rats reflects the removal of the site of production of one or more intestinal hormone(s) or factor(s) responsible for these effects. In unoperated rats examined 4 hours after the last trypsin inhibitor ingestion a reduction of the pancreatic trypsinogen and amylase and an increase of the intestinal amylase were found, indicating a secretory response of the pancreas to the intraluminal trypsin inhibitor; the low values of intestinal trypsin found in these rats probably reflect inhibition of rat trypsin by the bovine lung trypsin inhibitor.
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PMID:Abolishment of oral trypsin inhibitor stimulation of the rat exocrine pancreas after duodeno-jejunal resection. 125 Nov 28

A highly purified amylase protein inhibitor from the kernels of hexaplois wheat, designated 0.19 according to its gel electrophoretic mobility, has been characterized according to its circular dichroism spectra determined at different pH values and in the presence or absence of dissociating and reducing agents. The 0.19 albumin has also been characterized according to the specificity with which it inhibits 21 alpha-amylases from different origins and according to its sensitivity to a number of chemical and enzymatic treatments of its inhibitory action on human saliva and Tenebrio molitor L. larval midgut alpha-amylases. Inhibitory activity of 0.19 toward human saliva amylase significantly increased when the inhibitor was incubated with the enzyme before the addition of starch, but it was not affected by the preincubation of 0.19 with starch. Maltose reversed the inhibition of human saliva by 0.19 and showed some inhibitory activity toward the enzyme. However, maltose concentrations that only slightly affected amylase activity were very effective in restoring the amylase activity inhibited by 0.19. The inhibitory action of 0.19 on human saliva and T. molitor L. amylases were equally resistant to trypsin and thermal treatments, but 0.19 was readily inactivated by incubation with pepsin or by reduction of disulfide bonds. The inhibition of the mammalian amylase by 0.19 was adversely affected by a treatment with CNBr (1:100 ratio of methionine residues to CNBr) whereas the inhibition of the insect amylase was not. As shown by circular dichroism measurements in the far ultraviolet, 0.19 is a protein with about 50% of ordered structure. Significant and largely reversible changes have been observed in the aromatic CD spectrum of 0.19 at alkaline pH values or in the presence of sodium dodecyl sulfate. These changes, which were associated with a partial loss of inhibitory activity, indicate that ionizable tyrosine groups contribute significantly to the ellipticity bands of 0.19 in the near ultraviolet.
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PMID:Further characterization studies of the alpha-amylase protein inhibitor of gel electrophoretic mobility 0.19 from the wheat kernel. 125 58

Ten patients with a well-established ileostomy were studied in a metabolic ward and alterations in ileostomy contents of trypsin and bile acids were measured during the ingestion of an elemental diet. After a 4-day control study the patients were given an elemental diet as the sole nutritional source for a 10-day period. For the last 3 days of the study an additional 2 litres of water were consumed with the elemental diet. The mean daily faecal output for the group during the control period was 578 +/- 300 ml, and during administration of the elemental diet the fistula output fell to 418 +/- 190 ml (P less than 0-02) and there was a fall in the concentration of sodium in the ileal fluid (104-7 +/- 22 mEq/l to 80-2 +/- 25 mEq/l, P less than 0-01). For the group as a whole there was a fall in the concentration of trypsin (0-671 +/- 0-53 i.u./ml to 0-554 +/- 0-56 i.u./ml, P less than 0-025) and bile acids (0-911 +/- 0-56 mmol/ml to 0-662 +/- 0-53 mmol/ml, P less than 0-005) in the ileal excreta. Althoug the concentration of amylase in the ileal fluid rose, the total output was not altered. Oral administration of an additional 2 litres of water did not later the concentration of trypsin or bile acids in the ileal fluid. It is concluded that elemental diet ingestion produces changes in ileal fistula output which are of benefit to the patient with an enterocutaneous fistula. Output from the fistula of fluid and electrolyte is less and the corrosive nature of the discharge is reduced.
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PMID:Decreased trypsin and bile acids in ileal fistula drainage during the administration of a chemically defined liquid elemental diet. 125 13

A new experimental model has been found whereby acute hemorrhagic pancreatic necrosis with fat necrosis is induced in 100% of young female mice fed a choline-deficient diet supplemented with 0.5% DL-ethioine. The onset of the pancreatic necrosis has been shown to follow accumulation, and subsequent activation, of pancreatic zymogens with intraparenchymal formation of significant amounts of elastase, chymotrypsin, and trypsin. Evidence was obtained that the proteolytic enzymes are released also in the circulation and cause a significant drop in the content of the serum protease inhibition alpha 1-antitrypsin and alpha2-macroglobulin. Increased levels of plasma amylase were found to accompany the onset of the pancreatic necrosis.
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PMID:Acute hemorrhagic pancreatic necrosis in mice. Intraparenchymal activation of zymogens, and other enzyme changes in pancreas and serum. 126 63

This study was undertaken to investigate the incidence of postoperative hyperamylasemia and amylase levels of intraperitoneal drainage in 106 patients undergoing major abdominal surgery. The results were as follows: 1. Postoperative hyperamylasemia was found in 36.8% of all patients, with higher incidence of hyperamylasemia being in accordance with greater surgical intervention to the pancreas. 2. The isoamylase pattern of postoperative hyperamylasemia was dominant in the salivary type. 3. The levels of such serum pancreatic enzymes as lipase, trypsin and elastase 1 were higher in the pancreatic-type group than in the salivary-type group, particularly with the elastase 1 levels being statistically higher in the former. 4. Increases in peritoneal amylase activity were found in those cases of greater surgical intervention to the pancreas, postoperative hyperamylasemia and higher serum pancreatic isoamylase levels. 5. Diagnosis of postoperative pancreatitis was confirmed in one case by clinical and laboratory findings and CT examination. It might be concluded that postoperative high peritoneal amylase levels suggest occurrence or possible occurrence of postoperative pancreatitis.
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PMID:[Postoperative hyperamylasemia in patients undergoing abdominal surgery: the relationship between serum and peritoneal amylase levels]. 127 73

The effects of emeriamine, a new anti-diabetic drug, on exocrine and endocrine pancreatic function in normal and diabetic rats have been studied both in vivo and in vitro. It was found that emeriamine dose-dependently normalized the symptoms of hyperingestion and hyperposia in streptozotocin (STZ)-induced diabetic rats, with fasting glucose levels significantly decreased and insulin levels not changed. In STZ-induced diabetic rats, there was a significant increase in pancreatic lipase and trypsin contents and a sharp decrease in amylase content. These changes in lipase and trypsin, but not in amylase were normalized by administration of emeriamine. In the normal rat, emeriamine had no effect on either serum glucose or insulin levels, but significantly decreased the pancreatic amylase, lipase as well as trypsin contents by 68%, 58% and 51%, respectively. In vitro, emeriamine (10(-8) - 10(-4) mol l-1) had no effect on enzyme release from pancreatic acini either under basal or carbachol-stimulated conditions. Emeriamine inhibited glucose-induced insulin release from isolated pancreatic islets. In conclusion, emeriamine has an inhibitory effect on synthesis of pancreatic enzymes and on glucose-stimulated insulin release.
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PMID:Effect of emeriamine on exocrine and endocrine pancreatic function in normal and diabetic rats. 128 Aug 55

The presence of the enzymatically active allergens equivalent to Der p I (cysteine protease), Der p III (serine protease) and amylase in extracts of Dermatophagoides pteronyssinus, D. farinae and Euroglyphus maynei was determined using appropriate enzymatic techniques. Biochemical equivalents of all three allergens were present in each extract studied. Studies also showed that the mite extracts contained a variety of other biochemically active enzymes including trypsin, chymotrypsin, carboxypeptidase A and B, glucoamylase and lysozyme. Marked differences in the relative concentrations of some of these enzymes in different mite extracts were observed, particularly trypsin and carboxypeptidase A. The enzymes were physicochemically similar to equivalent enzymes from vertebrate and invertebrate sources. Chromatofocusing studies of faecal extracts derived from D. pteronyssinus and D. farinae showed that several isoforms of each enzyme were present. The data indicated that there were more trypsin isoforms, with pI over a wider range, in extracts prepared from D. pteronyssinus. Proteases and carbohydrases were also found in extracts prepared from faecally enriched material suggesting that they were endoperitrophic and associated with mite digestion. The data suggest that not only are the group I, III and amylase allergens a consistent feature of most pyroglyphid dust mites but also that other proteases and carbohydrases present in mite faeces are allergenic.
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PMID:A comparative study of allergenic and potentially allergenic enzymes from Dermatophagoides pteronyssinus, D. farinae and Euroglyphus maynei. 128 68


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