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)

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

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

The elevation of plasma pancreatic elastase 1 in patients with pancreatic cancer is caused by concomitant pancreatitis. There is no report that pancreatic ductal cell carcinoma tissue itself produced elastase 1. A 54-year-old woman underwent total pancreatectomy for pancreatic ductal cell carcinoma. Her plasma elastase 1 level subsequently decreased from the preoperative value of 406 ng/dl to values ranging between 96 ng/dl and 119 ng/dl, until 6 months after the operation, when it began to increase gradually to a maximum of 300 ng/dl in association with local recurrence and hepatic metastasis. Immunohistochemical staining of elastase 1 was positive in the primary tumor resected at operation as well as in the locally recurrent and hepatic metastatic tumors obtained at autopsy. These findings suggested that elastase 1 was produced by the tumor cells in this patient. This is the first case in which pancreatic ductal cell carcinoma cells produced elastase 1.
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PMID:Pancreatic ductal cell carcinoma producing pancreatic elastase 1. 841 80

Views on the existence of a negative feedback between pancreatic secretion and intraduodenal of proteases in humans are controversial. The objective of the study was to find out whether enzyme substitution will have an impact on pancreatic enzyme secretion and pain in chronic pancreatitis. The preparation Panzytrate 2500 (2 x 3 capsules/day containing 1250 units of proteases per capsule) was administered for a 4-week period. In 18 patients with chronic pancreatitis (7 with the severe and 11 with the medium severe and mild form of pancreatitis) the faecal and serum pancreatic elastase was assessed one day before and one day after enzyme substitution therapy. A significant reduction of the faecal elastase concentration (p = 0.03) and serum elastase (p = 0.00375) was recorded in patients with mild and medium severe CP. The values of faecal and serum pancreatic elastase 1 were insignificantly reduced also in patients with severe chronic pancreatitis. Pain relief was statistically significant already after two weeks' administration of enzyme substitution therapy (p = 0.0233) and after four weeks' treatment (p = 0.00766). The results support the importance of the negative feedback on regulation of pancreatic secretion and the positive effect of substitution therapy on pain in chronic pancreatitis.
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PMID:[Effect of pancreatic substitutes on fecal and serum elastase and on pain in patients with chronic pancreatitis]. 1122 80

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