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 most important fatal complications of acute pancreatitis are respiratory dysfunction and anuria. Phospholipase A2 has been postulated to be associated with pathologies of various diseases, such as acute pancreatitis, septic shock and multiple injuries. We have recently developed immunoassays for the measurement of pancreatic and nonpancreatic synovial-type phospholipase A2. The present prospective study on 35 consecutive patients with acute pancreatitis indicated that the concentration of synovial-type phospholipase A2, the catalytic activity of phospholipase A2 and the concentration of C-reactive protein in serum were significantly higher in those patients suffering from acute pancreatitis who needed respirator treatment than in those who managed with spontaneous breathing, while there was no difference between these groups in the concentration of pancreatic phospholipase A2. The only significant difference between patients whose highest creatinine concentration rose up to 140 mumol/l and those whose highest creatinine concentration remained below this cutoff value was in their synovial-type phospholipase A2 values. The increased concentration of nonpancreatic synovial-type phospholipase A2 in serum was associated with pulmonary and renal complications. These results emphasize the role of synovial-type phospholipase A2 in the pathophysiology of acute pancreatitis.
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PMID:Increased concentrations of synovial-type phospholipase A2 in serum and pulmonary and renal complications in acute pancreatitis. 145 57

The effect of fat-rich diet (F) and chronic ethanol ingestion in experimental acute pancreatitis (AP) on plasma enzyme activities and the composition of ascitic fluid were studied in rats. 96 male Wistar rats were randomized into four groups. Two groups, one of which drank 15% (v/v) ethanol as their drinking solution, received the F-diet for 12 weeks. The rest of the rats served as controls receiving standard laboratory food (S). Half of the control animals drank ethanol and the other rats had tap water. AP was induced by retrograde bile infusion into the pancreatic ducts and relaparotomy performed after 24 hours follow-up period. All animals surviving were exsanguinated and the ascitic fluid collected. Phospholipase A2 (PLA2) correlated with the mortality rate in the S-diet receiving groups but no changes could be seen after the F-diet. Ethanol in combination with the F-diet caused a significant increase in total protein content of ascitic fluids (p less than 0.001). Trypsin inhibiting capacity was significantly decreased in the same groups (p less than 0.01) and total proteolytic activity was highest in the ascitic fluids of the F-diet and ethanol receiving rats. No significant differences in the PLA2 activities in the ascitic fluids between the groups were observed. It is suggested, that the composition of ascitic fluid generated during experimental AP is of importance to the outcome of the disease.
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PMID:The effect of fat-rich diet and chronic ethanol ingestion on ascitic fluid and plasma enzyme activities in acute pancreatitis in rats. 244 Feb 13

The effects of standard, fat-rich, protein-rich, and carbohydrate-rich diets combined with either long-term ethanol ingestion or tap water ingestion on the behavior of plasma phospholipase A2 activity during experimental acute pancreatitis were studied in rats. Phospholipase A2 activity was compared with amylase activity in the plasma. Three hundred eighty-four male Wistar rats were randomized into eight groups receiving different diets with either 15 percent (volume for volume) ethanol or tap water for 12 weeks. Thereafter, all groups were subdivided into control (intact) and pancreatitis subgroups. Pancreatitis was induced by retrograde bile infusion into the pancreatic ducts. Sampling was performed 24 hours after induction in the surviving rats. Ethanol ingestion alone and in combination with the fat-rich diet increased the mortality rate (p less than 0.05), whereas the lowest mortality rate was observed in the carbohydrate-rich diet and water and the carbohydrate-rich diet and ethanol groups. Plasma phospholipase A2 activity increased in most of the groups, but it correlated with the mortality rate in the standard diet group only. Plasma amylase activity increased significantly in all groups, but did not correlate with mortality rate. Plasma phospholipase A2 activity seems to be dependent on diet in experimental acute pancreatitis in rats. Plasma amylase activity may be less affected by the dietary composition, but the lack of a correlation with mortality makes it unreliable as a parameter of severity in experimental acute pancreatitis.
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PMID:Behavior of plasma phospholipase A2 activity in experimental acute pancreatitis according to diet. 245 24

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

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

Phospholipase A2 was localized with peroxidase anti-peroxidase (PAP)-technique in pancreatic tissue resected from normal portions of tumor-bearing glands of 4 patients and from pancreases of 16 patients suffering from either acute or chronic pancreatitis. In acute pancreatitis the enzyme immunoreactivity was detected in the apical zymogen granule portion of acinar cells and in ductal secretory material similarly as in normal tissue. At the border of necrotic and non-necrotic exocrine parenchyma the staining reaction was evenly dispersed throughout the cytoplasm or localized in small cell fragments. There was no reaction in necrotic acinar cell remnants. Some dilated acinar lumina contained intensively stained plugs. Fat necroses were stained but surrounding neutrophil leukocytes were unstained. Thrombosed small vessels were also unstained. In chronic pancreatitis, diminished staining characterized small acinar cells at the border of lobules. Some macrophages stained positively. It was concluded that during acute inflammation in pancreas, localization of phospholipase A2 in pancreatic tissue is abnormal, and that phospholipases A2 of neutrophil leukocytes and platelets are not crossreactive with the secretory enzyme.
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PMID:Immunohistochemical localization of phospholipase A2 in human pancreas in acute and chronic pancreatitis. 634 33

Systemic prostacyclin and thromboxane A2 production in rat experimental acute pancreatitis has been evaluated by measuring the urinary excretion of the 2,3-dinor 6-keto prostaglandin F1 alpha and 2,3-dinor thromboxane B2, respectively. Acute pancreatitis was induced by intraductal administration of 4.5% sodium taurocholate (0.1 ml/100 mg body weight) and intravenous cerulein perfusion (5 micrograms/kg/hr) for 6 hr, respectively. Urinary excretion of 2,3-dinor 6-keto prostaglandin F1 alpha and 2,3-dinor thromboxane B2 were much more important in sodium taurocholate- than in cerulein-induced acute pancreatitis. These data confirm an altered prostacyclin and thromboxane metabolism occurring in experimental acute pancreatitis. Phospholipase A2 activity and the effect of gabexate mesilate on the arachidonate metabolism were also evaluated.
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PMID:Changes of systemic prostacyclin and thromboxane A2 in sodium taurocholate- and cerulein-induced acute pancreatitis in rats. 767 83

Phospholipase A2 (PLA2) is the rate limiting enzyme in the formation of prostaglandins and probably plays a key part in the pathology of various inflammatory diseases. In acute pancreatitis, the catalytic activity of PLA2 in serum correlates with the severity of the disease. The cellular source of the catalytically active PLA2 in serum of patients suffering from acute pancreatitis and other diseases is unknown. Immunoassays for the measurement of pancreatic group I PLA2 and nonpancreatic synovial type group II PLA2 have recently been developed and the present study investigated the presence of group I and group II PLA2s in serum samples from 36 patients with severe acute pancreatitis. The catalytic activity of PLA2 showed a highly significant correlation with the concentration of synovial type PLA2 (r = 0.939, p = 0.001) but not with the concentration of pancreatic PLA2 (r = 0.067, p = 0.698). The results suggest that pancreatic PLA2 circulates mostly as inactive enzyme in patients with acute pancreatitis whereas synovial type PLA2 is responsible for the increased catalytic activity of the enzyme and thus might be associated with the pathophysiology of the disease.
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PMID:Pancreatic and synovial type phospholipases A2 in serum samples from patients with severe acute pancreatitis. 817 68

Phospholipase A2 (EC 3.1.1.4; PLA2) is detected in serum by determination of either the catalytic activity of the enzyme or the concentration of the enzyme protein by immunoassays. The most sensitive methods for determining PLA2 catalytic activity are radiometric assays, with a substrate of synthetic phospholipid (e.g., phosphatidylcholine or phosphatidylethanolamine) containing a 14C- or 3H-labeled fatty acid at the sn-2-position. Membranes of autoclaved Escherichia coli grown in the presence of radioactive oleic acid may also be used as a substrate. The released fatty acids are separated from the unreacted substrate and quantified by liquid scintillation counting. PLA2 catalytic activities are increased in serum in sepsis, acute pancreatitis, peritonitis, multiple injuries, rheumatoid arthritis, and other arthropathies. Immunoassays--radioimmunoassay, enzyme-linked immunosorbent assay, or time-resolved fluoroimmunoassay--are based on the use of either polyclonal or monoclonal antibodies to purified PLA2s. Specific assays have been developed for both pancreatic group I PLA2 (PLA2-I) and nonpancreatic group II PLA2 (PLA2-II). The cellular source of PLA2-I in serum is the pancreatic acinar cell. Increased serum PLA2-I values have been reported in acute pancreatitis, pancreatic cancer, and abdominal trauma. Increased PLA2-II values are found in conditions involving inflammation, e.g., sepsis, infections, acute pancreatitis, various forms of arthritis, cancer, complications of pregnancy, and postoperative states. Good correlations have been found in serum samples between the catalytic activity of PLA2 and the concentration of PLA2-II but not PLA2-I. PLA2-II may represent an acute-phase protein. The cellular source of the PLA2-II in serum is unknown; it is present in large amounts in cartilage and Paneth cells, prostatic gland cells, seminal fluid, lacrimal gland cells, and tears, but cannot be demonstrated by immunohistochemical or immunochemical methods in inflammatory cells.
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PMID:Serum phospholipases A2 in inflammatory diseases. 825 15

Elevated phospholipase A2 activities in serum were measured in patients suffering from acute pancreatitis or various inflammatory diseases. The photometric phospholipase A assay of Hoffmann & Neumann (Klin. Wochenschr. 67 (1989) 106-109) was combined with immunoabsorption by different monoclonal antibodies directed against pancreatic phospholipase A2. Pancreatic phospholipase A2 was purified from human duodenal juice. Monoclonal antibodies were prepared by fusion of spleen cells from immunized mice with P3X63-Ag8-653 myeloma cells. Samples with phospholipase A2 activity were incubated in monoclonal antibody-coated microtitre plates. Phospholipase A2 activities were determined in the monoclonal antibody-treated samples as well as in control samples. The method allows the determination of the fraction of human phospholipase A2 isoenzymes in various biological materials. For pancreatic phospholipase A2 the specific binding capacity was about 60-80%, the unspecific binding was 5-30%. Practically no cross-reactivity was seen with partially purified serum phospholipase A2, with recombinant platelet phospholipase A2, or with the sera of patients with non-pancreatic diseases. In conclusion, the present study confirmed the presence of pancreatic phospholipase A2 in human duodenal juice and in the ascites of necrotizing pancreatitis. However, pancreatic isoenzyme was absent in non-pancreatic inflammatory diseases. Therefore, elevated phospholipase activities in non-pancreatic inflammatory diseases cannot be attributed to the pancreas.
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PMID:Differentiation of human phospholipase A2 isoenzymes in serum and other body fluids with use of monoclonal antibodies. 831 67


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