Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0001339 (acute pancreatitis)
 10,593 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

This paper reviews recent developments of analytical methods for the determination of alpha-amylase, of its isoenzymes, and of lipase. The evaluation of severity and etiology of acute pancreatitis by enzyme assays, e.g., pancreatic elastase 1, phospholipase A2, and routine enzymes are discussed. The limited significance of enzyme determinations as compared to imaging and endoscopic procedures for the diagnosis of chronic pancreatitis is demonstrated. Indirect "tubeless" tests for the evaluation of pancreatic exocrine insufficiency with respect to the secretion of chymotrypsin (chymotrypsin in stool and NBT-PABA test) and cholesterol esterase (pancreolauryl test) are reviewed. Finally, the superiority of morphologic investigations over biochemical tests for the timely detection of pancreatic carcinoma is shown.
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PMID:Advances in the enzyme diagnosis of pancreatic diseases. 225 33

Immunoreactive phospholipase A2 (EC 3.1.1.4) was measured by a new sensitive time-resolved fluoroimmunoassay in the serum of 58 healthy subjects and 103 patients with acute pancreatitis. Patients with acute pancreatitis were grouped according to the etiology and clinical severity of the disease. The mean phospholipase A2 concentration in the reference (healthy) group was 5.5 (SD 1.9) micrograms/L. In acute pancreatitis the mean phospholipase A2 concentration was increased on the first day after hospital admission in all groups, and returned to normal somewhat more slowly than did serum amylase, especially in the patients with severe alcoholic pancreatitis. In this latter group the mean concentration of serum phospholipase A2 on the first day was 42.6 (SD 29.5) micrograms/L. In patients with pancreatic cancer, serum phospholipase A2 was 29.2 (SD 21.3) micrograms/L. The phospholipase A2 and amylase values were closely associated in all groups. The clinical sensitivities were 90.9% for severe alcoholic pancreatitis and 87.5% for pancreatic cancer. Immunochemical determination of phospholipase A2 in serum provides fast and specific detection of injury to pancreatic acinar cells. In addition to the early diagnosis of acute pancreatitis, follow-up determinations of phospholipase A2 seem to be useful in differentiating between mild and severe forms of pancreatitis.
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PMID:Immunoreactive phospholipase A2 in serum in acute pancreatitis and pancreatic cancer. 240 88

The new synthetic polyvalent protease inhibitors gabexate mesilate (ethyl-p[6-guanidinohexanoyloxy]-benzoate methansulfonate) and camostate (N,N-dimethylcarbamoylmethyl-4-[4-guanidinobenzoyloxy]-phenylacetate methansulfonate) were tested for possible inhibition of phospholipase A2 activity. In a pilot study, we treated 17 patients suffering from acute pancreatitis with continuous intravenous administration of gabexate mesilate, 450 mg/d. The results were compared with a placebo group (same standard therapy) of 21 patients suffering from acute pancreatitis. In vitro experiments showed that, at concentrations between 10(-4) and 5 X 10(-4) mol/L (depending on the enzyme assay employed) for gabexate mesilate and between 10(-3) and 5 X 10(-4) mol/L for camostate, a 50% reduction in phospholipase A2 activity was effected. Comparing the two groups of acute pancreatitis patients after 6 days of treatment with gabexate mesilate, we observed a statistically significantly lower alpha-amylase activity in the serum of treated patients compared with the placebo group.
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PMID:Gabexate mesilate and camostate: new inhibitors of phospholipase A2 and their influence on the alpha-amylase activity in serum of patients with acute pancreatitis. 241 25

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

Acute pancreatitis (AP) is believed to result from intraparenchymal activation of trypsin and other digestive enzymes within the pancreas followed by autodigestion of the gland. Gabexate mesilate (FOY), a synthetic guanidino acid ester exhibiting potent and versatile inhibitory actions on a number of proteinases (e.g., trypsin, kallikrein, C1-r, C1 esterase, plasmin, thrombin, phospholipase A2), was examined for its ability to protect the rat pancreas against development of AP induced by pharmacological doses of ceruletide (CRT). Rats were i.v. infused for 6 h with either CRT (5 micrograms/kg/h) or CRT + FOY (50 mg/kg/h). In FOY-treated rats the serum amylase and trypsinogen concentrations were reduced by 60 and 80%, respectively, compared to rats infused with CRT alone. Histologically, the extent of acinar cell vacuolization in the pancreas was significantly reduced and interstitial edema, although not assessed by quantitative morphometric techniques, appeared to be qualitatively lessened in the FOY-treated rats. The ability of FOY to inhibit significantly AP produced by supramaximal doses of CRT, coupled with its inhibitory properties on components of the coagulation and complement cascades, stress the importance of continued research on this compound as a potential therapeutic agent for treatment of AP and its systemic sequelae.
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PMID:Gabexate mesilate (FOY) protects against ceruletide-induced acute pancreatitis in the rat. 244 41

The effects of standard, fat-rich, protein-rich, and carbohydrate-rich diets combined with either long-term ethanol ingestion or tap water ingestion on the behavior of plasma phospholipase A2 activity during experimental acute pancreatitis were studied in rats. Phospholipase A2 activity was compared with amylase activity in the plasma. Three hundred eighty-four male Wistar rats were randomized into eight groups receiving different diets with either 15 percent (volume for volume) ethanol or tap water for 12 weeks. Thereafter, all groups were subdivided into control (intact) and pancreatitis subgroups. Pancreatitis was induced by retrograde bile infusion into the pancreatic ducts. Sampling was performed 24 hours after induction in the surviving rats. Ethanol ingestion alone and in combination with the fat-rich diet increased the mortality rate (p less than 0.05), whereas the lowest mortality rate was observed in the carbohydrate-rich diet and water and the carbohydrate-rich diet and ethanol groups. Plasma phospholipase A2 activity increased in most of the groups, but it correlated with the mortality rate in the standard diet group only. Plasma amylase activity increased significantly in all groups, but did not correlate with mortality rate. Plasma phospholipase A2 activity seems to be dependent on diet in experimental acute pancreatitis in rats. Plasma amylase activity may be less affected by the dietary composition, but the lack of a correlation with mortality makes it unreliable as a parameter of severity in experimental acute pancreatitis.
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PMID:Behavior of plasma phospholipase A2 activity in experimental acute pancreatitis according to diet. 245 24

The peritoneal permeability to differently sized dextran molecules; Mw 4,000, 10,000, 20,000, and 40,000 was investigated in rats with bile-induced acute pancreatitis. Following intraperitoneal deposition, repeated blood samples for measurement of the different dextrans were collected. The results showed increased peritoneal permeability to molecules between 4,000-20,000 daltons in animals with pancreatitis, whereas there was no significant difference for molecules of 40,000 daltons compared to healthy control animals. Also, the passage of phospholipase A2 (Mw 14,000) over the peritoneal membrane was increased during pancreatitis. It is suggested that the transperitoneal route may be of pathophysiological importance in the development of the systemic components of severe acute pancreatitis.
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PMID:Increased peritoneal permeability in acute experimental pancreatitis. 246 19

The purpose of this study was to assess the involvement of oxygen radicals and phospholipase A2 in acute pancreatitis. Acute pancreatitis was induced in rats by the CCK-analogue cerulein (5 micrograms/kg.h) for 30 min, 3.5 h, and 12 h. At the end of the infusion, serum enzymes and the lipid peroxidation products conjugated dienes and malondialdehyde in the tissue were measured. Moreover, tissue samples underwent lightmicroscopical examination. After 3.5 h cerulein, an interstitial edema and a beginning accumulation of granulocytes in the pancreatic gland is observed. These changes are aggravating within 12 h, leading to tissue necrosis and migration of the granulocytes into the tissue. Concomitantly amylase and lipase increased by 15 and 35 times, respectively. Conjugated dienes and malondialdehyde increase already after 30 min cerulein and reach their highest levels after 3.5 h cerulein. At the same time the tissue activity of phospholipase A2 is elevated three fold. Rats were treated with superoxide dismutase and catalase before cerulein infusion. Treatment significantly prevents tissue necrosis, granulocyte accumulation, and edema formation. The enhanced activity of phospholipase A2, however, is unaffected by the treatment. Oxygen radicals seem to be instrumental in the development of the disease.
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PMID:Involvement of oxygen radicals and phospholipase A2 in acute pancreatitis of the rat. 246 44

In a prospective clinical trial 85 patients with acute pancreatitis were analysed for serum total amylase, pancreatic amylase, pancreatic lipase, trypsin, elastase 1, and immunoreactive phospholipase A2 (IR-PLA2). The diagnostic sensitivity of serum IR-PLA2 was comparable to that of serum total amylase, pancreatic amylase, and trypsin. The specificity of IR-PLA2 is superior to that of serum total amylase determination due to the fact that the IR-PLA2 determination is based on an antibody against human pancreatic PLA2.
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PMID:Diagnostic value of immunoreactive phospholipase A2 in acute pancreatitis. 246 45

Because the severity of acute pancreatitis is difficult to assess in the early stage, analyses were made of the diagnostic specificity and sensitivity of computed tomography (CT), C-reactive protein (CRP), serum phospholipase A2 and other laboratory parameters. In a series of 88 patients with clinically suspected severe acute pancreatitis, statistically significant differences were found between mild and severe disease in regard to CRP (97.1 vs. 265.7 mg/l), contrast enhancement of the pancreas at CT (45.3 vs. 22.7 Hounsfield units) and phospholipase A2 activity (5.3 vs. 11.2 nmol FFA/ml min). No significant intergroup difference was found in number of prognostic signs (1.7 vs. 4.1) or in extrapancreatic scores at CT (4.4 vs. 6.4). The sensitivity/specificity of different methods in severe pancreatitis were as follows: Prognostic signs 77.5/75%, CRP (greater than 140 mg/l) 100/81%, phospholipase A2 (greater than 11 nmol FFA/ml min) 42/100%, extrapancreatic score at CT (greater than 4) 100/29%, and contrast enhancement of the pancreas (less than 30 HU) 66/100%. Amylase determination was nonspecific (2-4%). The outcome in acute pancreatitis was most accurately predictable with CT or CRP.
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PMID:Early assessment of acute pancreatitis. A comparative study of computed tomography and laboratory tests. 246 76


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