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)

The activity of phospholipase A2 (PA2) was measured in the plasma of rats after the induction of acute pancreatitis. Buffered sodium taurocholate (3.75% w/v), injected into the pancreatico-biliary duct, was used to induce acute pancreatitis. Blood was taken at 1-h intervals for the measurement of phospholipase A2, glucose, lipase, and arterial gases. Plasma lipase was markedly elevated in the test groups, indicating acute pancreatitis, but no significant difference in PA2 activity was seen between the controls and the test group. However, in four animals the PA2 activity was elevated and in all cases this was accompanied by a low arterial pO2. This supports the theoretical role of PA2 in the pathogenesis of the respiratory complications observed in severe acute pancreatitis.
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PMID:Phospholipase A2 activity in taurocholate-induced acute pancreatitis in the rat model. 249 73

1. Evidence suggests that activation of phospholipase A2 and production of eicosanoids and platelet-activating factor (PAF) are involved in various responses associated with severe tissue damage and shock. It was postulated that the plasma level of the precursor and degradation product of PAF, lyso-platelet-activating factor (lyso-PAF), might be increased in acute severe illness. 2. After plasma extraction, lyso-PAF was acetylated in vitro to PAF, which was measured by bioassay using 5-[14C]hydroxytryptamine-labelled rabbit platelets. Measurements were made in 18 severely ill patients (five with cardiogenic shock; five with severe infection, five after repair of abdominal aortic aneurysm, two with acute pancreatitis; 13 males, five females). Plasma lyso-PAF in these patients was 33 +/- 15 (SD)ng/ml (range 5-111 ng/ml), whereas values in normal males (40-65 years) ranged from 102 to 253 ng/ml (n = 15) and in females from 74 to 174 ng/ml (n = 10). Depression of plasma lyso-PAF did not relate closely to the patient group nor to specific therapy, but repeated measurements in each of 10 patients showed an increase in plasma lyso-PAF (P less than 0.002), associated with clinical improvement. 3. Evidence was obtained indicating that neither the presence of an inhibitor in the assay system nor reconversion of PAF to lyso-PAF in vitro produced the unexpected depression of plasma lyso-PAF. 4. The mechanisms responsible, which may have therapeutic implications, remain to be elucidated.
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PMID:Plasma levels of the lyso-derivative of platelet-activating factor in acute severe systemic illness. 258 28

Several studies suggest that the activation of pancreatic phospholipase A2 (PLA2) and its release from injured acinar cells play an important role in the pathogenesis of acute pancreatitis. Elevated catalytic activity of PLA2 in serum is associated especially with severe forms of the disease. PLA2 has been purified from human cadaver pancreas and an antiserum raised against the enzyme in rabbits. Immuno-histochemical localization of PLA2 in pancreatic tissue was abnormal in acute pancreatitis. A time-resolved fluoroimmunoassay for human pancreatic PLA2 has been developed. Increased serum concentrations of immunoreactive PLA2 were found in acute pancreatitis during the first week after hospital admission. The values returned to normal somewhat more slowly than corresponding serum amylase values. The immunochemical determination of PLA2 in serum provides a fast and specific detection of injury to pancreatic acinar cells. The pancreas is not the only source of PLA2 in acute pancreatitis. The nonpancreatic PLA2 may originate from various inflammatory cells, but this hypothesis remains to be proven.
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PMID:The role of phospholipase A2 in human acute pancreatitis. 264 59

Several studies suggest that phospholipase A2 (PLA2) plays an important role in the pathology of acute pancreatitis. PLA2 is activated within the pancreas in experimental and human acute pancreatitis. Elevated catalytic activity of PLA2 in serum is associated especially with the severe forms of the disease. The pancreas seems not to be the only source of the enzyme entering the circulation in acute pancreatitis. The source of the non-pancreatic PLA2 may be various inflammatory cells, but this hypothesis remains to be proven. The results of the treatment of experimental acute pancreatitis with PLA2 inhibitors have been promising, but adequate human trials have not been conducted.
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PMID:The role of phospholipase A2 in acute pancreatitis. 268 47

In a prospective clinical trial, 85 patients with acute pancreatitis, including 50 with acute interstitial-edematous pancreatitis and 35 with necrotizing pancreatitis, were recruited. Serum pancreatic immunoreactive phospholipase A2 (IR-PLA2), serum phospholipase A catalytic activity (CA-PLA), and serum phospholipase A2 catalytic activity (CA-PLA2) were determined daily between day 1 and day 10 after the onset of the disease. The serum course of IR-PLA2 values for patients with acute interstitial-edematous pancreatitis was comparable to that for patients with necrotizing pancreatitis. In contrast, the determination of CA-PLA and of CA-PLA2 specific activity in the serum revealed a high differentiation between patients with interstitial edematous and those with necrotizing pancreatitis. The overall accuracy for differentiating patients with necrotizing pancreatitis from those with the interstitial-edematous type was 79% for CA-PLA and 77% for CA-PLA2 (cut-off level: CA-PLA, 15 U/L, day 1-5; CA-PLA2, 3.5 U/L, day 1-5). Patients with pancreatitis-associated pulmonary complications showed significantly higher CA-PLA and CA-PLA2 values in the serum. This study demonstrates the role of serum catalytic phospholipase A2 in human acute pancreatitis where the development of pancreatic necrosis and pulmonary failure is concerned.
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PMID:Role of phospholipase A2 in human acute pancreatitis. 268 22

Serum and ascitic phospholipase A2 (PLA2) activity was assayed in rat model of acute pancreatitis. Serum PLA2 activity was increased at the onset of acute pancreatitis, but had no correlation with severity of disease. The increase of PLA2 in ascites was, on the other hand, correlated well with severity of disease. Pancreatic PLA2 activity was also increased in the course of acute pancreatitis, which reflects increase in particulate fraction and showed obviously different pattern from amylase activity. Increase of PLA2 activity on particulate fraction was due to activation of membrane bound PLA2. These data suggest that activated membrane bound PLA2 exacerbates pancreatitis. The possibility of participation of endotoxin was also to be considered.
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PMID:[Study of phospholipase A2 in serum, ascitic exudate and pancreatic tissue in acute pancreatitis in rats]. 273 96

Daily measurements of serum phospholipase A2 activity were carried out on 73 consecutive patients admitted to hospital with acute pancreatitis. During the first 6 days there were significant differences in activity in those patients predicted as severe by multiple prognostic criteria when compared with those with mild disease. Follow-up studies at 6 weeks showed no difference between those graded as mild and those graded as severe at the time of attack. In the patients with elevated activity, nine had this at the time of admission and all were raised within 24 h. Elevated activity correlated well with the clinical outcome and showed good agreement with the multiple prognostic criteria in the prediction of severe disease. It is suggested that measurement of serum phospholipase A2 activity may provide a simple test for the early identification of most patients with severe acute pancreatitis.
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PMID:Serum phospholipase A2 activity in acute pancreatitis: an early guide to severity. 276 13

We tested the new radioimmunoassay method of serum phospholipase A2 (PLA2). In healthy individuals, serum PLA2 concentrations were 301 +/- 65.6 ng/dl (mean +/- SD), and in patients with acute pancreatitis, significant elevations of serum PLA2 concentrations were observed. In clinical course of acute pancreatitis, serum PLA2 was maintained high level more longer than serum amylase and elastase 1. In patients with chronic pancreatitis, serum PLA2 concentration were low at a stage of severe exocrine dysfunction, and high at a stage of acute exacerbation. In patients with pancreatic cancer, serum PLA2 concentration were changed in accord with severity of disease states. After endoscopic retrograde pancreatography, serum PLA2 levels immediately elevated significantly, and returned to basal levels 24 hours later. Serum PLA2 concentrations were within normal range in patients with other malignant tumors, diabetes mellitus, chronic liver diseases, and hypertension, whereas in patients with chronic renal failure serum PLA2 concentrations were elevated. These results suggest that measurement of serum PLA2 can be clinically useful for diagnosis of pancreatitis and monitoring of mild and severe stage of pancreatitis.
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PMID:[Clinical studies of serum phospholipase A2 immunoreactivity]. 279 50

We have developed an immunoassay for human pancreatic secretory phospholipase A2 based on time-resolved fluorescence. The labeled antibody technique in combination with the time-resolved fluorometric detection of the Europium label, which essentially eliminates all background fluorescence, resulted in a high sensitivity and a wide linear range. Our assay is a one-incubation, multi-site, solid-phase assay on polystyrene microtiter strips, even though a polyclonal antibody was used. Increased levels of immunoreactive phospholipase A2 are found by this assay in sera of patients suffering from acute pancreatitis.
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PMID:Time-resolved fluoroimmunoassay of pancreatic phospholipase A2. 292 48

A position-specifically labelled phosphatidylcholine is the substrate for the selective determination of Phospholipase A2 in serum, ascites and tissue samples. Optimal reaction conditions and simplifications of handling are discussed. A control group of human serum samples ranged up to 2.1 U/l. The maximum serum activity in samples of patients with acute pancreatitis was 126 U/l. In human ascites activities up to 380 U/l were measured. The method described here turned out to be a practicable instrument for the determination of phospholipase A2 activity using only commercially available reagents.
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PMID:A radiochemical test for phospholipase A2 catalytic activity. 292 50


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