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)

Serum from 48 patients with acute pancreatitis (21 with interstitial-edematous and 27 with necrotizing pancreatitis) was monitored for immunoreactive (IR) phospholipase A2 (PLA2) protein concentration and PLA catalytic activity. In both groups within 48 h after start of acute pancreatitis an up to tenfold increase of IR-PLA2 was demonstrable. Determination of IR-PLA2 revealed no differences between the groups. In contrast, determination of PLA catalytic activity allowed us to differentiate between patients with interstitial-edematous and necrotizing pancreatitis.
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PMID:Prognostic value of serum phospholipase A in acute pancreatitis. 292 55

Acute haemorrhagic pancreatitis was produced in the dogs by transduodenal injection of autologous bile into the main pancreatic duct. There was no significant change in the activity of three regulatory enzymes of phosphatidylcholine biosynthesis (glycerophosphate acyltransferase, cytidyltransferase and cholinephosphotransferase) in lung; however, there was a 42% decrease in the amount of dipalmitoyl phosphatidylcholine (surfactant) in lung lavage due to acute pancreatitis. The decrease in lavage phospholipid content was associated with 5-fold increase in phospholipase A2 activity of lung lavage, and massive accumulation of osmiophilic spheroid structures in the alveolar space.
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PMID:Effects of experimental acute pancreatitis in dogs on metabolism of lung surfactant phosphatidylcholine. 303 36

We investigated the effect of a new synthetic protease- and phospholipase A2-inhibitor gabexate mesilate (FOY) in a multicenter (6 hospitals in Hannover and vicinity) double-blind study on the clinical course of acute pancreatitis. 50 patients were randomized into two subgroups. One group was treated with 3 X 300 mgs of gabexate mesilate per day for 9 days as a continuous intravenous infusion, the control group received placebo. There was no difference in these two groups regarding age and sex, but there was a discrepancy concerning the severity (stage I-IV) of the acute pancreatitis at the onset of treatment. More of the patients in the gabexate mesilate-group had severe disease on admission to hospital. Of the 7 patients (14%) who died, 5 were in the gabexate mesilate-group whereas only 2 were in the placebo group. This difference in the mortality rate is not significant. There was, however, a significant difference at the 5% level between the verum-group and the control group concerning the decline in alpha-amylase activity in serum and the number of complications. The difference was greatest in alcohol induced acute pancreatitis. A non-parametric test showed a significant reduction in hospitalisation time in the gabexate mesilate-group. Due to the small number of patients and the inhomogeneous clinical course of the acute pancreatitis a definite conclusion concerning the effect of gabexate mesilate on the clinical course of acute pancreatitis is not possible. Further studies with a much greater number of patients and more homogeneous groups with respect to the severity of the acute pancreatitis at the onset of the therapy with gabexate mesilate or placebo are necessary.
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PMID:[Gabexate mesilate in the treatment of acute pancreatitis. Results of a Hannover multicenter double-blind study with 50 patients]. 308 76

Therapeutic use of the perfluorochemical emulsion, Fluosol DA, in acute pancreatitis was experimentally discussed in view of maintaining the local blood flow and oxygen supply in the pancreas to avoid further aggravation of pancreatitis. Acute pancreatitis was induced by deoxycholate injection into the pancreatic duct in adult mongrel dogs. Fluosol DA or 6% hydroxyethylstarch (HES) solution as control was transfused at 20 ml/kg/hour for the first 3 hours. Fluosol DA and HES solution improved the depressed cardiac output and pancreatic blood flow to normal levels. Compared with HES solution, Fluosol DA administration revealed a prominent increase in oxygen tension in the pancreatic tissue, which had decreased severely from onset of pancreatitis. Fluosol DA administration brought about better preservation of pancreatic mitochondrial functions. Despite no significant differences in blood levels of other pancreatic enzymes between Fluosol DA and HES solution, the sharp decrease in plasma postheparin phospholipase A2 suggested the protection of involved systemic organs including pancreas. Thus, maintaining pancreatic blood flow and increasing the oxygen transport by Fluosol DA administration seemed to play a positive role in inhibiting the progress of pancreatitis, though improvement of survival rate in acute pancreatitis was incomplete by Fluosol DA administration alone.
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PMID:Experimental studies on fluosol DA administration in acute pancreatitis. 317 91

Serious pulmonary complications are often associated with acute pancreatitis. The destruction of pulmonary surfactant by the action of pancreatic phospholipase A2 (PLA2), together with pulmonary edema, is considered an important etiopathogenic factor of acute respiratory insufficiency. This experimental study was undertaken to elucidate the destruction of pulmonary surfactant in acute pancreatitis using the lung pressure volume curve (P-V curve). Acute hemorrhagic pancreatitis was induced in mongrel dogs by a retrograde injection of Na-taurocholate into the main pancreatic duct. Pulmonary surface tension was measured by P-V curve and the effect of PLA2 on pulmonary surfactant was assessed by the ratio of lysolecithin and lecithin, which are essential components of pulmonary surfactant (Ly/Le) in lung wash. Extravascular lung water volume (Ww/Dw) and blood gases were also measured. The value of Ly/Le and serum PLA2 rose significantly from the 3rd hour. On the contrary, no significant differences were seen on P-V curve until the 12th hour but after 20 hours surface tension increased significantly. Ww/Dw and A-aDO2 increased after 3 and 12 hours, respectively. These findings, the degradation of lecithin and the elevation of surface tension accompanied with an increase of serum PLA2, suggest that pulmonary surfactant is destroyed in severe acute pancreatitis, and that the increased capillary permeability of the lung precedes the deterioration of surface tension as the cause of pulmonary insufficiency.
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PMID:[Experimental study on the pathogenesis of pulmonary insufficiency in acute pancreatitis and changes in the pulmonary surfactant]. 322 26

Localization of phospholipase A2, lipase and colipase immunoreactivity were studied in paraffin embedded tissue sections. The samples were taken from the pancreas of 12 patients suffering from acute haemorrhagic necrotizing pancreatitis, and from diseased adipose tissue of 7 patients suffering from traumatic mammary fat necrosis. Peroxidase-antiperoxidase immunohistology revealed consistent positive reaction against phospholipase A2, lipase and colipase at the border of fat necrosis in pancreatic interlobular adipose tissue and in peripancreatic, mesenterial and retroperitoneal fat. The fat necroses of the breast were devoid of reaction. The results support the idea that in addition to lipase colipase and phospholipase A2 participate in the development of fat necrosis in acute pancreatitis. Pancreatic lipolytic enzymes are not present in the adipose tissue in mammary fat necrosis.
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PMID:Fat necrosis in human acute pancreatitis. An immunohistological study. 352 Nov 89

The present study examines the value of C-reactive protein (CRP) determinations in the assessment of the severity of acute pancreatitis and the correlation of CRP with serum phospholipase A2 activity and the clinical status. Fifty three patients with acute pancreatitis were studied; 17 with haemorrhagic pancreatitis and 36 with a mild form of the disease. S-phospholipase A2 activity increased significantly (p less than 0.05) in patients with fatal pancreatitis but not in those with mild disease. Phospholipase A2 concentrations were below 10 nmol FFA/ml min in mild, while they rose to 20-40 nmol FFA/ml min in haemorrhagic pancreatitis. In fatal cases very high (up to 50-60 nmol FFA/ml min) serum phospholipase A2 concentrations were recorded. The increase in CRP was greater in the patients with severe pancreatitis. One day after admission mean CRP was 280 mg/l in patients with haemorrhagic and 45 mg/l in those with the mild pancreatitis (p less than 0.001). High CRP values also correlated with the prognostic signs indicative of severe pancreatitis. CRP and S-phospholipase A2 determinations are valuable in the early assessment of the severity of acute pancreatitis, but the CRP assay is much easier to include in hospital routine.
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PMID:C-reactive protein (CRP) and serum phospholipase A2 in the assessment of the severity of acute pancreatitis. 362 21

An improved radiochemical method is presented for the selective determination of phospholipase A2 activity in human serum and ascites, using only commercially available reagents. The method can be applied to large quantities of samples. As substrate we used 1,2-dipalmitoyl-sn-glycero(3)phosphorylcholine and phosphatidylcholine containing tritiated palmitic acid in position 2 (1-palmitoyl,2-[9,10-3H]palmitoyl-sn-glycero(3)phosphorylcholine). The liberated fatty acids are extracted and radioactivity is detected in a liquid scintillation spectrometer. A preliminary reference range of human serum samples was established ranging up to 1.0 U/l. In sera of patients with acute pancreatitis we found activities up to 20 U/l. The correlation of phospholipase A2 activity with that of other enzymes and with the severity and complications of acute pancreatitis was investigated. A possible relationship between phospholipase A2 activities and pulmonary complications is discussed.
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PMID:Improved method for the determination of phospholipase A2 catalytic activity concentration in human serum and ascites. 369 38

The factors causing a decline in renal perfusion were studied in anaesthetized dogs with acute pancreatitis 4 h after the forceful injection of bile into the pancreatic duct. In 11 such dogs, glomerular filtration rate (GFR) decreased by 40.4% from the control state (P less than 0.05), whereas the clearance of para-aminohippurate (CPAH) declined by 50.2%. These changes were associated with a 15.3% decline in cardiac output (P less than 0.05) and a 26.2% fall in plasma volume. Glomerular morphology was entirely normal. When hypovolemia was prevented by infusing homologous plasma over the 4-h period of observation, the normally observed decline in GFR, CPAH, and cardiac output was prevented. The decline in plasma volume, associated with a rising hematocrit and declining plasma protein concentration, and the associated decrement in renal perfusion, could be entirely duplicated by the infusion of trypsin, chymotrypsin, elastase, and phospholipase A2 (but not lipase or amylase) into normal dogs. These perturbations also were prevented by the concurrent infusion of 4% albumin in saline. At 24 h, however, the renal failure became unresponsive to volume replenishment. We conclude that the decline in renal perfusion in dogs at 4 h with acute pancreatitis is entirely due to hypovolemia, induced by the release of specific enzymes from the inflamed gland, which causes the loss of protein-rich plasma from the vascular space.
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PMID:Renal failure in dogs with experimental acute pancreatitis: role of hypovolemia. 378 59

The problem of whether human pancreatic phospholipase A2 (PLA2) can really hydrolyze membrane phospholipids in vitro was studied to understand pathophysiology of acute pancreatitis. Total amount of lysophospholipids generated in erythrocytes by exogenously added human pancreatic PLA2 (2 micrograms/ml) was only 12% of the amount of sphingomyelin, which was not decomposed by the enzyme. About fivefold the amount of lysophospholipids was generated in ghost membranes during one-sixth of the incubation time compared to that in intact erythrocyte membranes. Escherichia coli lipopolysaccharide (LPS) (10 micrograms/ml) was able to stimulate membrane-associated PLA2 of erythrocytes, the amount of lysophospholipids generated being 12.5% of that of sphingomyelin without adding the exogenous PLA2. The stimulation of membrane-associated PLA2 in erythrocytes was inhibited by pretreatment of lipopolysaccharide with polymyxin-B sulfate. When intact erythrocytes were incubated with human pancreatic PLA2 and LPS, the amount of generated lysophospholipids was 24% of that of sphingomyelin. These results suggested that the exogenously added human pancreatic PLA2 cannot degrade phospholipids of intact erythrocytes so extensively under physiological conditions, and, in acute pancreatitis, unknown factors may be involved in the hydrolysis of phospholipids. LPS, which activates membrane-associated PLA2, may be one of the factors, and thus membrane phospholipids are hydrolyzed in the disease.
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PMID:Hydrolytic activities of human pancreatic phospholipase A2 and endotoxin-stimulated endogenous phospholipase A2 toward membrane phospholipids of erythrocytes. 388 99


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