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)

Total protein, alpha1-antitrypsin, alpha2-macroglobulin, amylase, methemalbumin, tryptic amidase activity, radioimmunoassayable elastase 2, and three lysosomal hydrolases were determined in the ascites fluid from patients with acute pancreatitis. In eight patients methemalbumin was detected in ascites and serum, supporting the diagnosis of hemorrhagic pancreatitis. Significant levels (4-45 microgram/ml) of tryptic amidase activity were detected in ascites samples from all patients. Evidence is presented which demonstrates that the tryptic amidase activity is due to alpha2-macroglobulin-bound trypsin. Pancreatic elastase 2, determined with a new sensitive and specific radioimmunoassay, ranged from 400 to 2100 ng/ml in serum and from 650 to 4460 ng/ml in ascites fluid. Substantial amounts of alpha2-macroglobulin-bound trypsin and elastase 2, entering the circulation from the peritoneal cavity, might be responsible for certain serious complications seen in acute pancreatitis. However, with the exception of serum calcium and methemalbumin and the ascites fluid methemalbumin and total protein, none of the biochemical parameters studied showed a distinct correlation with the patient's outcome.
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PMID:Studies on the ascites fluid of acute pancreatitis in man. 62 83

Serum elastase-1, amylase, lipase, and trypsin-like immunoreactivity were measured in a group of 17 consecutive patients with acute pancreatitis. When assayed within 24 h of the onset of symptoms, all enzymes were found to be elevated, thus showing similar sensitivity. Elastase-1 did not improve the diagnostic score of the other enzymes studied. Owing to their much quicker and less expensive determinations, amylase and lipase should be considered the best initial markers of pancreatic injury. However, during the course of pancreatitis, amylase and in a lesser degree lipase returned to normal in more cases than elastase or trypsin; both were still elevated in 90% of the patients 10 days after the onset of the symptoms. Thus, trypsin and/or elastase-1 should be reserved for cases of doubtful or delayed diagnosis. The specificity and the positive predictive value of these enzymes need to be evaluated.
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PMID:Comparison of elastase-1 with amylase, lipase, and trypsin-like immunoreactivity in the diagnosis of acute pancreatitis. 243 92

Computerized tomography and ultrasound are helpful in the diagnosis of acute pancreatitis. The procedures, however, are not always available and so laboratory tests continue to play an important role. Serum amylase measurement is the most widely used test, despite its lack of sensitivity (75-92%) and specificity (20-60%). A cut-off point of 3-6 times the upper reference limit increases the specificity greatly, but at the expense of sensitivity. A method using chloronitrophenyl-maltotrioside as substrate has recently been rejected by the IFCC. A method using ethylidene-protected 4-nitrophenyl-maltoheptaoside and a new alpha-glucosidase has emerged as the method of choice. Amylase isoenzyme determinations have higher specificity than total amylase measurements. Serum lipase methods are more sensitive and specific, but methodological problems persist. Cationic trypsin-1 measurements yield high sensitivity but low specificity. Elastase-1 is claimed to correlate best with the clinical symptoms. Reasons for the widely differing reports on sensitivity and specificity of tests for pancreatitis are discussed.
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PMID:Support of the diagnosis of pancreatitis by enzyme tests--old problems, new techniques. 902 27

Recently an ELISA using specific antibodies to detect elastase-1 in serum has become available. Earlier studies using a radioimmunoassay reported a prolonged elevation of serum elastase as compared to other pancreatic enzymes in acute pancreatitis. The aim of the present study was to compare the changes of serum levels of ELISA-elastase-1, lipase and amylase in acute pancreatic damage following ERCP. Blood samples were prospectively collected at five time points before and after the endoscopic procedures in 212 patients. Samples were analyzed for pancreatic serum enzymes, acute phase proteins and routine parameters. A pain score was used for clinical evaluation. Relevant post ERCP pancreatic damage was defined as CRP elevation from < 10 mg/l to > 10 mg/l in the presence of persistent abdominal pain without laboratory evidence of cholangitis and without clinical or laboratory signs of pancreatitis before the endoscopic procedures. Elastase-1 time course paralleled the courses of lipase and amylase peeking at six hrs. There was no prolonged elevation of elastase-1. Ten out of 204 patients (4.9%) were found to have relevant pancreatic damage. Depending on the cut off point used, sensitivity/specificity were as follows: lipase 80-100%/30.9-71.6%; amylase 70-90%/44.3-88.7%; elastase-1 60-90%/64.9-81.4%. In conclusion ELISA-elastase-1 is a marker of acute pancreatic damage similar to lipase and amylase. Although elastase-1 may show a better specificity than the other enzymes, this seems to be a matter of definition of the normal range. The determination of serum ELISA-elastase-1 does not provide additional information in acute pancreatic damage as compared to a combination of lipase and amylase.
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PMID:Determination of elastase-1 serum levels in post ERCP/EST pancreatic damage. 1049 4

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

Liver injury is a manifestation of the systemic inflammatory response during acute pancreatitis. We have demonstrated that elastase induces macrophage tumor necrosis factor (TNF) production in distant organs, thus mimicking pancreatitis-associated organ injury. The aim of this study was to determine the mechanism by which elastase induces hepatic cytokine production. Rat livers (n = 40) were perfused with elastase +/- gadolinium (Gd) to inhibit Kupffer cells. Liver parenchymal enzymes and TNF were measured in the effluent. In vitro, rat hepatocytes or Kupffer cells were treated with elastase (1 U/ml) +/- Gd (0.5 mg/ml) or pyrrolidine dithiocarbamate (PDTC; 0.5 mg/ml). TNF protein, TNF messenger RNA, and NF-kappa B activation were determined. In vivo, Gd blunted the elastase-induced TNF production and decreased AST, ALT, LDH, and nonviable cells (propidium iodide) (P < or= 0.03 vs. elastase). In vitro, elastase induced TNF production from Kupffer cells (P < 0.001 vs. control) but not from hepatocytes. Gd or PDTC significantly attenuated the elastase-induced TNF production (P < 0.001). Elastase-induced overexpression of TNF messengerRNA and activation of NF-kappa B was attenuated by Gd. Pancreatic elastase induces a pattern of liver injury similar to that seen during acute pancreatitis by activating cytokine production and gene expression within Kupffer cells via NF-kappa B. Gd exhibits a protective effect against elastase-induced liver injury by inhibiting activation of NF-kappa B.
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PMID:Pancreatic elastase induces liver injury by activating cytokine production within Kupffer cells via nuclear factor-Kappa B. 1202 2

Pancreatic elastase-1 is a proteolytic enzyme exclusively produced in the pancreas, is stable when passing through the bowel, and its determination is associated with chronic pancreatitis. The clinical diagnosis of pancreatitis is based on anamnesis, physical examination, radiological, sonographic, endoscopic, and laboratory findings. Nowadays, there is a test for the determination of fecal elastase-1, by enzymatic reaction (enzyme-linked immunosorbent assay, ELISA), which specifically determines human elastase-1, promoting the pancreatic function evaluation. Parameters such as linearity, calibration curve, sensitivity, specificity, precision, accuracy, recovery, and receiver operator characteristic (ROC) curve are used to evaluate the test. The aim of this study was the validation of the immunoenzymatic assay (ELISA) and the use of its results in patients with HIV, alcoholics, and under antiretroviral therapy. The study involved 157 patients, 95 of them were HIV-infected, and 62 were completely healthy. The elastase-1 ELISA kit from Bioserv was used, and we noted that the obtained results were linear, sensitive, precise, and accurate. Moreover, our results suggest that this test can be a laboratory evaluation to determine the relationship of pancreatitis with alcohol use, but not its association with antiretroviral use in HIV patients (P=0.424). This test is useful to diagnose pathologies related to pancreatic insufficiency.
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PMID:Validation of fecal elastase-1 determination using immunoenzymatic assay in HIV-infected patients. 1862 2

L-asparaginase (L-asp) is a well-known anticancer agent used in the treatment of acute lymphoblastic leukemia (ALL) in children. However, it is also known to induce several acute complications, such as acute pancreatitis. This is a presentation of two pediatric acute lymphoblastic leukemia (ALL) cases of asparaginase-associated pancreatitis (AAP) diagnosed at an early stage based on elevated serum elastase-1 levels, in the presence of normal serum amylase levels. Early diagnosis and treatment of AAP, although imperative, is occasionally difficult if only standard diagnostic procedures are followed. Elastase-1 is a potentially useful marker for the early diagnosis of AAP. Therefore, the measurement of elastase-1 levels, in addition to amylase and lipase levels, is recommended in L-asp-treated patients.
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PMID:Early diagnosis of asparaginase-associated pancreatitis based on elevated serum elastase-1 levels: Case reports. 2464 3