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
Query: EC:3.4.21.4 (
trypsin
)
42,187
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Gastric juice from 15 normals, 20 patients with gastric ulcer and 14 patients with erosive haemorrhagic gastroduodenitis was investigated in respect of its activity on unheated and heated fibrin plates and its content of FDP and plasminogen or plasmin with immunochemical methods. Gastric juice from normals showed no activity on unheated and heated fibrin plates, and no FDP or plasminogen could be demonstrated. In the patients with gastric ulcer the gastric juice showed little or no fibrinolytic activity on fibrin plates except in 2, who had
regurgitation
of duodenal juice and neutral pH of the juice. These patients had equally high activity on heated as on unheated plates and no plasmin could be demonstrated. It was shown that this activity was not due to fibrinolysis, but to non-specific proteolytic activity (probably
trypsin
). The patients with erosive haemorrhage gastroduodenitis exhibited quite a different picture. The gastric juice from these patients showed extremely high activity on fibrin plates, the activity was higher on unheated than on heated plates. The activity was inhibited in vitro by addition of EACA and in vivo after administration of AMCA. The occurence of plasmic could be demonstrated directly immunologically in the gastric juice. By comparsion of plasmin and
trypsin
in various assays it could further be improved that the gastric juice in these cases contained plasminogen activator and plasmin. The patients with erosive haemorrhagic gastroduodenitis showed no increase in fibrinolysis in the blood, but low values for plasminogen and alpha2-M, and the serum contained FDP. These findings in the blood and gastric juice were interpreted as signs of local fibrinolysis in the stomach and duodenum. There is reason to assume that this gastric fibrinolysis contributes substantially to the bleeding tendency. The effect of administration of AMCA on fibrinolytic activity and the haemorrhage lends support to the assumption of such a mechanism.
...
PMID:Gastric fibrinolysis. 0 Aug 7
Among 51 patients with refractory symptomatic reflux esophagitis seen during an 18-month period, 8 (16%) had undergone previous partial gastrectomy. Either Billroth II (n = 6) or Billroth I (n = 2) resection had been carried out for peptic ulceration 18 months to 30 years beforehand. Each patients was evaluated by symptom scoring, endoscopy, and 24-hour pH monitoring plus a 16-hour esophageal aspiration study, in which 2-hourly aliquots were measured for acid, pepsin, conjugated and unconjugated bile acids, and
trypsin
. After conversion to a 45 cm Roux-en-Y gastroenterostomy, symptom scoring and endoscopy were repeated at 6 to 12 months in all eight patients. Pepsin, acid, and unconjugated bile acids were seldom present in esophageal aspirates. Conjugated bile acids in concentrations up to 30 mmol/L and
trypsin
up to 428 micrograms/ml were found in cases of severe esophagitis, mostly during nocturnal rest. Esophagitis, heartburn,
regurgitation
, and bilious vomiting were eradicated by Roux-en-Y conversion, but other postgastrectomy symptoms (early satiety, dumping, epigastric pain, and diarrhea) were largely unchanged. Postgastrectomy esophagitis resistant to medical therapy seems likely to be caused by nocturnal exposure to
trypsin
and conjugated bile acids; it is well controlled by a 45 cm Roux-en-Y conversion.
...
PMID:Evaluation and surgical correction of esophagitis after partial gastrectomy. 172 72
Fasting serum immunoreactive
trypsin
(IRT) concentrations were measured in 35 healthy subjects. In 10 of them serum IRT levels were also evaluated after administration of secretin (GIH, 75 CU i.v. over 2 minutes); in 7 after a Lundh meal; in 12 after a standard protein meal (Liebig meat extract, 15 g in 150 ml of water) and in 13 after a glucose (1 g/Kg) oral load. Serum IRT was measured by radioimmunoassay (Trypsik kit, CIS, Sorin-Biomedica, Saluggia, Vercelli, Italy). Fasting serum IRT was 25.8 +/- 9 ng/ml (mean +/- SD). No correlation was found between age and serum IRT levels, nor were any statistical differrences observed in IRT concentration between the two sexes. A standard protein meal, Lundh meal or oral load of glucose did not provoke a significant increase in serum IRT levels. Only rapid i.v. injection of secretin was able to induce a significant rise of IRT over basal levels in healthy subjects. This behaviour is probably due more to an engorgement of the pancreatic ductal system with
regurgitation
of trypsinogen into the blood steam rather than to a direct effect of secretin on the synthesis and secretion of
trypsin
or to intestinal reabsorption of this enzyme.
...
PMID:Basal and stimulated serum immunoreactive trypsin in normal subjects. 693 49
Serum immunoreactive
trypsin
(IRT) response to secretin injection was studied in 13 patients with chronic pancreatitis with different degrees of exocrine dysfunction and in 10 control subjects. The maximal increase of serum IRT from basal values and the integrated
trypsin
output (ITO) after secretin administration were significantly correlated with the output of chymotrypsin into the duodenum during caerulein-secretin infusion (p < 0.01), but not with the output of lipase nor of bicarbonate. Serum IRT response to secretin stimulation was greater in 4 of the 5 patients with chronic pancreatitis with mild to moderate exocrine dysfunction than in the control group, suggesting an increased
regurgitation
of IRT into the blood stream by the pancreas, probably due to some degree of obstruction to pancreatic secretory flow in absence of severe acinar cell damage. Conversely, the response of serum IRT after secretin administration in 7 of the 8 patients with severe exocrine pancreatic deficiency was lower than in control subjects, probably because of the advanced distruction of the acinar pancreatic tissue. The response of serum IRT to secretin stimulation seems to vary following pancreatic function impairment and might reflect the degree of pancreatic exocrine dysfunction in chronic pancreatitis.
...
PMID:Serum immunoreactive trypsin after secretin stimulation in chronic pancreatitis. 693 52
Serum immunoreactive
trypsin
(IRT) under basal conditions and after pancreatic stimulation with secretin was studied in 10 patients with type IV hyperlipoproteinemia (HLP) and in 10 control subjects. No significant difference was observed between basal values of the two groups (p = NS). The increase of serum IRT was already significant 5 minutes after secretin administration (p < 0.01) and persisted with significance for one hour in both groups. The integrated
trypsin
output (ITO) was significantly greater in type IV HLP than in controls (510.3 +/- 17.8 and 72.2 +/ 17.6 respectively, mean +/- SEM, p < 0.0125). Only 2 (20%) of 10 patients with HLP had an ITO in the range of the controls. No significant correlation was found between ITO and triglyceride levels (p = NS). The response of serum IRT to secretin in HLP patients appears comparable to that observed in alcoholics and in patients with chronic pancreatitis with mild to moderate exocrine dysfunction, in whom there may be an abnormal
regurgitation
of
trypsin
-like material into the blood stream after secretin stimulation, probably due to an obstruction to pancreatic secretory flow. A similar obstructive mechanism may be hypothesized also in patients with HLP, but no data concerning the exocrine pancreatic secretion and the histological features of the pancreas are available to confirm this hypothesis.
...
PMID:Serum immunoreactive trypsin in type IV hyperlipoproteinemia. 693 55
Serum
trypsin
-like immunoreactivity (TLI) was studied in alcoholics without evidence of pancreatic disease and in controls. Basal values were 29 +/- 4.6 microgram/l (mean +/- S.E.M) in alcoholics and 23 +/- 4.4 microgram/l in controls (p not significant). The injection of secretin was followed by a significant increase of serum TLI in both groups; the integrated
trypsin
output (ITO) in the first hour after secretin administration was 947 +/- 403 (mean +/- S.E.M.) in alcoholics and 76 +/- 15 in controls (p less than 0.05). In 9 (75%) of the alcoholics tested, ITO was higher than the highest ITO of controls. The increase of serum TLI after injection of secretin is probably due to secretion and/or
regurgitation
of trypsinogen into the bloodstream when the pancreas is stimulated with intravenous secretin. In the light of experimental studies on chronic ethanol intoxication in animals, the increased ITO observed in alcoholics may suggest obstruction to pancreatic secretory flow in spite of the absence of any clinical sign of pancreatic disease.
...
PMID:Secretin-stimulated trypsin-like immunoreactivity in alcoholics. 722 47
Nasogastric enteral feeding is not tolerated in patients with gastric atony and in many critically-ill patients in whom gastric emptying may be delayed and in whom gastro-oesophageal
regurgitation
may lead to pulmonary aspiration of enteral feed and the development of pneumonia. Initial attempts to overcome these problems led to the development of post pyloric enteral feeding techniques with the infusion port of the tubes positioned in the duodenum. In many centres this technique is still the most practised post-pyloric enteral feeding technique. Nasoduodenal feeding tubes often retroperistalse into the stomach. The technique of choice, therefore, in these difficult patients is to position the infusion port of the feeding tube well distal to the ligament of trietz (post ligament of trietz nasojejunal enteral tube feeding). While nasogastric and nasoduodenal enteral feeding techniques have been shown to elicit a stimulatory exocrine pancreatic response, distal jejunal enteral feeding does not. During this mode of feeding the ileal brake is activated and pancreatic exocrine pancreatic secretion inhibited by the action of the released peptide YY and glucagon-like peptide-1 hormones, in turn the inhibition of pancreatic secretion being the result of inhibition of
trypsin
secretion. In the light of the findings showing the absence of a stimulatory pancreatic exocrine response to nasojejunal enteral feeding these patients should receive a predigested rather than a polymeric enteral diet.
...
PMID:Formulation of enteral diets for use in jejunal enteral feeding. 1849 70
The spatial distribution of proteolytic enzymes in the adult foregut of Protophormia terraenovae was studied in the context of protein digestion and
regurgitation
. Based on substrate specificity, pH optima, and use of specific protease inhibitors, all adults tested displayed enzyme activity in the foregut consistent with pepsin,
trypsin
and chymotrypsin. Chymotrypsin-like and
trypsin
-like enzyme activity were detected in all gut fluids and tissues tested, with chymotrypsin displaying the highest activity in saliva and salivary gland tissue, whereas maximal
trypsin
activity was evident in the crop. Pepsin-like activity was only evident in crop fluids and tissues. The activity of all three enzymes was low or undetectable (pepsin) in the fluids and tissue homogenates derived from the esophagus and cardia of any of the adults assayed. Fed adult females displayed higher enzyme activities than fed males, and the activity of all three enzymes were much more prevalent in fed adults than starved. The pH optimum of the
trypsin
-like enzyme was between pH 7.0 and 8.0; chymotrypsin was near pH 8.0; and maximal pepsin-like activity occurred between pH 1.0 and 2.0. Regurgitate from fed adult females displayed enzyme activity consistent with the proteolytic enzymes detected in crop gut fluids. Enzymes in regurgitate were not derived from food sources based on assays of bovine liver samples. These latter observations suggest that adult flies release fluids from foregut when encountering dry foods, potentially as a means to initiate extra-oral digestion.
...
PMID:Spatial characterization of proteolytic enzyme activity in the foregut region of the adult necrophagous fly, Protophormia terraenovae. 2496 46