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Query: UMLS:C0001339 (acute pancreatitis)
 10,593 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We have developed a model of experimental haemorrhagic pancreatitis in pigs with a 100% mortality within 24 h without treatment. In this model we have studied the production of peritioneal exudate and compared the concentrations of amylase, lipase and phospholipase A2 in the ascitic exudate and serum. The results suggest that the determination of phospholipase A2 might be important in the diagnosis and follow-up of acute pancreatitis.
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PMID:Phospholipase A2 in serum and ascitic exudate in experimental acute haemorrhagic pancreatitis in pigs. 51 Mar 26

The amylase-creatinine clearance ratio was first proposed as a useful tool in the diagnosis of acute pancreatitis, and later it was claimed that trypsin creatinine clearance ratio was a sensitive and accurate test of pancreatic cancer. More recent observations have undermined the role of both clearances in the diagnosis of acute pancreatitis, and their utility in patients with chronic pancreatic diseases has largely been ignored. Three orders of factors, (a) the physicochemical characteristics of the protein, (b) the glomerular filtration rate variations, and (c) renal tubular damage, may have a role in determining the changes in the plasma-urine transfer of enzymes such as amylase and trypsin. Amylase urinary output is related both to variations in amylase serum levels (since this enzyme probably is not intensively reabsorbed by the tubule) and to the presence of renal tubular damage. Trypsin plasma-urine transfer changes depend greatly on the presence of tubular alterations. Elastase 1 and phospholipase A2 urinary outputs can also be predicted on the basis of the presence of tubular damage. Renal tubular alteration in pancreatic diseases may depend on the damaging effect of toxic substances (proteolytic enzymes, for example) released by the inflamed pancreas; the role of liver damage and of extrahepatic jaundice, which are frequent findings in chronic pancreatic diseases, should also be considered. However, toxic compounds such as ethanol, which can alter the pancreas and possibly the kidney, could also have a key role in the genesis of urinary findings in pancreatic diseases.
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PMID:Urinary enzymes excretion in pancreatic diseases. Clinical role and pathophysiological considerations. 137 38

Prostacyclin metabolism in rat acute pancreatitis was evaluated by measuring the tissue levels of 6-keto-prostaglandin F1 alpha (6-keto-PGF1 alpha) and the urinary excretion of 2, 3-dinor 6-keto-PGF1 alpha. Acute pancreatitis was induced by i.v. cerulein perfusion and was confirmed by the pancreas enzyme changes and the histological findings. Significantly enhanced tissue and urinary prostacyclin levels were found in acute pancreatitis rats, when compared to the controls. Concomitantly, an enhanced tissue phospholipase A2 (PLA2) activity was also found. These data show the importance of 2, 3-dinor PGF1 alpha as an inflammatory marker in cerulein-induced pancreatitis.
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PMID:Altered systemic and tissue prostacyclin in cerulein induced acute pancreatitis in rats. 138 68

Early diagnosis of threatening renal complication is essential for the adequate treatment of acute pancreatitis. Deposition of phospholipase A2 (PLA2) in rat renal proximal tubular cells has been observed in experimentally induced acute pancreatitis. The value of measuring the catalytic activity of PLA2 in serum as an early warning of developing renal tubular cell injury was therefore investigated in a prospective study of 31 consecutive patients suffering from acute pancreatitis. A positive correlation was found (r = 0.66, P < 0.001) between the highest serum PLA2 activity, as measured early in the course of acute pancreatitis, and the highest N-acetyl-beta-glucosaminidase (NAG):creatinine ratio in the urine. The correlation between the highest serum concentration of immunoreactive pancreatic PLA2 and the highest urinary NAG:creatinine ratio was weaker (r = 0.36, P < 0.05). These results indicate that the measurement of the catalytic activity of PLA2 in serum early in acute pancreatitis may provide a simple test for the detection of threatening renal complication.
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PMID:Renal tubular cell injury and serum phospholipase A2 activity in acute pancreatitis. 139 77

Extracellular phospholipases A2 play an important role in articular and extra-articular inflammatory processes. Secretory non-pancreatic phospholipase A2 (PLA2) has been implicated in the pathogenesis of articular inflammation in rheumatoid arthritis, whereas pancreatic PLA2 contributes to the tissue damage associated with acute pancreatitis. Since in experimental models lipophilic tetracyclines such as minocycline and doxycycline are antiinflammatory, we examined their effects on PLA2 activity using two assay systems in vitro. We found that minocycline and to a lesser degree doxycycline were markedly inhibitory to both pancreatic and non-pancreatic PLA2. Using [14C]oleic acid labeled Escherichia coli membrane phospholipids as substrate, the IC50 values for minocycline and doxycycline were 3.6 x 10(-5) M (18 micrograms/mL) and 0.98 x 10(-4) M (47 micrograms/mL), respectively. In a scooting mode assay using the synthetic phospholipid 1-palmitoyl-2-(10-pyrenedecanoyl)-3-L-phosphatidylmethanol as substrate, IC50 values for minocycline were 5 microM (2.47 micrograms/mL) for non-pancreatic PLA2 and 8 microM (3.95 micrograms/mL) for pancreatic PLA2. Addition of excess calcium up to 50 mM did not reverse the inhibitory activity of tetracyclines. We conclude that lipophilic tetracyclines inhibit PLA2, probably by interaction with the substrate, and may be a useful adjunct in the therapy of inflammatory conditions in which PLA2 is implicated pathogenetically.
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PMID:Inhibition of enzymatic activity of phospholipases A2 by minocycline and doxycycline. 141 38

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

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

Pancreatic phospholipase A2 and non-pancreatic ascitic phospholipases A2 were studied in sera of healthy individuals and of patients suffering from sepsis or acute pancreatitis. In gel filtration experiments, immunoreactive ascitic phospholipase A2, as determined in serum by a time-resolved fluoroimmunoassay, eluted either unassociated with an apparent M(r) of 10,000-14,000 or associated with proteins of high molecular mass. Catalytically active ascitic phospholipase A2 was associated with high molecular weight proteins. In acute pancreatitis the catalytically active and immunoreactive pancreatic phospholipase A2 eluted mainly as a protein of M(r) of 14,000. The results of the gel filtration experiments indicate that pancreatic phospholipase A2 is not associated with other proteins in human serum, whereas ascitic phospholipase A2 is associated with protein(s) of relative high molecular weight, or exists in different polymeric forms. We also purified phospholipase A2 from sera of healthy individuals by ion exchange chromatography and HPLC. The enzyme was homogenous, displayed an M(r) of approximately 13,500 as judged by SDS-polyacrylamide gel electrophoresis, and reacted with an antibody raised against ascitic phospholipase A2.
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PMID:Characterization of two phospholipases A2 in serum of patients with sepsis and acute pancreatitis. 162 22

Malonic dialdehyde as an indirect marker of the lipid peroxidation was found increased in the acute pancreatitis compared with persons of the same age and sex. Its concentrations inversely correlated to those of the serum calcium during the course of the disease and additionally they proved to be indicator of the prognosis. Postulating that the acute pancreatitis must be a "free radical disease", in a randomized clinical study the adjuvant therapy of the acute necrotizing pancreatitis (n = 8) with sodium selenite was carried out in a daily dose of 500 micrograms. The lethality of the control group was 89% (8 out of altogether 9 patients), no patient died in the therapy group. By the selenium therapy within 24 hours a normalization of the serum calcium and a decrease of the increased MDA-values could be achieved. It was concluded that by selenium increased activities of the phospholipid-hydroperoxide-glutathione peroxidase were induced, by means of which a peroxidation protection of membrane fatty acids, an inhibition of the activity of phospholipase A2 and an interruption of the arachidonic acid cascade must have been reached.
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PMID:[Acute pancreatitis--a free radical disease. Decrease in fatality with sodium selenite (Na2SeO3) therapy]. 131 23

The diagnostic significance of serum immunoreactive pancreatic phospholipase A2 (PLA2) was studied in 119 patients with pancreatic disease, 200 with various non-pancreatic disease, and 203 healthy controls using radioimmunoassay (RIA) specific to human pancreatic PLA2. This newly developed RIA using monoclonal antibody was satisfactorily sensitive and reliable. Serum PLA2 was elevated in all six patients with acute pancreatitis. Frequency of abnormal serum PLA2 levels was 60% in chronic pancreatitis (n = 52) and 67% in pancreatic cancer (n = 61). Serum PLA2 levels were low in chronic pancreatitis with severe exocrine insufficiency and advanced pancreatic cancer. In chronic pancreatitis, patients with low serum PLA2 level showed lower enzyme output in secretin test than patients with normal or high serum PLA2 level. Frequency of abnormal PLA2 levels was 27% in non-pancreatic disease and, in particular, patients with renal failure showed high PLA2 levels. Sensitivity (62%) and efficiency (69%) of serum PLA2 assay in pancreatic disease were superior to those of amylase. In conclusion, serum PLA2 determination using RIA was useful for the diagnosis of acute pancreatitis by high serum PLA2 levels and the diagnosis of severe exocrine pancreatic insufficiency by low serum PLA2 levels.
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PMID:The diagnostic value of serum pancreatic phospholipase A2 (PLA2) in pancreatic diseases. 170 72


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