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)

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

It is suggested that the important drugs rifampicin and halothane and the raised glucose levels in diabetes mellitus exert injurous effects on cells through a lysosomal mechanism. Further evidence is given of by time rifampicin induction of beta-glucuronidase and beta-N acetylglucosaminidase and its possible relation to hepatitis and pancreatitis. On the basis of preliminary data halothane may cause hepatitis connected to lysosomal enzyme release in the presence of other aggravating factors common to the perioperative period. The onset of diabetic vascular complications may be related to the similar raised levels of lysosomal enzymes found in insulin, drug and diet controlled disease. Release of these enzymes into plasma may be a marker of important changes in the lysosome, whether due to enzyme induction or damage, and could be a primary mechanism of many disease processes including some thought to be mainly autoimmune in character. Routine estimation in the clinical laboratory along with existing cytoplasmic and microsomally derived enzymes in the chemical screen would be a useful way of surveying lysosomal changes in the wide spectrum of disease in a general hospital.
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PMID:Rifampicin, halothane and glucose as mediators of lysosomal enzyme release and tissue damage. 341 3

We measured the activity of a non-lysosomal alpha-glucosidase with pH optimum near 6.0 in serum from a wide variety of patients, using the fluorogenic substrate, 4-methylumbelliferyl-alpha-D-glucopyranoside. Acutely ill patients with cystic fibrosis (CF) demonstrated significant increases in alpha-glucosidase compared with CF outpatients. The former group of CF patients experienced far more severe chronic pulmonary disease than did the latter, whereas both groups had similar degrees of gastrointestinal impairment. Patients with pancreatitis associated with trauma or complicated by severe necrosis, hemorrhage, or abscess also displayed greater increases in alpha-glucosidase than did patients with uncomplicated (edematous) pancreatitis. For CF outpatients and patients with either edematous pancreatitis or pancreatic cancer, the alpha-glucosidase activity was similar to that for the general hospital-patient population. Corresponding changes were not observed for other measured serum glycosidases (alpha-fucosidase, alpha-mannosidase, beta-glucuronidase, beta-N-acetylglucosaminidase). Measurement of serum alpha-glucosidase may be of value in assessing the clinical course in CF and in differentiating necrotizing from edematous pancreatitis.
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PMID:Measurement of alpha-glucosidase activity in serum from patients with cystic fibrosis or pancreatitis. 351 92

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 inflammatory process in pancreas affects the function and structure of kidneys both by enzymatic toxemia and impairment of the renal circulation. In this study the stability of renal lysosomes in AEP in dogs treated with cytoprotective agent PGI2 was investigated. AEP was induced by injection of the bile and trypsin into the pancreatic duct; experiments were terminated after 12 hours. In lysosomal enriched subfraction of the kidney cortex (sedimenting in 15 000 x g) in untreated group (N = 5) relative free activity (r.f.a.) of cathepsins (Cs), acid phosphatase (APh) and beta-glucuronidase (BG) increased to 51,67 and 62% respectively, whereas in healthy dogs (N = 6) these activities were 20,38 and 25%. In dogs (N = 6) treated with PGI2 at the dose of 20 ng/kg/min. during 12 hrs, the r.f.a. of Cs, APh and BG was 18,40 and 49%, whereas in dogs (N = 5) additionally pretreated during 1 hr before induction of AEP with the same dose of PGI2, its values achieved 19,40 and 47% respectively. Our results suggest the stabilizing effect of PGI2 on kidney lysosomes damaged in acute experimental pancreatitis in dog. As possible mechanisms of prostacyclin action are discussed: limitation of necrotic process in the pancreas; improvement of renal haemodynamics; direct cytoprotective effect on the kidney.
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PMID:The renal lysosomes in acute experimental pancreatitis in dogs treated with prostacyclin (PGI2). 637 45

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

In 15 mongrel dogs acute experimental pancreatitis (AEP) was induced by injection of bile and trypsin into the pancreatic duct. After 12 hrs in lysosomal enriched subfraction of the liver in untreated group (N = 5) relative free activity of cathepsins (Cs), acid phosphatase (AP) and beta-glucuronidase (beta G) increased to 50,62, and 53% respectively in comparison to the healthy dogs (N = 6) : 19,43 and 20%. In dogs with AEP treated with prostacyclin (PGI2) in the dose of 20 ng/kg X min for 12 hrs these activities of Cs, AP and beta G were lowered to 30,55 and 41% in comparison with the untreated group. In dogs with AEP (N = 5) additionally pretreated during 1 hr before the induction of AEP with the same rate of PGI2 i.v. infusion, the relative free activity of enzymes was similar to the treated group. After two hrs incubation of lysosomal enriched subfraction in acidic medium (pH = 5,0), the highest values of relative free activity were observed in untreated group, the difference being more pronounced in comparison with control group than before incubation. In those animals treated and pretreated with PGI2, postincubation activities were much lower than in untreated dogs. These results suggest the stabilising effect of PGI2 on hepatic lysosomes, damaged during the course of AEP in dogs.
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PMID:Prostacyclin (PGI2) stabilises hepatic lysosomes during acute experimental pancreatitis in dogs. 675 74

Nine lysosomal enzymes and alkaline phosphatase have been assayed in human pancreatic juice from controls and patients with chronic calcifying pancreatitis. Specific activities were evaluated by a nonparametric test (Wilcoxon) with a probability of 2 P less than or equal to 0.5. The values of acid phosphatase, alpha-glucosidase, beta-glucosidase and alpha-galactosidase are significantly higher in pathological juices; the values of alpha-mannosidase and beta-glucuronidase are also increased in the same patients but at the limit of significance. Alkaline phosphatase, beta-hexosaminidase and alpha-fucosidase follows the same trend but the values are not statistically significant between the two groups of patients. Studies on skin cultures of four patients with chronic calcifying pancreatitis demonstrate that the increased specific activities of lysosomal enzymes in the pathological juices do not correspond to a leakage of these enzymes into the extracellular space as described for cystic fibrosis.
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PMID:Alkaline phosphatase and acid lysosomal hydrolases in pancreatic juice and fibroblast cell cultures of patients with chronic calcifying pancreatitis. 680 85

The role of lysosomal hydrolases in the pathogenesis of acute pancreatitis and secondary liver injury, as an important aspect of multisystem organ failure, remains unclear. The purpose of this study was to assess the lysosomal fragility in both organs in acute experimental pancreatitis (AEP) of graded severity in dogs. In 7 dogs, the moderate (M) and in 13 dogs severe (S) variant of bile--trypsin AEP--was induced; 6 dogs were in control group (C). The 24 h survival time was 6/7 and 6/13, respectively. After that time, the dogs were sacrificed and the lysosomal enriched subfraction (L) from both organs was isolated by ultracentrifugation. The total (T) and free (F) activities of beta-glucuronidase (beta G), cathepsins (Cs) and acid phosphatase (AcP) according to Gianetto and de Duve were assayed. The fractional free activity (% F/T) was adapted as and index of lysosomal stability. The %F/T of BG in the homogenate of the pancreas in AEP(S) was higher than that in AEP(M) (92% vs. 71%, p < 0.05, and vs. 37% in C, p < 0.005). The %F/T of Cs and AcP showed a similar pattern. The %F/T of beta G in L of the liver in AEP(S) was 38% vs. 29% in AEP(M), (p < 0.05), and vs. 20% in C (p < 0.05). In AEP in dogs the %F/T activities of lysosomal hydrolases in the pancreas and liver were increased, suggesting the labilization of lysosomal membranes in severe form of this disease. Our results support the pathogenic role of lysosomal hydrolases in the damage to the pancreas and liver in acute pancreatitis.
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PMID:The role of lysosomal alterations in the damage to the pancreas and liver in acute experimental pancreatitis in dogs. 752 Sep 59

The decompartmentation of lysosomal compartment in pancreatic acinar cells with consecutive activation of zymogens might play an important role as a "trigger mechanism" in acute pancreatitis. The admixture of lysosomal hydrolases to secretory enzymes in pancreatic juice was found, but their role in pancreatic secretion remains obscure. The aim of the present study was to assess the fragility of pancreatic lysosomal structure after maximal (optimal) or supramaximal stimulation of rats with cerulein during 3, 6, 12 h, and after recovery. In the mitochondrial-lysosomal (M-L) and in the supernatant (S) of pancreases free (F) total (T), and fractional free (%F/T) activities of beta-glucuronidase (beta G), acid phosphatase (AcP), cathepsins (Cs), and beta-N-acetyl-hexosaminidase (NAH) were estimated. In edematous pancreatitis following supramaximal stimulation with cerulein, a significant increase of %F/T of beta G in whole homogenate began at 6 h of hyperstimulation in comparison to the control (93 vs 42% p < 0.01). This increment persisted until 12 h of hyperstimulation and declined after 24 and 48 h of recovery to 67-69%. The changes of %F/T of beta G in M-L followed those in whole homogenate, and additionally the increase free activity in S after 6 h of hyperstimulation and after 24 h recovery occurred. The respective activities of other hydrolases showed a similar pattern of changes. It is of interest that fragility of lysosomal membranes increases significantly also after maximal stimulation when inflammatory changes were absent. Our results suggest that the increase of lysosomal fragility of the pancreas is most unlikely pathological in itself, but also occurs during stimulated pancreatic secretion.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:The lysosomal hydrolases in the rat pancreas after maximal or supramaximal stimulation with cerulein. 780 14


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