Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0001339 (acute pancreatitis)
 10,593 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A radioimmunoassay for measurement of human pancreatic secretory trypsin inhibitor in nanogram quantities has been developed. The sensitivity of the assay now permits examination of the inhibitor content of various body fluids, wherein other methods exhibit serious short-comings. In healthy blood donors the serum level was 8.1 microgram/l. In patients with acute pancreatitis levels as high as 320 microgram/l have been measured, and patients who underwent endoscopic retrograde cholangiopancreatography showed an elevated inhibitor level in serum immediately after the examination without any clinical signs of disease, the highest registered value being 128 microgram/l. In peritoneal lavage fluid from patients with severe acute pancreatitis levels of 5-304 microgram/l have been measured. In urine the inhibitor level is about 14 microgram/l in healthy persons. The urine from one patient with proteinuria of glomerulo-tubular type contained 380 microgram/l.
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PMID:A radioimmunoassay for measurement of human pancreatic secretory trypsin inhibitor in different body fluids. 66 78

Autopsy studies have shown that approximately 56% of patients on long-term continuous ambulatory peritoneal dialysis (CAPD) develop various pancreatic abnormalities, such as acute and chronic pancreatitis, fibrosis, and acinar dilatation. This prevalence of anatomical abnormalities is similar to that observed in patients on hemodialysis and higher than that in those with normal renal function. However, clinical acute pancreatitis is an uncommon complication of CAPD (0.9%), and this prevalence is similar to that (1.7%) of patients on hemodialysis. We can attribute acute pancreatitis in CAPD patients to no single factor. Perhaps preexisting anatomical abnormalities of the pancreas make the CAPD patient susceptible to acute pancreatitis when exposed to a variety of physiological and nonphysiological influences. The diagnosis of acute pancreatitis in CAPD patients is difficult, because symptoms and signs are similar to those of dialysis-associated peritonitis. Serum amylase values three times greater than the upper limit of normal and effluent amylase greater than 100 U/L suggest the diagnosis of acute pancreatitis. Serum lipase, isoamylase, and pancreatic secretory trypsin inhibitor are not helpful. In confirming the diagnosis, a computed tomography (CT) scan is more helpful than ultrasound, although it is positive in only 50-60% of cases. One should harbor a high index of suspicion concerning acute pancreatitis if a CAPD patient presenting with suspected peritonitis has either a negative effluent culture or does not respond to antibiotic therapy.
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PMID:CAPD and pancreatitis: no connection. 138 Aug 40

We examined the protective effect of human pancreatic secretory trypsin inhibitor (PSTI), a specific trypsin inhibitor secreted from pancreatic acinar cells into the pancreatic duct, on cerulein-induced acute pancreatitis in conscious rats. The protective effect of human PSTI-RS, an analogue of PSTI with Arg-44 to Ser substitution which has a longer half-life in vitro, was also examined. Intraperitoneal administration of a pharmacological dose of cerulein to conscious rats induced acute pancreatitis, characterized by light microscopy as cellular disorganization of the acini and interstitial edema. Intravenous infusion of human PSTI (10, 50 or 250 micrograms/rat/h) into rats with cerulein-induced acute pancreatitis decreased their pancreatic wet weight and plasma amylase concentration. It also caused a dose-dependent decrease in vacuoles in acinar cells and interstitial edema. Human PSTI-RS, which has a longer half-life in vivo, was more effective than native PSTI at the same dose rate (10 micrograms/rat/h) in reducing pancreatitis. These results suggest that human PSTI may have a beneficial effect on acute pancreatitis.
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PMID:Protective effect of human pancreatic secretory trypsin inhibitor on cerulein-induced acute pancreatitis in rats. 145 47

Serum pancreatic enzymes (amylase, trypsin, pancreatic elastase 1, pancreatic phospholipase A2) and serum pancreatic secretory trypsin inhibitor (PSTI) were measured in 22 patients with moderate or severe acute pancreatitis. Serum levels of all pancreatic enzymes were elevated at the initial determination, but they fell rapidly to normal in both moderate and severe pancreatitis. In contrast, PSTI in severe pancreatitis increased after admission and reached the maximum on the second to the forth day after onset. There was a significant positive correlation between the level of PSTI and that of acute phase reactant (fibrinogen, alpha 1-antitrypsin), and serum PSTI in severe acute pancreatitis changed as if it was one of acute phase reactants. There was also a significant negative correlation between the level of serum PSTI and that of alpha 2-macroglobulin.
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PMID:[Changes in serum pancreatic enzymes and pancreatic secretory trypsin inhibitor in patients with severe acute pancreatitis]. 241 44

The concentration of the pancreatic secretory trypsin inhibitor (PSTI) was measured in serum from 360 patients with acute abdominal diseases. Elevated levels were found in acute pancreatitis, cholangitis, choledocholithiasis, acute cholecystitis, pancreatic pseudocyst, malignancy, renal failure and in several different inflammatory conditions not connected with the pancreas. The results suggest the possibility of an extra-pancreatic production of PSTI, especially since the changes seen over time do not favour leakage or reabsorption as the cause of the high PSTI levels seen in acute pancreatitis. PSTI rather behaves as an acute phase reactant, as judged from the parallelism in the reaction pattern with antichymotrypsin.
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PMID:Serum levels of immunoreactive PSTI in acute abdominal disorders, with special reference to a possible extrapancreatic PSTI production. 243 67

Cleavage of C3 and kininogen in human plasma following the addition of increasing amounts of human cationic trypsin was studied using an in vitro model. The cleavage was correlated to the degree of saturation of the plasma protease inhibitors alpha 2-macroglobulin and alpha 1-proteinase inhibitor, and also with varying amounts of human pancreatic secretory trypsin inhibitor. When alpha 2-macroglobulin reached about 70% saturation, there was a prompt cleavage of most of the C3 and kininogen in spite of the presence of 90% free alpha 1-proteinase inhibitor. The consumption of alpha 1-proteinase inhibitor decreased with increasing concentrations of the pancreatic secretory trypsin inhibitor. This inhibitor was needed in a concentration of about 10 mumol to block trypsin-induced C3 and kininogen cleavage completely. As trypsin is thought to be the key trigger enzyme of the pathophysiological changes in acute pancreatitis, it seems reasonable to propose that the pancreatic secretory trypsin inhibitor might be of therapeutic interest in severe acute pancreatitis provided large enough amounts can be made available.
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PMID:Influence of the human pancreatic secretory trypsin inhibitor on trypsin-induced C3 and kininogen cleavage: an in vitro study. 243 81

The clinical usefulness of serum pancreatic secretory trypsin inhibitor (PSTI) in pancreatic disease and gastric and colorectal cancer has been examined. The results showed that serum PSTI in acute pancreatitis was significantly higher than in normal subjects and it was also raised in acute exacerbations of chronic pancreatitis. Although the sensitivities of serum PSTI, amylase and elastase I were similar, serum PSTI in necrotizing hemorrhagic pancreatitis was 2.7 times higher than in mild acute pancreatitis. Only a few patients with chronic pancreatitis showed increased concentrations and the mean value was near normal. The mean PSTI in patients with pancreatic and colorectal cancer was higher than normal, although that of gastric cancer was within normal limits. The sensitivity of serum PSTI measurements in patients with these three malignant diseases was only about 30%. The results suggested that the measurement of serum PSTI could be useful in the diagnosis of acute pancreatitis, but of limited value in the diagnosis of other disease which we examined.
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PMID:The measurement of serum immunoreactive pancreatic secretory trypsin inhibitor in gastrointestinal cancer and pancreatic disease. 245 73

Extrapancreatic findings at computed tomography (CT), performed within 24 h in 42 consecutive episodes of acute pancreatitis, were classified according to a scoring system (EP score) and were correlated to Ranson's prognostic signs, to duration of hospital stay, biochemical changes in plasma and pancreatic ischaemia found at CT with contrast enhancement. Increasing EP score was found to be related to increasing number of positive Ranson's signs, longer hospital stay and pancreatic ischaemia. Plasma levels of immunoreactive cationic trypsin and amylase were not proportional to EP score. alpha 1-protease inhibitor, antichymotrypsin but not immunoreactive pancreatic secretory trypsin inhibitor increased proportionally to EP score. No changes related to EP score were seen in alpha 2-macroglobulin levels. Serum levels of trypsin-alpha 1-protease inhibitor complex were maximal after 3 days and most pronounced in cases with high EP scores. Plasma levels of factor X, alpha 2-antiplasmin and C1-esterase inhibitor were found to be inversely proportional to EP score.
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PMID:Pathobiochemistry and early CT findings in acute pancreatitis. 248 91

Carboxyl ester lipase was purified from human pancreatic juice. Antisera were raised in rabbits and the monospecificity of the antibody was verified by immunoblotting. The enzyme was present in zymogen granules of acinar cells, in occasional duct cells, and in secretory material in normal pancreas in immunohistochemistry. Also, occasional cells in the epithelium of small intestinal villi but not the granules of Paneth cells, were stained. Decreased and evenly dispersed staining was observed in necrotic acinar cells in acute pancreatitis, whereas the reaction was intensive in plugs in acinar lumina. Interstitial staining was seen around necrotic pancreatic lobules and in areas of fat necrosis. This staining pattern is similar to that obtained with antisera against other lipolytic pancreatic proteins, but differed from that with antisera against trypsin and pancreatic secretory trypsin inhibitor. We conclude that carboxyl ester lipase behaves similarly to the other lipolytic enzymes during acute pancreatitis and that interstitial localization of secretory lipolytic enzymes is characteristic of the necrotizing inflammatory process in pancreas.
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PMID:Carboxyl ester lipase in human tissues and in acute pancreatitis. 268 25

The objective of this investigation was to test the capacity of recombinant human pancreatic secretory trypsin inhibitor (rhPSTI) to provide prophylaxis against experimental pancreatitis. Acute hemorrhagic pancreatitis was induced by intraductal injection of sodium taurocholate in rats and by intraductal injection of bile in dogs. In one treatment group of rats the injection of taurocholate was preceded by injection of rhPSTI. In a second group of rats the rhPSTI was given intraperitoneally starting 15 min after the induction of acute pancreatitis. The survival rate in a control group of rats was 13%. In contrast, the survival rate in groups receiving rhPSTI intraductally or intraperitoneally was 80% and 63%, respectively. The survival rate in a control group of dogs was 40% at 24 h and 0% at 48 h. In contrast, all the dogs receiving a single intraductal dose of rhPSTI, either immediately before the bile injection or mixed with the bile, survived for up to 6 weeks. Detailed biochemical and immunohistologic studies in the dog indicate that, whereas rhPSTI cannot prevent the initial bile-induced injury, it does prevent the subsequent development of that injury to the point where there is massive damage to the pancreas and the surrounding tissues, and changes in blood chemistry. The development of the initial injury is, therefore, presumed to involve activation of trypsinogen. Since rhPSTI prevents the serious consequences of experimental pancreatic injury by blocking the action of trypsin, and since the pathobiochemistry of human acute pancreatitis also implies an important role for trypsin, it is possible that rhPSTI could protect humans from the pancreatitis that complicates endoscopic retrograde cholangiopancreatography and endoscopic papillotomy.
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PMID:Local administration of human pancreatic secretory trypsin inhibitor prevents the development of experimental acute pancreatitis in rats and dogs. 281 37


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