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)

Serum levels of immunoreactive trypsin (TIRS) were determined in 61 children having either alpha 1 antitrypsin deficit, chronic hepatitis, syndromic or non-syndromic ductular hypoplasia, or extrahepatic biliary atresia. Fasting TIRS values in both patients with chronic hepatitis (213 M 81 ng/ml) and with extrahepatic biliary atresia (159 +/- 88 ng/ml) didn't show statistically significant differences in relation to control values (172 +/- 44 ng/ml). However, in children with alpha 1-antitrypsin deficit (518 +/- 275 ng/ml; p less than 0.02) or syndromic (594 +/- 331 ng/ml; p less than 0.01) and non-syndromic ductular hypoplasia (558 +/- 183 ng/ml; p less than 0.02) TIRS levels were significantly above control values. Even more, in these last three groups of patients, their TIRS values were clearly greater than in extrahepatic biliary atresia patients. According to the above findings, we suggest that TIRS values may be a valuable marker for the differential diagnosis between intra and extrahepatic cholestasis.
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PMID:[Levels of serum immunoreactive trypsin in children with intra- and extrahepatic cholestasis]. 348 16

Trypsin activity and concentration of alpha 1-antitrypsin in amniotic fluid were measured in patients with and without premature rupture of membranes. Trypsin activity in amniotic fluid with premature rupture of membranes (127 +/- 57 U/L) was found to be significantly higher than in cases without premature rupture of membranes (14 +/- 20 U/L) (p less than 0.01). The concentration of alpha 1-antitrypsin in amniotic fluid with premature rupture of membranes (6.8 +/- 5.5 mg/dl) was significantly lower than in cases without premature rupture (25.2 +/- 20.2 mg/dl) (p less than 0.01). Trypsin activity and concentration of alpha 1-antitrypsin in amniotic fluid were not influenced by rupture of membranes and labor. These studies suggest that high trypsin activity and low concentration of alpha 1-antitrypsin in amniotic fluid is one cause of premature rupture of membranes.
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PMID:The relationship between trypsin activity in amniotic fluid and premature rupture of membranes. 349 Jul 88

Oxidant injury and release of proteolytic enzymes in prematures with respiratory distress syndrome (RDS), who are treated with ventilators and oxygen, have been postulated as possible causes of bronchopulmonary dysplasia (BPD). The premature may be at particular risk due to low levels of antiproteases, such as alpha-1-proteinase inhibitor (alpha 1PI), and antioxidants, such as ceruloplasmin (CER). Both alpha 1PI and CER deficiencies have been correlated with the severity of RDS. We studied serial alpha 1PI activity as measured by trypsin inhibitory capacity (TIC) and CER in the serum 27 prematures who required ventilator therapy for RDS. Serum TIC values for day 1 were significantly lower (0.34 vs. 0.92 mg inhibited/ml of sample) in the 13 patients who developed BPD compared to the 14 who did not. No significant differences were seen on succeeding days. No significant differences in CER were seen, although both groups had levels 33-50% of adult normals (11.3 vs 9.3 mg/dl). Other significant variables included birthweight (p less than 0.005), severity of RDS (p less than 0.03), and gestational age (p less than 0.03). One way analysis of variances demonstrated day 1 TIC to be the most significant variable (p less than 0.0001), followed by weight (p less than 0.007), severity RDS (p less than 0.04), and gestational age (p less than 0.03). CER levels were not a significant variable. A formula utilizing unstandardized canonical discriminant function including day 1 TIC, birthweight, severity of RDS, and gestational age was 100% sensitive and 85% specific in the prediction of BPD for the original study group. In an additional 25 consecutive admissions with severe RDS of whom 18 survived, the formula was 100% sensitive (6/6) and 75% specific (9/12).(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Serial trypsin inhibitory capacity and ceruloplasmin levels in prematures at risk for bronchopulmonary dysplasia. 349 55

One of the major lens-structural proteins, alpha-crystallin, is a multimeric protein containing 40 subunits of approx. 20 kDa each. There are two subunit types with distinct but similar structures. This protein was capable of inhibiting trypsin, chymotrypsin and elastase, but had no effect on thrombin or kallikrein. Complete inhibition was not observed, but rather plateau levels of inhibition were obtained in each case. Maximum inhibition was observed at a ratio of 1 mol of alpha-crystallin for every 9-10 mol of trypsin. alpha-Crystallin also inhibited the labeling of the active site of trypsin by [3H]diisopropyl fluorophosphate (DFP). Greater than 90% inhibition of DFP labeling was observed at a ratio of 1 mol of alpha-crystallin for every 7-8 mol of trypsin. Both trypsin and [3H]DFP-labeled trypsin formed a complex with alpha-crystallin, as demonstrated by gel-filtration chromatography. The active site of trypsin when bound to alpha-crystallin was still capable of reacting with p-nitrophenyl p-guanidobenzoate and soybean trypsin inhibitor, but was inaccessible to alpha 1-antitrypsin. These data suggest that alpha-crystallin acts as a multivalent modified inhibitor which is consistent with the proposed quaternary structure of alpha-crystallin.
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PMID:The binding and inhibition of trypsin by alpha-crystallin. 349 15

Developing neurons and Schwann cells have been shown to secrete proteases. The influence of these proteases on neurite outgrowth by cultured sensory ganglia was examined by adding specific protease inhibitors. Neonatal mouse dorsal root ganglia were cultured directly on tissue-culture plastic dishes in serum-free N2 medium with different protease inhibitors. Soybean trypsin inhibitor was found to double the extent of neurite outgrowth by 4 days in vitro. Ovomucoid trypsin inhibitor and leupeptin also increased neurite outgrowth, while alpha 1-antitrypsin, antipain and phenylmethylsulfonyl fluoride elicited a smaller effect. Furthermore, added trypsin or thrombin inhibited neurite outgrowth and the inhibition could be reversed by soybean trypsin inhibitor, while exogenous plasminogen or urokinase were inhibitory only at high concentrations. Thus neurite outgrowth probably requires a closely regulated system of protease secretion and protease inhibitor production.
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PMID:Effect of proteases and their inhibitors on neurite outgrowth from neonatal mouse sensory ganglia in culture. 354 23

Pure uterine fluid, obtained from 18 women in the luteal phase, was pooled and gel filtered. Inhibitory activity against trypsin, chymotrypsin and elastase was present in fractions containing alpha 2-macroglobulin, alpha 1-antitrypsin, alpha 1-antichymotrypsin and antileukoprotease. After solid-phase adsorption with antibodies to these inhibitors, no inhibitory activity remained. It was concluded that the entire inhibitory capacity of the proteinases studied was attributable to inhibitors derived from serum and antileukoprotease. These proteinase inhibitors which are present in uterine fluid during the luteal phase might be of significance during the implantation process.
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PMID:Inhibitors of trypsin, chymotrypsin and elastase in human uterine fluid. 363 50

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

The effects of alpha 1-antitrypsin (alpha 1-AT), alpha 1-acid glycoprotein (alpha 1-AGP), and haptoglobin (Hp), the main constituents of alpha-globulin and which belong to acute-phase proteins, on NK activity were examined using K562 cells as the NK target cells. Among the three proteins, alpha 1-AT and alpha 1-AGP had inhibitory effects on NK activity for "fast target" K562 cells. The alpha 1-AT preparations having the same protein concentration and a different trypsin inhibitory capacity (TIC) had an equal effect. Although alpha 1-AT and alpha 1-AGP equally reduced the NK activity, the mechanism involved in the reduction differed, in that the effect of alpha 1-AT directed toward NK cells reduced their binding capacity with the target cells. alpha 1-AGP probably interacts with a cytotoxic factor secreted from NK cells following effector-target interaction. These studies suggest that each of the acute-phase proteins, which increase following inflammation, inhibits NK cell function by two distinct mechanisms.
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PMID:Influence of acute-phase proteins on the activity of natural killer cells. 387 63

In six pigs intravenous administration of Escherichia coli endotoxin caused septic shock and a significant increase in serum cationic trypsin-like immunoreactivity (CTLI), with activation of cationic trypsinogen to trypsin and formation of complexes between cationic trypsin, on the one hand, and alpha 2-macroglobulin and alpha 1-antitrypsin, on the other, compatible with acute pancreatitis. In contrast, intraduodenal infusion of E. coli endotoxin to seven other pigs was without effect on the general circulation and on the serum CTLI.
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PMID:Effect of intravenous and intraduodenal administration of Escherichia coli endotoxin on the porcine pancreas as evaluated by changes in the serum cationic trypsin-like immunoreactivity. 389 Jan 37

All concentrated human fecal extracts tested formed precipitates in double immunodiffusion with goat antiserum to IgE, as well as with normal goat sera. However, no such precipitates were formed by fecal extracts and rabbit sera. IgE precipitates obtained with both goat and rabbit antisera to IgE showed reactions of non-identity with the former precipitates which seemed to represent complexes of trypsin or chymotrypsin in feces and an alpha-protein in goat sera. This alpha-protein, which was responsible for the non-immunoglobulin precipitations, was different from human alpha 1-antitrypsin. The trypsin-like components in feces had low molecular weights, and might represent degradation products of trypsin or chymotrypsin. After using a second labelled antiserum, precipitates between rabbit antiserum to IgE and extracts of feces could be visualized by means of autoradiography. They were seen in fecal extracts in which IgE could also be determined by a double-antibody paper radioimmunoassay technique (paper radio immunosorbent test; PRIST). Since the concentrations measured by a radioactive single-radial immunodiffusion method correlated to some extent with the PRIST concentrations, the latter precipitates were likely to represent IgE in feces.
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PMID:Detection of immunoglobulin E in feces by immunoprecipitation, and characterization of associated non-immunoglobulin precipitins. 391 41


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