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

Nineteen patients with acute pancreatitis were examined for the activity of LDH, NADH-tetrazolium oxidoreductase, acid phosphatase, the content of calcium salts, cAMP and cGMP in biopsy tissue of the pancreas; pancreatic enzymes and bicarbonates in the duodenal contents and pancreatic juice. The activity of enzymes participating in oxidative metabolism in epithelial cells of the intact pancreas appeared elevated. During the development of destructive changes in the pancreatic parenchyma, the processes of intracellular oxidation get inhibited, the enzymes go out into the intercellular space, calcium transport gets impaired, and acid phosphatase is activated. It has been found that in acute destructive pancreatitis, primarily impaired are epithelial cells of the islets, followed by the impairment of the epithelium of the acini and at the last moment of that of the excretory ducts. The data obtained enable one to regard cyclonucleotides, calcium, pancreatic enzymes and lysosomal hydrolases as pathogenetic elements of acute pancreatitis.
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PMID:[Morphofunctional elements of the pathogenesis of acute pancreatitis]. 164 89

In 110 patients with acute pancreatitis the authors studied the activity of intracellular enzymes in the blood (LDH, CPC, ALaT, ASaT, transamidinase) in a complex with indices characterizing the condition of the membrane cell systems, in particular: activity of acid phosphatase, content of 17-ketosteroids, activity of plasma chemiluminescence, concentration of beta-lipoproteins in blood. Complex study of these indices makes it possible to make a sufficiently objective judgement of the severity of the membrane disorders in acute pancreatitis and verity the form and control the treatment of the disease.
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PMID:[Diagnosis of membrane disorders in acute pancreatitis]. 232 43

The pulmonary complications are severe sequeles of acute pancreatitis. The pathogenesis of these complications is unsolved. The purpose of this work was to evaluate the status of lung lysosomes and phospholipase A activity in acute experimental pancreatitis (AEP) and the effect of heparin as a potentially protective agent. Taurocholate-induced AEP in rats lasting 24 and 48 hours was treated with heparin intraperitoneally (2 mg/kg every 8 hours). The total activity of cathepsins and B-glucuronidase in lysosomal enriched subfraction increased markedly during 48 hours of AEP in untreated animals, but the relative free activity was maximal after 24 hours. Free activity of cathepsins and acid phosphatase in supernatant was maximal after 24 hours. The phospholipase A activity was maximally elevated (more than twofold) after 48 hours. Heparin prevented the increase of activity of B-glucuronidase, depressed the relative free activity of all investigated lysosomal hydrolases and inhibited the phospholipase A activity in the lung homogenate. Our results indicate the significance of labilization of lung lysosomes and increment of phospholipase A activity in the lungs in the damage of this organ during AEP in the rats, and suggest the beneficial effect of heparin on these factors.
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PMID:The lung lysosomal hydrolases and phospholipase A in acute experimental pancreatitis with reference to heparin treatment. 243

In acute pancreatitis, damage to the liver is an important aspect of multiorgan failure. In 28 dogs (20 with bile-trypsin induced acute experimental pancreatitis (AEP], 'total' and 'free' activity of lysosomal hydrolases: beta-glucuronidase, cathepsins and acid phosphatase in mitochondrial and lysosomal subfraction of the liver were determined 12 h or 24 h after the induction of AEP. The respiratory control ratio with sodium succinate as a substrate, using Clarck's electrode and uncoupler-dependent ATP-ase activity in mitochondrial subfraction, was assayed. Groups of dogs were treated or pretreated with prostacyclin (PGI2), 20 ng.kg-1.min-1 i.v. for 12 or 13 h. The relative free activity of hydrolases was significantly elevated in untreated AEP after 12 h and was partially normalized in AEP after 24 h or after 12 h followed by treatment and pretreatment with PGI2. Respiratory control ratio was twice lower than normal in AEP after 12 h and partially normalized after 24 h post PGI2 treatment. The relative free activity of lysosomal hydrolases was highly negatively correlated with respiratory control ratio. It was concluded, that during AEP in dogs the function of liver mitochondria and lysosomal stability are impaired. The significant correlation found between the mitochondrial and lysosomal lesions points to lysosomal-mitochondrial interactions in liver damage in AEP. Prostacyclin in the investigated dose partially prevents the mitochondrial and lysosomal lesions in liver in this disease.
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PMID:Lysosomal-mitochondrial interrelationships in damage to the liver in acute experimental pancreatitis in dogs. Treatment with prostacyclin (PGI2). 304 48

The activities of a number of lysosomal hydrolases were determined in sera from 100 patients with cystic fibrosis (CF), age 2-35 yr, and age-matched controls: beta-hexosaminidase activity was significantly elevated (p less than 0.005) in CF patients from all age groups. alpha-Mannosidase activity was increased only in the older CF patients (greater than 13 yr). The following enzyme activities were not altered in CF serum: alpha-fucosidase, beta-glucuronidase and acid phosphatase. The abnormal patterns of serum alpha-mannosidase and beta-hexosaminidase in CF cannot be explained by pancreatic disease or undernutrition, since serum values of these hydrolases in patients with anorexia nervosa or acute pancreatitis were not altered. However, the altered activities of the alpha-mannosidase and beta-hexosaminidase were proportional to the degree of pulmonary insufficiency in the CF group, indicating that these changes are probably a secondary consequence of the primary disease process. Except for beta-hexosaminidase, because differences in the serum hydrolases in CF do not become apparent until the second decade of life, determinations of lysosomal enzyme activities in serum will probably be of little diagnostic value.
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PMID:Serum lysosomal hydrolases in cystic fibrosis. 316 78

The liver affection in acute experimental pancreatitis (AEP) could be reflected by changes of enzymatic activity in the liver and in serum. The histoenzymatic studies of the liver of dogs with AEP of different severity and time of duration induced according to Elliott's method were performed and the constellation of serum enzymatic activities considering treatment with prostacyclin was estimated. The histoenzymatic reactions on succinic dehydrogenase, lactic dehydrogenase and alkaline phosphatase were depressed with progression of time and severity of AEP. In contrast, the reaction on acid phosphatase was augmented at the same time. Serum AspAT, AlAT and alkaline phosphatase were augmented in the later phase of AEP, but acid phosphatase and beta-glucuronidase were not significantly changed. The treatment with PGI2 limited both histoenzymatic reactions and alterations of serum enzymatic activities. These results support the significance of changes in enzymatic activities in the course of liver reaction on pancreatogenic noxa during acute pancreatitis, and suggest the protective effect of PGI2 against liver injury in this disease.
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PMID:The enzymatic studies of the liver in acute experimental pancreatitis in dogs treated with prostacyclin (PGI2). 329 21

The levels of pancreatic digestive enzymes, lysosomal hydrolases, and protease inhibitors were evaluated in ascites fluid from 24 patients with acute pancreatitis diagnosed as alcoholic, gallstone-induced, or idiopathic. In this group the concentrations of amylase (354 +/- 98 ng/ml), immunoreactive cationic trypsinogen (1840 +/- 238 ng/ml), and immunoreactive elastase 2 (1492 +/- 262 ng/ml) were greatly elevated in comparison to the corresponding serum values. Enzyme levels in ascites from the idiopathic pancreatitis group tended to be higher than the levels from the other two groups. Activity of acid phosphatase and beta-glucuronidase was significantly higher in ascites compared to serum in all groups. On the other hand, levels of immunoreactive alpha 1-protease inhibitor and alpha 2-macroglobulin in ascites fluid were about half the average concentrations reported for normal serum. Significant amounts of tryptic amidase activity (61.7 +/- 13.7 micrograms/ml) were observed, indicating a trypsin-alpha 2-macroglobulin complex. These data indicate an imbalance in the protease-to-inhibitor ratio in ascites fluid from patients with acute pancreatitis. Coupled with elevated ribonuclease activity (27.4 +/- 3.4 units), a positive methemalbumin test in 23 of 24 patients (1.1 +/- 0.4 mg hematin/100 ml), and an average protein concentration of 4.0 +/- 0.2 g/100 ml, these observations demonstrate that abdominal paracentesis and the biochemical analyses of ascites fluid provide useful information related to the biochemical events in acute pancreatitis and may be useful in the diagnosis of difficult cases, but their predictive value of severity remains to be established.
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PMID:Biochemical studies in peritoneal fluid from patients with acute pancreatitis. Relationship to etiology. 381 84

The effects of hormonal or cholinergic stimulation on survival and on activities of lysosomal enzymes and amylase in pancreatic tissue and ascites were studied in rats with induced pancreatitis. Pancreatitis per se caused an increase of the activities of cathepsin D, N-acetyl-beta-D-glucosaminidase and amylase, and a decrease of acid phosphatase in pancreatic tissue. Pancreatic protein concentration was not influenced. In pancreatitic rats administration of cerulein or carbachol markedly decreased survival rate. Cerulein increased the activities of cathepsin D and amylase in ascites and cathepsin D and acid phosphatase in pancreatic tissue. Carbachol increased the activities of cathepsin D and amylase in ascites and acid phosphatase in pancreatic tissue. Both cerulein and carbachol decreased the activity of amylase in pancreatic tissue. Administration of secretin or the anticholinergic drug Pro-Banthine did not influence survival rate or the activities of lysosomal enzymes and amylase in ascites. In pancreatic tissue the activity of acid phosphatase was slightly increased by secretin or Pro-Banthine. In conclusion, the results show a nonparallel alteration of lysosomal enzyme activities in pancreatic tissue in rats with pancreatitis. Cerulein and cholinergic stimulation decreased survival rate and brought about a marked increase of cathepsin D activity in ascites and, in the case of cerulein, also in pancreatic tissue. The implication of lysosomes and especially the catheptic proteases in the pathogenesis and outcome of acute pancreatitis deserves further attention.
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PMID:Hormonal and cholinergic effects on amylase and lysosomal enzyme activities in pancreatic tissue and ascites of rats with acute experimental pancreatitis. 619 36

Majority of literature data support the significance of proteases activation in pathogenesis of acute pancreatitis. The ability of cathepsins to the activation of trypsinogen was shown and the labilization of lysosomes of pancreas in different models of acute experimental pancreatitis (AEP) was reported. In present work the dynamic of lysosomal changes during the course of AEP in dogs is evaluated. AEP was induced in 17 mongrel dogs by Elliot's method. Six healthy dogs served as a control group (I). Pancreatitic dogs were killed after 6 hr (G. II, n = 5), after 12 hrs (G. III, n = 5), and after 24 hrs (G. IV, n = 6 survivors). The pancreata were removed and divided into segments A (less advanced changes, [B] most advanced changes) and C (intermediate changes). The lysosomal enriched subfraction was isolated from the C segments at 15 000 X g for 20 min. The total (T) and free (F) activity of beta-glucuronidase (beta-G), acid phosphatase (AP), acid cathepsins (Cs) was estimated and the value F/T (relative free activity-r.f.a.) was calculated as an index of lysosomal stability. The progressive increase of r.f.a. of hydrolases in whole homogenate and in lysosomal enriched subfraction depending on time of AEP was observed suggesting labilization of pancreatic lysosomes. This labilization was more expressed in corresponding parts of organ with more advanced pathological changes. The differences between part A and B were most evident after 6 hrs of AEP. The labilization of lysosomes is more pronounced after 12 and 24 hrs than after 6 hrs in analogical parts of organ. These results indicate that labilization of lysosomes in pancreas correspond to the degree of pathological changes of pancreatic tissue.
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PMID:Pancreatic lysosomal hydrolases in acute experimental pancreatitis in dogs. 651 6

Rats infused with a supramaximally stimulating dose of the cholecystokinin-pancreozymin analogue caerulein develop acute interstitial pancreatitis (M. Lampel and H.F. Kern. Virchows Arch. A 373: 97-117, 1977). We have studied the early (30-180 min) morphological changes in pancreatic acinar cells induced by infusing caerulein (2.5 micrograms X kg-1 X h-1). The techniques of thin-section electron microscopy, freeze fracture, and enzyme and immunocytochemistry were employed. Shortly (30 min) after the onset of caerulein infusion, large vacuoles appeared in the Golgi area. After longer periods of infusion, these vacuoles further enlarged (probably by fusion with other such vacuoles as well as autophagic vacuoles) and became more widely distributed in the cytoplasm. These large vacuoles were found to be acid phosphatase positive and to be labeled by antibodies directed against digestive zymogens as well as the lysosomal enzyme cathepsin D. These observations indicate that the large vacuoles contain both digestive zymogens and lysosomal hydrolases. During caerulein infusion, morphological evidence of exocytosis at the luminal plasmalemma was reduced or absent, and evidence of basolateral exocytosis was not noted. These studies suggest that secretagogue hyperstimulation with caerulein interferes with the processes involved in condensing vacuole maturation, which normally lead to the separation of digestive zymogens and lysosomal hydrolases. As a result, both types of enzymes remain within the same compartment. This may lead to the intracellular activation of digestive enzymes by lysosomal hydrolases and be an important step in the development of acute pancreatitis.
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PMID:Supramaximal caerulein stimulation and ultrastructure of rat pancreatic acinar cell: early morphological changes during development of experimental pancreatitis. 672 Aug 95


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