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)

Serial measurements of circulating antiproteases were carried out on 42 consecutive patients admitted with acute pancreatitis. In the 7 days following admission the serum levels of alpha 1 antitrypsin (alpha 1 AT), alpha 1 antichymotrypsin (alpha 1 ACT) and the trypsin inhibitory capacity (TIC) increased by more than 300 per cent. The serum concentration of alpha 2 macroglobulin (alpha 2 M) alone showed a decline which was most profound in those patients with severe acute pancreatitis. Initial experience of fresh frozen plasma as a source of extrinsic antiproteases in severe acute pancreatitis is that it fails to prevent the decline in alpha 2 M or increase the already elevated TIC of the patients' serum.
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PMID:Antiprotease capacity in acute pancreatitis. 376 47

Elevated levels of immunoreactive pancreatic secretory trypsin inhibitor (PSTI) were found in serum from patients with perforated duodenal ulcer, bacterial peritonitis, urosepticemia, pneumonia, acute renal failure, and also after different surgical procedures. The extent of the trauma seemed to determine the maximal level of PSTI. The increase found paralleled the changes seen in the acute-phase protein antichymotrypsin. There was, however, almost no increase in trypsinogen, thought to be produced together with PSTI in the acinar cells of the pancreas. In conclusion, there is evidence that PSTI is probably also produced somewhere outside the pancreas, in agreement with recent immunohistochemical data. This production may be part of a general acute-phase reaction. Thus, PSTI may have a more general inhibitory function against trypsin-like protease release in tissue injury, instead of being a purely local trypsin inhibitor in the pancreatic gland.
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PMID:Elevated pancreatic secretory trypsin inhibitor levels during severe inflammatory disease, renal insufficiency, and after various surgical procedures. 381 2

A trypsin inhibitor was extracted from the kale seeds with 0.01 M-HCl, precipitated with ammonium sulphate, and purified by affinity chromatography on immobilized trypsin and ion-exchange chromatography on QAE-Sephadex A-25. The inhibitor, of Mr 8 000, is composed of 64 amino acid residues and contains neither threonine nor methionine. Its isoelectric point is 8.9. In addition to trypsin, the inhibitor acts on subtilopeptidase A and shows a very weak antichymotrypsin activity. The factors modifying the arginine residues inactivate the inhibitor. A modified form of the inhibitor (with a broken reactive site peptide bond) has been isolated in pure form, and its properties were compared with those of the virgin form.
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PMID:Isolation and partial characterization of the trypsin inhibitor from the seeds of Brassica oleracea var. sabellica. 383 4

Concentration of alpha 1-antitrypsin (alpha 1-AT), alpha 1-antichymotrypsin (alpha 1-AChyT), inter-alpha-trypsin inhibitor (I-alpha-I), and alpha 2-macroglobulin (alpha 2-M) was measured in 27 serous middle ear effusions (MEEs) from 24 adult patients. The presence of protease-inhibitor complex was analyzed by crossed immunoelectrophoresis (CIEP). Mean concentration of alpha 1-AT was 361 +/- 90.0 mg/dl and was higher than that of other inhibitors: alpha 1-AChyT, 80.6 +/- 40.7; I-alpha-I, 21.3 +/- 21.5; alpha 2-M, 59.5 +/- 57.1. Molar concentration of alpha 2-M was the lowest. Most of alpha 1-AT and alpha 1-AChyT in MEEs were unsaturated; free inhibitors. Alpha-1-AT could be saturated by trypsin and elastase immediately, and only alpha 2-M could be saturated by papain (classical thiol protease). Serous MEEs have high anti-trypsin activity attributed to mainly free alpha 1-AT. Since level of alpha 2-M was very low, lysosomal thiol proteases could be one of the major proteases inducing proteolytic damage to middle ear mucosa.
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PMID:The significance of protease inhibitors in the pathogenesis of otitis media with effusion. 383 90

Human heparin cofactor II is a plasma protein that is known to inhibit thrombin. The rate of thrombin inhibition by heparin cofactor II is accelerated (greater than or equal to 1000-fold) in the presence of the glycosaminoglycans, heparin and dermatan sulfate. We have found that chymotrypsin A alpha is also inhibited by heparin cofactor II with a second-order rate constant value of 1.8 X 10(6) M-1 X min-1 at pH 8.0 and 25 degrees C. However, there was no measurable effect of heparin or dermatan sulfate on the rate of chymotrypsin inhibition. Arginine-modified heparin cofactor II showed a comparable percentage loss of both antichymotrypsin and antithrombin activities. Heparin cofactor II and chymotrypsin formed a stable complex with a Mr value near 90,000 when analyzed by NaDodSO4/polyacrylamide gel electrophoresis; this suggests a 1:1 reaction stoichiometry. The chymotrypsin cleavage site in heparin cofactor II was the same as that for thrombin, and primary structure analysis of the inhibitor showed a P'1-P'8 sequence of Ser-Thr-Gln-Val-Arg-Phe-Thr-Val ... . The results indicate that, in contrast to alpha 1-antichymotrypsin, which does not inhibit trypsin-like enzymes, including thrombin, heparin cofactor II can effectively inhibit both thrombin and chymotrypsin.
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PMID:Inhibition of chymotrypsin by heparin cofactor II. 386 4

Cysteine protease inhibitors that specifically reacted with several cysteine proteases were found in KSCN extract of human melanoma tissue. From 30 gm of the tissue, approximately 593.5 U inhibitor was obtained. The inhibitors were adsorbed on a papain-Sepharose column and could be eluted with 10 mmol/L phosphate buffer, pH 6.0, containing NaCl or KCl, or with 20 mmol/L acetate buffer, pH 4.0, containing KSCN. They revealed a strong inhibitory activity for cysteine proteases such as ficin, papain, and cathepsin B, but did not react with cysteine protease bromelain or serine protease trypsin. No immunologic relationship was confirmed between the inhibitor and other well-known plasma inhibitors such as alpha 1-antitrypsin, alpha 2-macroglobulin, alpha 1-antichymotrypsin, antithrombin III, C1-in-activator, and alpha 2-plasmin inhibitor. With Sephadex G-100, two main peaks of molecular weight 40,000 and 10,000 were detected in the KSCN extract of the human melanoma tissue. However, the inhibitors revealed three molecular weights of 10,000, 25,000, and 80,000 when estimated by Sephadex G-100 gel filtration after papain-Sepharose affinity chromatography. On the other hand, the molecular weights of the inhibitors changed to two peaks of 25,000 and 10,000 on rechromatography with a papain-Sepharose column.
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PMID:Cysteine protease inhibitors isolated from human malignant melanoma tissue. 393 99

A clinical and biochemical analysis of 27 attacks of acute pancreatitis was made throughout the course of the disease. In severe attacks alpha 2-macroglobulin (alpha 2-M) decreased during the first days, reaching values in blood below 40% of the normal value. In addition, this remaining alpha 2-M had a decreased trypsin-binding capacity, indicating circulating alpha 2-M protease complexes. The inter-alpha-trypsin inhibitor concentration was also decreased, whereas alpha 1-proteinase inhibitor, antichymotrypsin, and pancreatic secretory trypsin inhibitor increased. All changes were most pronounced in the peritoneal fluid and were also closely correlated to the severity of the disease, assessed by both Ranson's and McMahon's classification systems. All patients with clinical complications had profound biochemical changes. In accordance with earlier findings, activation of both the complement and kinin systems seems possible in both blood and peritoneal fluid at the low alpha 2-M concentrations found in severe attacks.
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PMID:Protease inhibitors in acute human pancreatitis. Correlation between biochemical changes and clinical course. 608 96

alpha 2-macroglobulin is probably the most important of the antiproteases in plasma. In this study, the relationships of plasma alpha 2-macroglobulin to the clinical features of acute pancreatitis as well as to plasma levels of other antiproteases, immunoglobulins, and immunoreactive trypsin, were investigated in 55 patients with acute pancreatitis. The mean level of alpha 2-macroglobulin in 395 plasma samples from the patients was 2.12 g/liter compared with 2.41 g/liter in 29 healthy subjects and 2.93 g/liter in 17 patients with septicemia. Plasma levels were lower in 12 patients with severe pancreatitis than in 43 with mild attacks, and the lowest levels in three fatal attacks were less than half the mean of the normal range. Lowest levels were recorded at a mean time of 3 days after admission in the patients with mild attacks, at 5 days after admission in the patients with severe attacks, and 9 days after admission in those with fatal attacks. In contrast, plasma levels of the alpha 1-proteinase inhibitor antichymotrypsin and C-reactive protein increased to above normal levels during the attack, significantly more so in severe compared with mild attacks. Plasma levels of IgA, IgG, and IgM remained within the normal range or were increased. In patients with severe pancreatitis, plasma levels of immunoreactive trypsin remained elevated for longer than in those with mild attacks although there was little initial difference in the levels. These data suggest that decreasing levels of alpha 2-macroglobulin during the course of acute pancreatitis are due to a specific mechanism and unrelated, for the most part, to any generalized effect of pancreatitis on protein synthesis. The formation of rapidly cleared complexes between alpha 2-macroglobulin and active proteases is the most tenable explanation for the depletion of plasma levels, but the clinical significance of the changes remains unclear.
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PMID:Relation of alpha 2-macroglobulin and other antiproteases to the clinical features of acute pancreatitis. 619 93

Blood serum separation by the method of gel filtration on Sephadex G-200 with the subsequent immunochemical determination of the quantitative content of basic proteolysis inhibitors permitted isolating the alpha 2-macroglobulin fraction while alpha 1-antitrypsin and alpha 1-antichymotrypsin separation was a failure. The immunochemical analysis of the antienzymic activity of the isolated inhibitors showed that 32.3 +/- 3.5% of the introduced kallikrein, 18.7 +/- 0.6% of trypsin and 14.4 +/- 4.1% of chymotrypsin were bound in the zone of alpha 2-macroglobulin. The rest of antienzymic activity was localized in the zone of alpha 1-antitrypsin and alpha 1-antichymotrypsin. After a preliminary saturation of blood serum with trypsin in the amount equivalent to its antitryptic capacity (200 micrograms/ml) the ability of alpha 2-macroglobulin to bind kallikrein and chymotrypsin lowers considerably (by 69 and 72%, respectively). In the zone of alpha 1-antitrypsin and alpha 1-antichymotrypsin a decrease in the ability to bind kallikrein and chymotrypsin amounted to 44 and 12% respectively. Thus, alpha 2-macroglobulin being bound with trypsin looses considerably its ability to bind other enzymes.
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PMID:[Antiproteinase activity of alpha 2-macroglobulin]. 620 37

An acid-stable protease inhibitor (AS-PI) has been previously demonstrated in ascitic fluid from patients with ovarian carcinoma. In this study, the AS-PI was further purified using DEAE-cellulose and isoelectric focusing (IEF), and a partial characterization was undertaken. On DEAE-cellulose ion-exchange column chromatography, AS-PI activity was observed in both adsorbed and non-adsorbed fractions. The former represented the main AS-PI peak. By IEF, the respective pI values were 1.6 and 4.5. By gel filtration, the molecular weight of the main (adsorbed fraction) AS-PI was 78 000. This AS-PI strongly inhibited trypsin and to a lesser extent chymotrypsin, but exerted no inhibitory effect on plasmin. It slightly inhibited SH proteases such as papain and ficin. Immunologically, AS-PI was distinct from alpha 1-antitrypsin, alpha 1-antichymotrypsin, inter-alpha-trypsin inhibitor, antithrombin III, C1-inactivator, alpha 2-macroglobulin and alpha 2-plasmin inhibitor. The main AS-PI reacted with and was neutralized by antiurinary trypsin inhibitor serum, and on immunoelectrophoresis, had a mobility slightly cathodal to serum albumin.
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PMID:Further purification and characterization of acid-stable protease inhibitor from ascites of an ovarian carcinoma patient. 643 8


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