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

Kinetics and distribution of i.v. human pancreatic phospholipase A2 (h-PLA2) were determined in intact and nephrectomized rats, and tissue localization of rat pancreatic PLA2 (r-PLA2) was studied by immunohistochemistry in experimental acute pancreatitis. The concentration of h-PLA2 and the catalytic activity of phospholipase A2 in plasma decreased exponentially in intact and nephrectomized animals after the injection. The initial 15-min half-life was considerably longer in nephrectomized animals, and higher h-PLA2 concentrations and PLA2 catalytic activities were found in plasma. h-PLA2 was localized in endocytotic vesicles and apical cytoplasmic vacuoles in proximal tubule cells of the kidney. The intensity of the immunoreaction decreased considerably between 15 and 50 min in these cells. No signs of tubular damage were seen by light microscopy. Neither immunoreactive h-PLA2 nor PLA2 catalytic activity was found in urine. r-PLA2 was observed in proximal tubule cells 15 min after an injection of sodium taurocholate (necrotizing pancreatitis group) or saline (edematous pancreatitis group) into the pancreatic duct. Signs of tubular damage were present in necrotizing pancreatitis, but tubular morphology was normal in the animals with edematous pancreatitis. We conclude that the proximal tubule cells of the kidney participate in the metabolism of circulating pancreatic PLA2, and considerably higher PLA2 levels persist in plasma in nephrectomized animals. Endogenous pancreatic PLA2 is detected in kidneys in acute pancreatitis.
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PMID:Pancreatic phospholipase A2 in proximal tubules of rat kidney in experimental acute pancreatitis and after intravenous injection of the enzyme. 159 53

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.
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PMID:The role of ascites and phospholipase A2 on peritoneal permeability changes in acute experimental pancreatitis. 170 33

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

To investigate the correlation between the initial levels of serum pancreatic enzymes and the severity of acute pancreatitis, serum amylase activity, immunoreactive trypsin content, phospholipase A2 activity and immunoreactive pancreatic phospholipase A2 content were comparatively measured in 22 patients with acute pancreatitis. Serum immunoreactive pancreatic phospholipase A2 content and phospholipase A2 activity in the severe group were significantly elevated as compared with those in the group of moderate pancreatitis on the first day of onset. The elevation of the initial immunoreactive phospholipase A2 content in the severe group was far greater than that of amylase activity, trypsin content and phospholipase A2 activity. The difference between immunoreactive phospholipase A2 content and phospholipase A2 activity was, in part, due to the presence of prophospholipase A2 in severe acute pancreatitis sera, but the phospholipase A2 content measured by radioimmunoassay was still about 5 times higher than that calculated from fully activated phospholipase A2 activity by trypsin.
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PMID:Usefulness of determination of serum immunoreactive pancreatic phospholipase A2 content for early identification of severe acute pancreatitis. 243

Forty-seven piglets were operated on; haemorrhagic pancreatitis was induced in 42 of them. The effects of pancreatic resection and peritoneal lavage on the development of the disease were compared. Since the pancreatic phospholipase A2 value has been shown to be important in the pathophysiology of the disease, the effect of pancreatic resection on the enzyme serum activities was studied. Early pancreatic resection and early peritoneal lavage were equally effective in reducing the mortality of the animals. When the pancreatic resection was performed later, most of the animals died. The difference in mortality between the groups was statistically significant (p less than 0.01). In the animals with late pancreatectomy the high serum phospholipase A2 activities fell to normal levels within a few hours after the operation. This strongly suggests that the enzyme is of pancreatic origin.
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PMID:The effect of early pancreatectomy and peritoneal lavage on the development of experimental haemorrhagic pancreatitis in pigs. 713 44

We investigated the concentration of immunoreactive pancreatic phospholipase A2 (pan-PLA2) and the catalytic activity of phospholipase A2 (CA-PLA2) in plasma, peritoneal fluid, and pancreas of rats in which acute hemorrhagic pancreatitis was induced by an intraductal injection of sodium taurocholate. The contribution of pancreas to the CA-PLA2 in plasma was studied by removing pancreatic PLA2 by absorbing plasma samples with a polyclonal antibody raised in a rabbit against rat pancreatic PLA2. Sodium taurocholate injected into the pancreatic duct produced hemorrhagic pancreatitis with necrosis and inflammatory cell invasion within 8 hr. Saline injection caused edematous pancreatitis, but sham operation did not alter pancreatic morphology from normal. The concentration of pan-PLA2 increased rapidly in plasma in all animals, but significantly more in sodium taurocholate-injected animals than in saline-injected or sham-operated animals. The level of CA-PLA2 in plasma increased in sodium taurocholate-injected animals only. There was no correlation between pan-PLA2 and CA-PLA2 values in plasma in sodium taurocholate-injected animals. The CA-PLA2 was marginally increased in pancreatic tissue of sodium taurocholate-injected animals compared to that of saline-injected and sham-operated animals at 8 hr. Treatment by the anti-pan-PLA2 antibody effectively removed pan-PLA2 from plasma and peritoneal fluid samples in sodium taurocholate-injected animals. The level of CA-PLA2 in plasma was similar before and after antibody treatment.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Phospholipase A2 in sodium taurocholate-induced experimental hemorrhagic pancreatitis in the rat. 763 43

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