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

Serum pancreatic enzymes (amylase, trypsin, pancreatic elastase 1, pancreatic phospholipase A2) and serum pancreatic secretory trypsin inhibitor (PSTI) were measured in 22 patients with moderate or severe acute pancreatitis. Serum levels of all pancreatic enzymes were elevated at the initial determination, but they fell rapidly to normal in both moderate and severe pancreatitis. In contrast, PSTI in severe pancreatitis increased after admission and reached the maximum on the second to the forth day after onset. There was a significant positive correlation between the level of PSTI and that of acute phase reactant (fibrinogen, alpha 1-antitrypsin), and serum PSTI in severe acute pancreatitis changed as if it was one of acute phase reactants. There was also a significant negative correlation between the level of serum PSTI and that of alpha 2-macroglobulin.
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PMID:[Changes in serum pancreatic enzymes and pancreatic secretory trypsin inhibitor in patients with severe acute pancreatitis]. 241 44

Serum pancreatic elastase 1 content in 45.9% of 203 samples from 32 patients with acute pancreatitis was found to be greatly elevated to greater than 1000 ng/dl, much higher than the control values (90 to 270 ng/dl), whereas serum alpha-amylase activity, in 62.3% of the same samples, was within the control range (100 to 460 IU/L). The increased pancreatic elastase 1 content persisted for several days after serum alpha-amylase activity returned to normal, suggesting that, compared with serum alpha-amylase activity, pancreatic elastase 1 content truly reflects the clinical course of acute pancreatitis. The measurement of pancreatic elastase 1 content appears to be more valuable in the diagnosis and prognosis of acute pancreatitis than that of serum alpha-amylase activity. In 41 patients with chronic pancreatitis, on the other hand, pancreatic elastase 1 content and serum alpha-amylase activity were within the normal range in 38.3% and 56.2% respectively, of 336 samples.
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PMID:Alterations in serum pancreatic elastase 1 content in acute and chronic pancreatitis: comparison with alpha-amylase activity. 387 32

Serum immunoreactive elastase 1 content was significantly elevated in acute pancreatitis. The mean content of the control group was 1.79 ng/ml (SD: 0.62 ng/ml), while that of patients with acute pancreatitis was 23.02 ng/ml (SD: 9.44 ng/ml). The increased content of pancreatic elastase 1 in acute pancreatitis continued for several days after onset, even though serum amylase activity had returned to normal.
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PMID:Changes in serum immunoreactive pancreatic elastase 1 in acute pancreatitis. 618 5

A radioimmunoassay for determination of human pancreatic elastase 1 was developed and the interaction of pancreatic elastase 1 with serum protease inhibitors (alpha 2-macroglobulin and alpha 1-antitrypsin) was investigated. Gel filtration studies showed that immunoreactive elastase 1 was present in serum and intact plasma as a complex with alpha 1-antitrypsin. Proelastase 1 in human pancreatic juice did not bind to protease inhibitors. But, after incubation with human serum or after activation with bovine trypsin, it was present as a complex with alpha 1-antitrypsin. The pancreatic elastase 1 content of the serum, measured by radioimmunoassay, was found to be influenced by the contents of both serum alpha 2-macroglobulin and alpha 1-antitrypsin. A significant inverse correlation was observed between the serum immunoreactive elastase 1 and alpha 2-macroglobulin contents in various hepatic diseases. The concentration of serum immunoreactive pancreatic elastase 1 was 1.79 +/- 0.62 ng/ml (mean +/- SD) in 28 normal controls. Its concentration was significantly increased in patients with acute pancreatitis, and although its concentration varied widely in patients with pancreatic cancer, its average concentration in these patients was significantly elevated.
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PMID:Radioimmunoassay of human pancreatic elastase 1. In vitro interaction of human pancreatic elastase 1 with serum protease inhibitors. 619 79

A radioimmunoassay for human pancreatic elastase 2 is described. DFP-Inactivated pancreatic elastase 2 is used both as standard and tracer. The concentration in normal human plasma is approximately 60 micrograms immunoreactive pancreatic elastase 2, which rises in acute pancreatitis. Pancreatic elastase 2 appears in plasma in a form with a molecular size exceeding that of the proenzyme. In vitro studies demonstrate that a complex between pancreatic elastase 2 and alpha 1-antitrypsin arises after incubation of a mixture of pancreatic juice and plasma. The results presented support the conclusion that proelastase is bound by alpha 1-antitrypsin after the discharge from the pancreatic gland to the extracellular tissue fluids around the gland.
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PMID:Studies on immunoreactive pancreatic elastase 2 in human serum. 696 10

By light and electron microscopic immunocytochemistry the distribution is described of human pancreatic elastase 1 (E1) during ontogenesis, in adults, in cases of acute and chronic pancreatitis, acute pancreatic ischaemia as well as pancreatic tumours. E1-positive cells were first detected in ductal sprouts in the 14th gestational week. Complete acini expressing E1 could be found from the 17th to the 20th week of gestation onwards. Scattered distinct E1-positive epithelia could be found in the ducts of fetal and adult pancreas. By immunoelectron microscopy, E1 was localized in rough endoplasmic reticulum, condensing vacuoles, zymogen granules of acinar epithelia and in acinar lumina. E1 appeared to be distributed homogeneously in zymogen granules. As specific markers of acinar cells, both monoclonal antibodies under study identified heterotopic pancreatic acini in peribiliar glands of the liver and also helped to visualize different damage patterns in pancreatitis. The acinar epithelia surrounding acute lipolytic necroses initially reacted more intensely with the E1-antibodies than undamaged pancreatic tissue. In acute ischaemia, acinar cells which are dissociated from intercalated ducts lost their immunocytochemical reactivity for E1. Pancreatic parenchyma involved in advanced acute pancreatitis as well as in chronic inflammation was detected only weakly by both E1-antibodies. However, atrophic lobules in post-inflammatory scars were stained more intensely by the E1-antibodies than normal parenchyma. Pancreatic tumours (adenomas, adenocarcinomas, solid-cystic tumours and islet cell tumours) were not labelled by these antibodies.
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PMID:Immunocytochemical localization of elastase 1 in human pancreas. 763 50

Pancreatic elastase 1 is secreted from pancreatic acinar cells as one of the digestive enzymes. Pancreatic elastase 1 is present in serum in a complex formation with alpha 1-antitrypsin, and is measured by immunological methods. Serum pancreatic elastase 1 increases in acute pancreatitis and chronic relapsing pancreatitis. As the serum level remains high for a long period after acute pancreatitis, serum pancreatic elastase 1 is also a tumor marker for the detection of early pancreatic cancer.
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PMID:[Pancreatic elastase 1]. 1179 73