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)

Previous studies have suggested that measurement of active enzymes in relation to proenzymes in serum of patients with pancreatitis may reflect the degree of zymogen activation in the gland. Here we describe the first single-tube assay for an active form of a pancreatic enzyme that is ordinarily synthesized as a proenzyme. Human procarboxypeptidase B, which we purified to near homogeneity, is approximately 13 000 Da larger than the active enzyme (EC 3.4.17.2). Antibodies specific for active carboxypeptidase B were obtained by affinity chromatography of anti-carboxypeptidase B antisera on a gel containing procarboxypeptidase B, then used to develop a single-tube radioimmunoassay for measuring active carboxypeptidase B in serum. Using this assay, we were able to detect, for the first time, active carboxypeptidase B in sera from patients with acute pancreatitis. Preliminary data show a correlation between the serum concentrations of active carboxypeptidase B and those of active trypsin complexed with serum inhibitors, but no correlation with serum amylase values.
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PMID:Radioimmunoassay of active pancreatic enzymes in sera from patients with acute pancreatitis. I. Active carboxypeptidase B. 401 33

A porcine pancreatic transplantation model was used to investigate possible protease activation in the pancreatic graft during preservation. After perfusion with Perfadex and cold ischemia for 24 h, but prior to reperfusion, activated carboxypeptidase B was demonstrated in tissue samples from the graft parenchyma with a Western blot technique, indicating that graft pancreatitis may already be initiated during the preservation phase. A higher degree of carboxypeptidase B activation was observed in grafts perfused at a pressure of 130 cm H20 than after perfusion at 70 cm H20. During reperfusion, the fraction of activated carboxypeptidase B gradually declined but was still detectable after 2 h. One group of pigs received aprotinin intravenously during reperfusion, but the protease inhibitor did not influence the degree of carboxypeptidase B activation in the biopsy specimen. Immunoblotting against cationic trypsinogen/trypsin was also performed. When activated trypsin was detectable, it never presented more than a few percent of the total amount of uncomplexed immunoreactive trypsinogen/trypsin.
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PMID:Protease activation in the porcine pancreatic allograft during preservation. 857 79

The incidence of acute pancreatitis within 100,000 inhabitants a year differs between 5 (Bristol) and 80 (USA). Even though the diagnosis of pancreatitis has become easier by the measurement of specific pancreatic enzymes there are still 30-40% of the fatal cases which are first diagnosed at autopsy. It is of utmost importance to assess the diagnosis and the severity of acute pancreatitis in the beginning to identify those patients with severe or necrotising disease who benefit from an early initiated intensive care therapy. Additionally, in view of new therapeutical concepts (e.g. antibiotic therapy in severe forms) and for the evaluation of new drugs, patients should be staged into mild and severe disease as early as possible. In most cases it is not possible to assess the severity clinically on hospital admission. Up to now the "gold standard" are imaging procedures (contrast-enhanced CT and MRI) which should be reserved for the severe cases to estimate the extent of pancreatic necrosis. The ideal predictor in blood or in urine should be objective, reliable, inexpensive, easy to measure, widely available, sensitive and specific. There are a variety of mediators of the "systemic inflammatory response syndrome" which are elevated in this disease (C-reactive protein, antiproteases, enzyme activation peptides like trypsinogen activation peptide (TAP) and carboxypeptidase B activation peptide (CAPAP), PMN-elastase, complement factors, chemokines and interleukins and others). Among all these mediators, C-reactive protein is the parameter best analysed. It has to be taken into account that it is not specific for AP and it's highest efficacy is reached after > 48 hours after the onset of disease. However, because usually a certain time elapses (approximately 24-48 hours) until patients are hospitalised the time delay seems not to a major disadvantage.
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PMID:[Acute pancreatitis--clinical and technical laboratory diagnostic and prognostic assessment]. 1107 88

We used a peptidomic approach for the analysis of the low molecular weight proteome in rat pancreatic tissue extracts. The goal was to develop a method that allows identifying endogenous peptides produced in the pancreas in the course of acute pancreatitis. The workflow combines peptides enrichment by centrifugal ultrafiltration, fractionation by isoelectric focusing, and LC-MS/MS analysis without prior enzymatic digestion. The method was assessed on pancreatic extracts from 3 rats with caerulein-induced pancreatitis and 3 healthy controls. A qualitative analysis of the peptide patterns obtained from the different samples was performed to determine the main biological processes associated to the identified peptides. Comparison of peptidomic and immunoblot data for alpha-tubulin, beta-tubulin and coatomer gamma showed that the correlation between the number of identified peptides and the protein abundance was variable. Nevertheless, peptidomic analysis highlighted inflammatory and stress proteins, which peptide pattern was related to acute pancreatitis pathobiology. For these proteins, the higher number of peptides in pancreatitis samples reflected an increase in protein abundance. Moreover, for murinoglobulin-1 or carboxypeptidase B, peptide pattern could be related to protein function. These data suggest that peptidomic analysis is a complementary approach to proteomics for investigating pathobiological processes involved in acute pancreatitis.
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PMID:Analysis of the pancreatic low molecular weight proteome in an animal model of acute pancreatitis. 2060 30