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)

Pancreatic juice and serum from patients with acute pancreatitis contain three enzymes that have lipolytic activity: L1 and L2, which are pancreatic isoenzymes or isoforms of lipase (EC 3.1.1.3), and L3, which is probably pancreatic carboxyl ester lipase, also known as cholesterol esterase (EC 3.1.1.13). These enzymes are readily separated electrophoretically on agarose and can be developed with an overlay of Kodak Ektachem lipase slide material. The latter acts as a dry-reagent developing substrate, with the enzymes producing blue bands in the slide material. We found L1 in about one-half of normal persons, L2 in none, and L3 in all. We assayed for amylase (EC 3.2.1.1), amylase isoenzymes, lipase, and lipase isoforms in the sera of 100 patients with suspected acute pancreatitis. L2 lipase has the greatest diagnostic efficiency for the diagnosis of pancreatitis, compared with total amylase, P3 amylase, and total lipase. Lipase and L2 could replace amylase, an inefficient test, for the diagnosis of patients with suspected acute pancreatitis. In patients receiving organ transplants, a serum amylase value of greater than 300 U/L or a lipase of greater than 1000 U/L discriminated well between patients with and without complications and (or) acute rejection.
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PMID:Lipase isoforms and amylase isoenzymes: assays and application in the diagnosis of acute pancreatitis. 170 30

For patients with symptoms of pancreatitis, measurement of amylase in serum reportedly is more sensitive than that of lipase in acute pancreatitis, whereas lipase reportedly is more specific. However, serum lipase activities exceeding the upper reference limit (URL) have been reported for many patients who did not have pancreatitis. I reviewed the serum lipase and amylase concentrations of 493 consecutive inpatients and emergency department patients for whom both tests were ordered. Serum lipase and amylase activities, determined with an Ektachem 700 analyzer, were less than or equal to URL for 390 patients (83%) and greater than URL for 103. Medical records of 101 of these 103 were reviewed; 18 had acute or chronic relapsing pancreatitis. In this latter group, serum lipase values greater than URL had 100% sensitivity and 84% specificity; those of serum amylase greater than URL had 72% sensitivity and 88% specificity. However, the test combination of serum lipase greater than URL and serum amylase less than or equal to URL also occurred in 84% of the patients in which review of the medical records revealed nonpancreatic gastrointestinal or hepatobiliary disorders as the primary problem (n = 55). Therefore, serum lipase activity measured with the Ektachem assay is also often increased in patients with intra-abdominal disorders that appear to be nonpancreatic.
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PMID:Lipase activity in serum measured with Ektachem is often increased in nonpancreatic disorders. 170 30

It is believed that activation of zymogen proteases occurs in the early development of acute pancreatitis. This hypothesis was proved on subcellular fractions of rat pancreas after induction of pancreatitis by infusion of high doses of cerulein for 2 h. Secretory enzyme activities were measured spectrophotometrically in subcellular fractions obtained by differential ultracentrifugation. Additionally, trypsin and chymotrypsin activities were detected by enzyme blots after isoelectric focusing. Finally immunoblotting (Western-blot analysis) for amylase, lipase, trypsin/ogen, and chymotrypsin/ogen was carried out on fractions separated by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). In cerulein pancreatitis, subcellular fractions of secretory granules and vacuoles showed significant amounts of free trypsin and chymotrypsin activities compared with controls. The presence of free activities of serine proteases was paralleled by the appearance of numerous low molecular weight peptides detected by 2-dimensional electrophoresis and SDS-PAGE, which in part represented proteolytically cleaved secretory proteins. It is concluded that the intracellular activation of serine proteases that occurs in cerulein pancreatitis could contribute to further acinar cell destruction.
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PMID:Evidence of intracellular activation of serine proteases in acute cerulein-induced pancreatitis in rats. 170 79

Acute pancreatitis with severe belt-like upper abdominal pain developed within 1-4 weeks of starting medication in three patients (29-year-old man with ulcerative colitis; 43-year-old woman and 22-year-old woman with Crohn's disease) treated, for the first time, with 5-aminosalicylic acid (mesalazine), 500 mg three times daily. Concentrations of lipase initially were 545, 1182 and 3000 U/l, and of amylase 243, 449 and 129 U/l, respectively. Symptoms receded within a few hours after the drug had been discontinued, enzyme levels returning to normal in the course of the next 2-3 weeks. On repeating the drug in two of the patients, in lower dosage, the pancreatitis recurred within a few days. These observations support the view that 5-aminosalicylic acid can cause acute pancreatitis, perhaps as an allergic reaction.
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PMID:[Pancreatitis associated with 5-aminosalicylic acid]. 170 59

145 clinical observations of 114 patients with Crohn's disease and 65 observations of 47 patients with ulcerative colitis were analyzed prospectively concerning the prevalence of pathologically elevated levels of serumamylase or -lipase and acute pancreatitis. Painless hyperamylasemia or hyperlipasemia were found in 18 of 114 patients with Crohn's disease (15.8%) and in 10 of 47 patients with ulcerative colitis (21.3%) without morphological abnormalities on ultrasound. Range of elevated serumamylase levels differs from 35 to 68 U/L (Ref.-value less than 34 U/L), range of serumlipase levels varies from 199 to 858 U/L (Ref.-value less than 190 U/L). Pathologically elevated levels of serumamylase and -lipase persisted for 17.7 +/- 9.0 (5-28) days in Crohn's disease and 22.8 +/- 9.8 (7-33) days in ulcerative colitis. No relation to the activity or the duration of the disease, drug treatment or the weight loss of the patients could be shown. Acute pancreatitis was found in 4 of 114 patients (3.5%) with Crohn's disease, whereas in ulcerative colitis acute pancreatitis was diagnosed in 1 of 47 patients (2.1%). Regarding the promoting factors, drugs (azathioprine and salazosulfapyridine) and mechanical alterations of the bile duct (primary sclerosing cholangitis) or the pancreas (pancreas divisum) were found in 4 of the 5 patients. However the case of a 23 year old woman suffering from Crohn's ileocolitis who died of an idiopathic pancreatitis remains obscure.
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PMID:[Hyperamylasemia, hyperlipasemia and acute pancreatitis in chronic inflammatory bowel diseases]. 170 51

Serum amylase activity and the amylase:creatinine clearance ratio (Cam:Ccr%) are two of the most commonly used indicators for the diagnosis of pancreatitis. However, published data on the effect of pregnancy on these indicators are conflicting. Furthermore, there are no published data on the effect of pregnancy on serum lipase activity, which is considered one of the most sensitive and specific indicators of pancreatitis. A study was undertaken to determine the effect of pregnancy and gestational age on serum amylase, serum lipase and Cam:Ccr% levels and to establish a baseline of normal values for use in the diagnosis of pancreatitis in pregnant women. Serum amylase, serum lipase and Cam:Ccr% levels were determined on a sample population consisting of 175 pregnant women with gestational ages ranging from 5 to 40 weeks and on a control group of 44 reproductive-age, nonpregnant women. The study results indicated that there is no significant difference in serum amylase, serum lipase and Cam:Ccr% levels between pregnant and nonpregnant women. Cam:Ccr% showed a small but statistically significant increase in the third trimester of pregnancy.
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PMID:Pancreatic enzyme activity in pregnancy. 171 46

During an 8-year period, 14 adult patients were hospitalized with typhoid fever confirmed by positive blood cultures for Salmonella typhi. Among these patients, we have retrospectively (n = 7) and prospectively (n = 7) evaluated pancreatic disturbance by serum amylase and lipase measurements at the time of admission. In 7 (50%) biological signs of pancreatitis were noted: mean amylase level 81 IU (range 30-201 IU, normal value less than 40 IU), mean lipase level 949 IU (range 468-2,000 IU, normal value less than 300 IU). Clinical signs of pancreatitis were observed in 4 cases, one of whom had a concomitant salmonella biliary tract infection and gall stones demonstrated by laparotomy and the others a normal biliary ultrasonographic examination with a swelling of the pancreas. No alcohol or drug use or other infection were noted before admission. This study suggests that biological or clinical pancreatitis should be considered as a frequent complication of typhoid fever. S. typhi should therefore be added to the list of pathogens implicated in the pathogenesis of non-alcoholic or non-lithiasic pancreatitis.
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PMID:Pancreatic disturbances and typhoid fever. 171 81

The pathogenesis of endoscopic retrograde cholangiopancreatography (ERCP)-induced pancreatitis is poorly understood. To elucidate a role for pancreatic enzymes in ERCP-induced pancreatitis, we measured serum amylase, lipase, trypsin, and elastase in 25 patients undergoing ERCP. Serum alpha 1-antitrypsin and alpha 2-macroglobulin, two major pancreatic protease inhibitors, also were measured. All pancreatic enzymes measured rose significantly after ERCP. Pancreatic duct cannulation was associated with a greater elevation in serum amylase and lipase. Circulating alpha 2-macroglobulin was reduced by 7% (p = 0.04) 6 h after ERCP, whereas circulating alpha 1-antitrypsin increased over the same time period. Papillotomy, stent placement, or underlying disease did not influence changes any further. Three patients developed ERCP-induced pancreatitis. All three patients had circulating alpha 2-macroglobulin levels below 243 mg/dl (p = 0.03). The ERCP-induced alterations in circulating pancreatic enzymes and their inhibitors are similar to changes seen in clinical pancreatitis. Low circulating alpha 2-macroglobulin levels may predispose to ERCP-induced pancreatitis.
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PMID:The effect of ERCP on circulating pancreatic enzymes and pancreatic protease inhibitors. 171 6

The essential role of cholecystokinin (CCK) in pancreatic regeneration after pancreatitis or resection has been supposed, but not yet clearly demonstrated. In rats, 6-8 weeks after 60% distal resection of the pancreas a gradual increase in pancreatic weight and contents of DNA, protein, trypsin, chymotrypsin and amylase, occurred (there was no increase in lipase); Pancreatic regeneration stopped thereafter. Nonparallel increases in enzyme values were similar to those seen after CCK administration. Indeed, basal CCK levels increased significantly by the 6th week and declined thereafter. A one month s.c. administration of CCK-octapeptide (CCK-8) (3 x 300 ng/kg/d) accelerated regeneration in the first month, but it had almost no effect during the second or third postoperative months. A two week s.c. administration of a specific CCK antagonist, CR 1409 (3 x 4 mg/kg/d) totally prevented regeneration by the fifth and sixth weeks, but did not diminish pancreatic weight or DNA and protein contents during the first two weeks. Alcohol administration (12 g/kg/d) reduced CCK release and prevented pancreatic regeneration during the three-month experimental period. These data indicate that CCK has an essential role in pancreatic regeneration and that the deleterious effect of alcohol on regeneration involves inhibition of CCK release.
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PMID:Essential role of cholecystokinin in pancreatic regeneration after 60% distal resection in rats. 802 68

We investigated pancreatic gene expression in the rat in response to taurocholate-induced acute pancreatitis. Concentrations of transcripts encoding pancreatic protein showed noncoordinated alterations. Contents in amylase, trypsinogen I, chymotrypsinogen B, elastase 1, and procarboxypeptidase A mRNAs decreased by greater than 50% during the acute phase (days 0-2), whereas actin and lithostathine mRNAs increased 5 and 0.6 times, respectively, and pancreatitis-associated protein (PAP) mRNA increased greater than 200 times, indicating redirection of the pattern of gene expression. Synthesis of pancreatic proteins was also altered in a noncoordinated manner. During the acute phase, it decreased more for trypsinogen I and chymotrypsinogen B than for amylase and lipase, whereas synthesis of the PAP increased dramatically. For amylase and chymotrypsinogen B, we compared the patterns of changes in mRNA concentrations, rates of synthesis, and pancreatic contents. Changes in enzyme contents and synthetic rates were temporally correlated during the acute phase. On the contrary, changes in mRNA concentrations and enzyme synthesis were not coordinated, suggesting that control of synthesis partly occurred at the posttranscriptional level. It was concluded that induction of pancreatitis is accompanied by transcriptional and posttranscriptional modifications resulting in rapid and massive rearrangement of the pattern of pancreatic protein gene expression.
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PMID:Pancreatic gene expression is altered during acute experimental pancreatitis in the rat. 171 58


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