Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.4.21.4 (trypsin)
42,187 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The present work describes the effect of seven naturally occurring proteinase inhibitors on the human pancreatic endopeptidases cationic trypsin, anionic trypsin, chymotrypsin I, chymotrypsin II, and protease E (an elastase-like protease). The inhibitors tested in order of their decreasing effectiveness were alpha-1-proteinase inhibitor (alpha-1-antitrypsin), lima bean trypsin inhibitor, soybean trypsin inhibitor, Bowman-Birk (soybean) inhibitor, Kunitz pancreatic trypsin inhibitor, porcine Kazal inhibitor, and chicken ovomucoid. The human trypsins demonstrated a higher degree of susceptibility to these inhibitors than did the chymotrypsins while human protease E showed remarkably little inhibition by any of these naturally occurring proteinase inhibitors except for alpha-1-proteinase inhibitor. The contribution of each of these proteolytic enzymes to the total proteolytic activity of crude extracts was also investigated using specific active-site directed reagents. These studies revealed that the trypsins constituted approximately 35% of the proteolytic activity while the chymotrypsins represent approximately 32% of the total proteolytic activity. Human protease E and possibly human pancreatic elastase are responsible for approximately 21% of this activity as measured on crude pancreatic extracts.
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PMID:Inhibition spectra of the human pancreatic endopeptidases. 108 8

This study was undertaken to investigate the incidence of postoperative hyperamylasemia and amylase levels of intraperitoneal drainage in 106 patients undergoing major abdominal surgery. The results were as follows: 1. Postoperative hyperamylasemia was found in 36.8% of all patients, with higher incidence of hyperamylasemia being in accordance with greater surgical intervention to the pancreas. 2. The isoamylase pattern of postoperative hyperamylasemia was dominant in the salivary type. 3. The levels of such serum pancreatic enzymes as lipase, trypsin and elastase 1 were higher in the pancreatic-type group than in the salivary-type group, particularly with the elastase 1 levels being statistically higher in the former. 4. Increases in peritoneal amylase activity were found in those cases of greater surgical intervention to the pancreas, postoperative hyperamylasemia and higher serum pancreatic isoamylase levels. 5. Diagnosis of postoperative pancreatitis was confirmed in one case by clinical and laboratory findings and CT examination. It might be concluded that postoperative high peritoneal amylase levels suggest occurrence or possible occurrence of postoperative pancreatitis.
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PMID:[Postoperative hyperamylasemia in patients undergoing abdominal surgery: the relationship between serum and peritoneal amylase levels]. 127 73

Amylase concentration in serum is frequently found increased in chronic renal insufficiency without being associated with pancreatic diseases. A prospective study was performed in 71 patients with chronic renal insufficiency undergoing hemodialysis for comparison of different pancreatic enzymes in serum. 7 patients were not considered in this comparative study because of chronic pancreatitis-like-changes in ultrasound. Increased serum concentrations were found for total amylase in 27 patients (42.2%), pancreatic amylase in 26 patients (25.0%), lipase in 50 patients (78.1%), immunoreactive trypsin in 61 patients (95.3%) and for elastase 1 in 7 patients (10.9%). Hemodialysis did not affect any of the investigated pancreatic serum-enzymes. Elastase 1 determination in serum appears superior to the other pancreatic serum-enzymes because of higher specificity, not limited by renal insufficiency. The different serum concentration of elastase 1 and trypsin, which have a similar molecular weight, points towards a completely different clearance mechanism for these enzymes.
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PMID:[Effect of chronic renal failure and hemodialysis on the pancreas-specific enzyme pattern in the serum]. 169 2

Serum concentrations of trypsin and elastase I were determined in 109 HIV Ab-positive patients (52 asymptomatic HIV-infected patients, 25 with lymphadenopathy syndrome, and 32 with acquired immunodeficiency syndrome) to assess the prevalence of possible pancreatic damage in these patients. Serum trypsin was abnormally elevated in 46 of the 109 patients (42.2%): 19 of the 52 asymptomatic HIV-infected patients (36.6%), 9 of the 25 with lymphadenopathy syndrome (36%), and 18 of the 32 with acquired immunodeficiency syndrome (56.3%). Serum elastase 1 was elevated in 14 of the 109 HIV Ab-positive patients (12.8%): 3 of the 52 asymptomatic HIV-infected patients (5.8%), 3 of the 25 with lymphadenopathy syndrome (12%), and 8 of the 32 with acquired immunodeficiency syndrome (25%). None of the patients with abnormally high serum pancreatic enzyme concentrations had clinically evident pancreatic disease. There was no statistically significant difference in serum levels of trypsin and elastase I between drug addicts and nonaddicts, between alcoholics and nonalcoholics, or between those with cytomegalovirus infection and those without. A significant inverse relationship was found between serum enzyme concentrations and the number of CD4+ lymphocytes. The results of this study show that high levels of serum trypsin and elastase are present in an elevated percentage of patients with acquired immunodeficiency syndrome, suggesting that the pancreas is frequently damaged in this disease. The finding of abnormally high serum enzyme concentrations not only in patients with AIDS, but also in asymptomatic carriers and in patients with lymphadenopathy syndrome suggests an association between HIV infection and the development of pancreatic lesions.
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PMID:Serum pancreatic enzymes in HIV-seropositive patients. 173 48

Using the Tb3+ luminescence technique, we showed that bovine subunit III, a defective pancreatic serine endopeptidase-like protease, possessed a single metal ion binding site able to bind Tb3+ with a high affinity comparable to that of porcine elastase. The topology of the metal ion binding site in subunit III is predicted from sequence homologies and modeling experiments based on the known crystallographic three-dimensional structures of the equivalent sites in porcine elastase 1 and bovine beta-trypsin. Moreover, the Tb3+ luminescence technique in parallel to a 19F NMR investigation, allowed us to measure the binding of a very potent specific inhibitor of porcine elastase (trifluoroacetyl-L-lysyl-alanyl p-trifluoromethylphenylanilide) to bovine subunit III. These results confirm that, although devoid of any specific activity, subunit III might possess a conformation close to that of an active enzyme and further support the analogy between subunit III and an elastase-like family.
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PMID:Binding of terbium and of an elastase inhibitor to bovine pancreatic subunit III, an inactive protease E. 230 77

In patients with pancreatic cancer deoxyribonuclease I (DNase I) serum levels were compared with those of other known pancreatic enzymes. Serum deoxyribonuclease I, elastase 1, immunoreactive trypsin, amylase and phospholipase A2 were determined in 40 healthy controls, 28 patients with pancreatic cancer, 49 with chronic pancreatitis and 40 with extra-pancreatic diseases. The analysis of variance showed a significant difference among groups for serum DNase I values. However, none of the 3 groups of patients had a mean deoxyribonuclease I value higher than that of the healthy controls. In pancreatic cancer and chronic pancreatitis patients, increases in the 4 pancreatic enzymes values were found in percentages that were higher than those for DNase I. A significant correlation was found between DNase I and phospholipase A2, but not between DNase I and elastase 1, immunoreactive trypsin and amylase serum activities. The findings indicate that deoxyribonuclease I serum determination is an even less satisfactory index of pancreatic malignancy than the other pancreatic enzymes. Rather than expressing pancreatic damage, any variations in this enzyme appear more likely to reflect an aspecific phenomenon.
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PMID:Deoxyribonuclease I serum activity in pancreatic cancer. 235 55

In order to investigate modifications of serum levels of elastase 1, immunoreactive trypsin, alpha 1-antitrypsin and alpha 2-macroglobulin in chronic pancreatic disease, and to speculate on the possible relationships among these parameters, the enzymes and inhibitors were assayed in the sera of 33 control subjects, 34 pancreatic cancer, 28 chronic pancreatitis and 36 extra-pancreatic diseases. An increase of elastase 1, alpha 1-antitrypsin and alpha 2-macroglobulin was detected in pancreatic cancer, chronic pancreatitis and extra-pancreatic diseases; no changes were found for serum immunoreactive trypsin. Multiple regression analyses showed that only 7% of elastase 1 was explained by inhibitors with alpha 1-antitrypsin playing a major role. Inhibitors did not influence immunoreactive trypsin. Our data indicate that the variations of the serum levels of proteases and antiproteases in chronic pancreatic disease are probably independent of each other.
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PMID:Serum elastase 1 and immunoreactive trypsin in chronic pancreatic disease: is there any relationship with trypsin inhibitors? 242 33

Porcine pancreatic hydrolases in juice and homogenate surveyed by electrophoretic separation in agarose gel, at pH 8.6 and subsequently characterized using substrates of various specificity, either directly in the gel or after transfer to nitrocellulose (enzymoblotting) showed: Anodal and cathodal trypsin with Bz-Arg-pNA. Chymotrypsin A, B, and C with similar, but not identical, activities to Suc-Ala-Ala-Pro-Phe-pNA, Bz-Tyr-pNA, Suc-Phe-pNA and Ac-Phe-beta NE and with differences in their molecular weights and electrophoretical charges. Elastase I and protease E with Suc-(Ala)3-pNA and MeO-Suc-Ala-Ala-Pro-Val-pNA and elastase I also with elastin. Elastase II with the chymotrypsin substrates and with elastin. Carboxypeptidase A with CN-Phe. Amylase with blue starch polymer.
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PMID:Identification and characterization of eight porcine pancreatic proteinases, carboxypeptidase A and amylase after electrophoretic separation using specific substrates. 244 43

The appearance and activity of various porcine pancreatic hydrolases were studied during fetal and postnatal development. Quantitatively, the enzyme activities in activated pancreas homogenates were low but increased during the second half of the fetal period, using the substrates Bz-Arg-pNA for measuring anodal and cathodal trypsin, Suc-Phe-pNA (chymotrypsin A and C, and elastase II) and Suc-(Ala)3-pNA (elastase I and protease E). Postnatally, after an initial decrease during the first week, the enzyme activities increased markedly, especially from 10-14 weeks to 6 months. The individual hydrolases were identified after electrophoretic separation in agarose gel and staining with various substrates either directly in the gel or after transfer to nitrocellulose membranes (enzymoblotting). During the fetal period, chymotrypsin A and B, elastase II, carboxypeptidase A, and amylase appeared at approximately 65 days and anodal trypsin, at approximately 76 days. After birth, new proteinases appeared after the first week including chymotrypsin C, cathodal trypsin, and protease E, whereas elastase I was found from 5 weeks after birth. Concomitantly, unidentified "fetal proteinase(s)" with caseinolytic, Ac-Phe-beta NE and CBZ-Ala-beta NE activities began to diminish and disappeared 10-14 weeks after birth. This study showed a marked increase in the overall pancreatic enzyme activities, as well as an age-dependent expression of the variety of pancreatic hydrolases during porcine ontogeny.
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PMID:Development of porcine pancreatic hydrolases and their isoenzymes from the fetal period to adulthood. 244 72

Serum elastase 1 has been evaluated in 115 patients with pancreatic and nonpancreatic gastrointestinal diseases and in 36 healthy controls. Increased serum elastase 1 values were found in all 27 patients with acute pancreatitis. If the diagnostic cutoff was established as the 2-fold increase above the upper normal range, sensitivity of elastase 1 (100%) was superior to pancreatic lipase (90%), immunoreactive trypsin (87%) and pancreatic amylase (78%). Specificity was 96% for elastase 1 at this cutoff. No distinction was possible between edematous and necrotizing acute pancreatitis on the basis of peak serum elastase 1 concentrations. Among 32 patients with chronic pancreatitis increased serum elastase 1 values were found in 22% and decreased values in 16% of patients, showing a striking parallelism to serum values of pancreatic lipase and immunoreactive trypsin. Specificity, established in controls and 49 patients with different gastrointestinal diseases, was 77% for elastase 1, 76% for immunoreactive trypsin, 83% for pancreatic lipase and 91% for pancreatic amylase. In addition, we investigated 21 patients with severe chronic renal diseases. In patients with renal insufficiency elastase was increased in 33%, comparable to the frequency of increased amylase and pancreatic amylase serum levels, whereas immunoreactive trypsin was increased in 95%. Immunoreactive trypsin showed a significant correlation to creatinin serum concentration, whereas the other enzymes did not.
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PMID:Serum elastase 1 in inflammatory pancreatic and gastrointestinal diseases and in renal insufficiency. A comparison with other serum pancreatic enzymes. 244 75


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