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)

Experimental haemorrhagic pancreatitis was induced in 12 piglets by infusing Nataurocholate trypsin into the pancreatic duct with simultaneous intravenous secretin stimulation. Within some minutes after the infusion all animals developed severe pancreatitis accompanied by the production of bloody ascites. Unless given specific treatment the pigs died within 24 h. Of the animals treated with xylocaine infusion (50 microgram/kg/min for 24 h) one died within 24 h, one during the second day, and four lived for over a week, at which time they were killed. Although xylocaine treatment signficantly improved the survival of the animals, it did not seem to influence the local damage of the pancreatic tissue. Xylocaine has been shown to inhibit phospholipase-A in vitro. It is possible that xylocaine also acts in vivo by inhibiting phospholipase-A, thus preventing lethal tissue damages at an early stage of pancreatitis.
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PMID:Xylocaine treatment in experimental pancreatitis in pigs. 72 7

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

Phospholipases, a group of enzymes that catalyze the hydrolysis of membrane phospholipids, are classified according to the bond cleaved in a phospholipid into PLA1 (EC 3.1.1.3), PLA2 (EC 3.1.1.4), PLB (EC 3.1.1.5), PLC (EC 3.1.4.3), and PLD (EC 3.1.4.4). This paper reviews source and structure of PLA2 and the involvement of PLA2 and PLC in several biological phenomena, such as, signal transduction, photoreception, biosynthesis of lung surfactant, sperm motility, and fertilization. New assays for PLA2 activity and concentration in biological fluids are discussed. Phospholipases are involved in many inflammatory reactions by making arachidonate available for eicosanoid biosynthesis. The determination of PLA2 activity and mass concentration in plasma is useful in the diagnosis and prognosis of pancreatitis and of septic shock. Naturally occurring phospholipase inhibitors, such as lipocortins act as second messengers in the anti-inflammatory response to steroids. Lipocortins may be valuable therapeutic agents, because they are more specific in their anti-inflammatory action than glucocorticoids; therefore, they are less likely to produce harmful side effects.
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PMID:Phospholipases in biology and medicine. 225 31

The nonhydrolyzable guanyl nucleotide GTP gamma S stimulated phosphoinositidase C activity in two preparations obtained from mouse pancreatic acini labeled with myo[2-3H]inositol: a cell-free membrane fraction and intact electropermeabilized acini. This action was dose-dependent, was shared by other nonhydrolyzable guanyl nucleotides such as GMP-phencyclidine hydrochloride and GMP-PMP, as well as by fluoride, and was calcium-independent. Contrarily, no effect was observed even at doses of GTP gamma S as high as 10 microM when the same protocol was repeated on identical acinar preparations from mice fed a choline-deficient, ethionine-supplemented diet. This regimen is known to uncouple secretagogue-receptor occupancy from inositol 1,4,5-trisphosphate generation in pancreatic acinar cells and lead to necrotizing hemorrhagic pancreatitis. These data lead us to conclude that the ethionine-induced inactivation of guanyl nucleotide-dependent pancreatic phosphoinositidase C in pancreatic acinar cells is not the result of either a decrease in GTP level or a decrease in GTP availability. These findings further confirm previous work from this laboratory, which has shown that the biochemical lesion induced by this diet occurs after the agonist-receptor binding step. The diet-induced lesion could be either at the level of the G-protein that couples the enzyme with the receptor or at the level of the phospholipase itself.
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PMID:Effects of a choline-deficient ethionine-supplemented diet on phospholipase C activity in mouse pancreatic acinar cell membranes and in electropermeabilized mouse pancreatic acini. 233 59

The development of a photometric procedure to measure phospholipase A activity has extended previous observations that this enzyme activity increases in several pathological states including pancreatic and inflammatory diseases. Serum phospholipase A in pancreatitis was characterized as a mixture of the pancreatic enzyme and a different phospholipase with a pH optimum at 8.0. The latter enzyme was also observed in nonpancreatic diseases like septicemia and acute lung failure which are characterized by an increase in tissue phagocyte activity. The possible pathogenic role of phospholipase(s) A, their intracellular regulation and the proposed mechanisms of release into the blood stream are discussed with respect to the present pathobiochemical knowledge. This includes the mechanism of activation of phagocytosis and the possible role of lipocortins known to be stimulated by glucocorticoid treatment.
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PMID:Serum phospholipase--regulatory and pathophysiological aspects. 264 58

Lipocortins, a group of corticosteroid-induced phospholipase-inhibitory proteins, are thought to play a prominent role in the mediation of the anti-inflammatory effects of steroids. The synthesis and release of these proteins may represent a major endogenous mechanism of regulation of extracellular phospholipase A2 (PLA2) activity. Because soluble PLA2 activity has been associated with circulatory collapse in hyperphospholipasemic conditions, such as septic shock and pancreatitis, we examined the relationship between circulating PLA2 activity and adrenocortical function. In a prospective study of 10 episodes of septic shock, serum PLA2 and cortisol levels correlated significantly in all survivors (p less than 0.0001), whereas such a correlation was absent in all nonsurvivors (p less than 0.07). No significant correlation of cortisol and adrenocorticotropic hormone (ACTH), or PLA2 and ACTH, was found in any patient, suggesting that the stimulus for cortisol release arises from outside the hypothalamic-pituitary axis. These data suggest that, in human beings, the regulation of soluble PLA2 activity may be mediated by adrenocortical hormones, perhaps through the intermediary action of lipocortins.
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PMID:Concordance of endogenous cortisol and phospholipase A2 levels in gram-negative septic shock: a prospective study. 283 77

One hundred nineteen children, either French or from the Ivory Coast, aged 1-8 years, were submitted to pancreatic function testing by duodenal aspiration. Trypsin, chymotrypsin, lipase, phospholipase, amylase, volume, bicarbonate, chloride, and calcium were estimated before and after an intravenous injection of 1 CU secretin + 3 CHR units pancreozymin per kilogram of body weight. Sixty-two patients were normal European children, and 11 were normal African children. Twenty-five African children presented with kwashiorkor and 10 African children had presented with kwashiorkor but had recovered at the time of the test. Three cases of recurrent kwashiorkor are also included. In the normal group of African children, phospholipase concentration, volume, and bicarbonate were significantly decreased but chymotrypsin and trypsin concentrations were not, when compared to the normal European population. In kwashiorkor patients, lipase, amylase, phospholipase, and chymotrypsin concentration were significantly decreased compared to normal Africans. Trypsin, volume, and bicarbonate were not affected. These modifications disappeared after refeeding. In cases of recurrent kwashiorkor, all enzymes, including trypsin, were decreased. Calcium was never modified. These modifications were very different from those observed in chronic alcoholic and hypercalcemic pancreatitis. In a two-year study, chronic calcifying pancreatitis (CCP) was diagnosed in 14 patients (13 males), hospitalized in Abidjan. The mean age at onset of the disease was 41 years (SD 12.71), which is very similar to European cases. The most frequent cause was alcoholism, as in Occidental countries. The nutrition of the population was low in protein, calories being provided mostly by manioc, but no apparent symptoms of malnutrition were observed in the parents of our patients.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Exocrine pancreatic function of children from the Ivory Coast compared to French children. Effect of kwashiorkor. 300 10

In a randomized double-blind study the effect of CaNa2EDTA, a phospholipase A2 inhibitor, was tested as a treatment for acute pancreatitis. CaNa2EDTA was infused intravenously during the first 2 days after admission to hospital, in addition to normal conservative treatment. CaNa2EDTA decreased the serum phospholipase A2 activity and appeared to promote recovery from the illness. To what extent the inhibition of serum phospholipase activity may prevent the progress of severe haemorrhagic pancreatitis or diminish mortality and morbidity in acute pancreatitis should be investigated in further studies.
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PMID:A randomized double-blind study using CaNa2EDTA, a phospholipase A2 inhibitor, in the management of human acute pancreatitis. 392 48

Using a standardized model of bile-induced acute pancreatitis, the reaction of phospholipase-A1 activity was investigated in parallel to that of phospholipase-A2, as well as their relationship to the pathomorphological spread of pancreatitis. While the measurement of the total free fatty acids (FFA) in serum as metabolites of phospholipase-A activity indicated variable reactions with the average remaining the same (0.186 +/- 0.15 to 0.192 +/- 0.153 mEq/l), phospholipase-A2 exhibited a highly significant increase from 9.6 +/- 2.2 to 18.2 +/- 5.4 nmol/ml/min (P less than 0.01). It was demonstrated that in parallel phospholipase-A1 also showed a highly significant increase from 2.5 +/- 1.2 to 6.7 +/- 3.1 nmol/ml/min (P less than 0.01). In relation to the pathomorphological score, both phospholipases showed a small increase at a low score (edema to focal necrosis), whereas in groups with a larger spread of the pancreatitis, score 5 or 6 (extended necrosis to retroperitoneal necrosis), the increase was substantially clearer. As a result of these findings, we conclude that phospholipase-A1 could possibly be used as phospholipase-A2 as an indicator of the severity of acute pancreatitis and that it should be taken into consideration in the very promising therapy with phospholipase-A-antagonists.
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PMID:Phospholipase-A1 and -A2 in experimental acute pancreatitis in rats. 399 56

Serum immunoreactive trypsin and phospholipase A2 were analyzed at regular intervals in seven patients hospitalized as a result of acute hemorrhage pancreatitis. alpha 1-Antitrypsin and alpha 2-macroglobulin levels and trypsin-inhibitor capacity of serum were determined simultaneously. Serum trypsin concentrations were markedly raised in all patients. The levels of immunoreactive trypsin remained elevated for longer periods than those of urinary amylase. alpha 1-Antitrypsin and trypsin-inhibitor capacity were also significantly increased as compared with the post-illness values, but alpha 2-macroglobulin decreased considerably, reaching the lowest levels on the 5th day after admission. Consequently, phospholipase and trypsin are released to the circulation during hemorrhagic pancreatitis, but the increase in trypsin is compensated for by an increase in trypsin-inhibitor capacity of serum due to elevated alpha 1-antitrypsin levels. The decrease of alpha 2-macroglobulin in hemorrhagic pancreatitis was one of the most interesting findings, and it is proposed that this inhibitor may be consumed in the elimination of proteases through the reticuloendothelial system. The two patients who died had higher phospholipase values than those who recovered, but the prognosis could not be predicted from the values of the other measured variables.
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PMID:Serum phospholipase A2, immunoreactive trypsin, and trypsin inhibitors during human acute pancreatitis. 618 6


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