Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UMLS:C0030305 (pancreatitis)
 16,014 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Peritoneal permeability to fluorescein-isothiocyanate-conjugated (FITC) dextran, mol wt 10,000 was studied in acute experimental pancreatitis (AEP) in rats. The aim of the study was to elucidate the role of the pancreatitis ascites and its phospholipase A2 activity on the observed peritoneal permeability increase during AEP. Phospholipase A2 activity of ascites was 40 U/microL 1 h after the induction of AEP and decreased during the next 3 h gradually to a plateau of about 20 U/microL, where it remained to the end of the experiment at 24 h. A similar pattern was seen for protein, amylase, and lipase although the initial peak was most pronounced for lipase. Pancreatitis ascites did not--irrespective of its age (1 or 20 h) or incubation time (3-20 h)--affect the peritoneal transport of FITC dextran 10,000 in healthy rats. Similarly, intravenously-administered ascites and intraperitoneal instillation of pancreatic phospholipase A2 dissolved in saline were without effects. On the other hand, in another group of healthy animals, phospholipase dissolved in fresh pancreatitis ascites caused a statistically significant increase of peritoneal transport, as defined. In rats with pancreatitis, the addition of phospholipase A2 to the peritoneal fluid increased peritoneal transport of FITC dextran 10,000 as well as phospholipase A2 itself. We conclude that phospholipase A2 when instilled into the peritoneal cavity in the presence of pancreatitis ascites, has the ability to increase peritoneal permeability to FITC dextran 10,000 in healthy, as well as in pancreatitis rats. However, the phospholipase A2 activity of rat pancreatitis ascites is not sufficient for this mechanism to work. This, however, does not exclude its existence in other species, including humans.
 ...
PMID:The role of ascites and phospholipase A2 on peritoneal permeability changes in acute experimental pancreatitis. 170 33

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.
 ...
PMID:Behavior of plasma phospholipase A2 activity in experimental acute pancreatitis according to diet. 245 24

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.
 ...
PMID:C-reactive protein (CRP) and serum phospholipase A2 in the assessment of the severity of acute pancreatitis. 362 21

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.
 ...
PMID:Differentiation of human phospholipase A2 isoenzymes in serum and other body fluids with use of monoclonal antibodies. 831 67

Phospholipase A2 (PLA2, E.C. 3.1.1.4) was purified from rat pancreatic tissue by heat treatment of the homogenate and use of cation-exchange chromatography on a CM-Sepharose column. The enzyme was apparently homogenous on SDS polyacrylamide gel electrophoresis, and its mol wt was estimated to be 14,400. An antiserum raised against rat pancreatic PLA2 in a rabbit was used in a solid-phase enzyme immunoassay employing inorganic pyrophosphatase (E.C. 3.6.1.1) as the enzyme label. As measured by this assay, the concentration of pancreatic PLA2 in plasma was found to be above normal in rats with hemorrhagic pancreatitis induced by an intraductal injection of sodium taurocholate. PLA2 was localized in pancreatic acinar cells and in the chief cells in the mucosa of the glandular stomach by immunohistochemistry. By immunoelectron microscopy, the immunogold conjugates were mainly located on profiles of zymogen granules in acinar cells.
 ...
PMID:Rat pancreatic phospholipase A2. Purification, localization, and development of an enzyme immunoassay. 850 52

Phospholipase A2 has been suggested to be involved in the pathogenesis and pathophysiology of acute pancreatitis. We determined phospholipase A2 and amylase activities in duodenal juice collected during a secretin test from 30 consecutive patients who were suspected to have chronic pancreatitis or biliary disease. The patients underwent endoscopic retrograde cholangiopancreatography (ERCP) the following day. In the 8 patients with ERCP findings of advanced chronic pancreatitis, the mean outputs of phospholipase A2, amylase, and bicarbonate were reduced by 74%, 72%, and 60% compared to the respective values in the 13 (control) patients without a diagnosis of any pancreatic disorder or jaundice. In the 3 patients with recurrent pancreatitis but normal ERCP findings and in the 6 patients with jaundice the output values were not significantly reduced compared to those in the patients without any pancreatic disorder or jaundice. The outputs of amylase and phospholipase A2 were not significantly interrelated, whereas the outputs of phospholipase A2 and bicarbonate correlated well. Receiver characteristic (ROC) curves confirmed the high specificity and sensitivity of phospholipase A2 or bicarbonate output in patients with ERCP findings of advanced chronic pancreatitis compared to those with no changes in pancreatic ducts, with similar probability values of 0.880 +/- 0.111 (SEM), compared to the respective lower value of amylase, 0.676 +/- 0.118. Phospholipase A2 and bicarbonate output proved of equal value as markers of chronic pancreatitis and were superior to amylase output in the secretin test.
 ...
PMID:Duodenal secretion of phospholipase A2, amylase, and bicarbonate in chronic pancreatitis. 960 59

Phospholipase A2 (PLA2) is an enzyme that catalyzes the hydrolysis of membrane phospholipids. This article reviews the source and structure of PLA2, the involvement of the enzyme in various biological and pathological phenomena, and the usefulness of PLA2 assays in laboratory diagnostics. Of particular importance is the role of PLA2 in the cellular production of mediators of inflammatory response to various stimuli. Assays for PLA2 activity and mass concentration are discussed, and the results of enzyme determinations in plasma from patients with different pathological conditions are presented. The determination of activity and mass concentration in plasma is particularly useful in the diagnosis and prognosis of pancreatitis, multiple organ failure, septic shock, and rheumatoid arthritis. A very important result is the demonstration that PLA2 is an acute phase protein, like CRP. Indeed, there is a close correlation between PLA2 mass concentration and CRP levels in several pathological conditions. Although the determination of C-reactive protein is much easier to perform and is routinely carried out in most clinical laboratories, the assessment of PLA2 activity or mass concentration has to be considered as a reliable approach to obtain a deeper understanding of some pathological conditions and may offer additional information concerning the prognosis of several disorders.
 ...
PMID:Phospholipase A2: its usefulness in laboratory diagnostics. 1043 55