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)

Endogenous gram-negative peritonitis leading to septic shock was induced in rats by a defined perforation of the coecum. Cationic trypsin-like immunoreactivity (CTLI) was measured in peritoneal fluid and serum by a radioimmunoassay method. Five, 10, and 15 h after the coecal perforation, CTLI in peritoneal fluid was significantly higher than before the coecal perforation and also higher than in the corresponding control rats. Moreover, CTLI in serum was under the same conditions significantly higher 10 and 15 h after the induction of peritonitis. Gel chromatography of peritoneal fluid and serum during peritonitis showed free CTLI and CTLI bound to both alpha-1-antitrypsin and alpha-2-macroglobulin, whereas only free CTLI could be detected in serum from control rats. These findings were accompanied by local ultrastructural changes in the acinar cells as evaluated by electron microscopy. The pathophysiologic implications of the findings are discussed.
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PMID:Impact of experimental endogenous gram-negative peritonitis on the pancreas of the rat as evaluated by cationic trypsin-like immunoreactivity in peritoneal fluid and serum and by electron microscopy of pancreatic tissue. 358

Solid and papillary epithelial neoplasms of the pancreas from six female patients were studied using immunohistochemistry and electron microscopy to define better their histogenesis. The tumors ranged in diameter from 5 to 15 cm (average: 9 cm), and, on cross section, most had areas of hemorrhage and necrosis, sometimes extensive. Microscopically, there was a solid and pseudopapillary pattern, with tumor cells typically having ovoid nuclei with delicate folding and indistinct nucleoli. Of note were the following: a relatively low mitotic rate (range: 0-6/20 hpf), the presence of hyaline globules (four of six cases), and collections of foam cells (three of six cases). Staining for cytoplasmic argyrophil granules was negative in each case. Ultrastructurally, the solid and papillary epithelial neoplasms of the pancreas showed evidence of acinar or ductular differentiation. Two contained zymogen granules, one had intermediate filaments (probably keratin), and three had abundant rough endoplasmic reticulum and mitochondria. Immunostaining was positive for chymotrypsin (six of six cases), trypsin (four of six), and amylase (three of six). None was positive for alpha-1-antitrypsin, neuron-specific enolase, pancreatic polypeptide, gastrin, glucagon, somatostatin, or insulin. The findings support an origin from exocrine pancreas, and follow-up indicates a low rate of malignancy, with local recurrence in two of the six patients.
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PMID:Solid and papillary epithelial neoplasm of the pancreas. An ultrastructural and immunocytochemical study of six cases. 381 76

A biologically active neutral peptide mediator is cleaved from a plasma protein substrate by an alpha-1-antitrypsin-inhibitable serine protease apparently residing on the membrane of the human neutrophil. The peptide mediator has an approximate mol wt of 1,000, and is distinguished from the kinin peptides by a neutral isoelectric point, susceptibility to inactivation by trypsin as well as chymotrypsin and activity on the isolated, atropinized, and antihistamine-treated guinea pig ileum with relatively little action on the estrous rat uterus. The neutrophil protease is fully inhibitable by DFP, trypsin inhibitors from lima or soy bean, and alpha-1-antitrypsin and is associated with the high mol wt fragments of the neutrophil and not the nuclear, lysosomal, or cytoplasmic subcellular fraction. The substrate has an approximate mol wt of 90,000 and is chromatographically separable from kininogen. The exquisite sensitivity of the neutrophil protease to alpha-1-antitrypsin was established both by inhibition with highly purified alpha-1-antitrypsin and by the inability of the protease to generate detectable neutral peptide in a homozygous (ZZ) alpha-1-antitrypsin-deficient patient without heat inactivation of the residual inhibitor. On the other hand, plasma from a (null) alpha-1-antitrypsin-deficient patient supported neutral peptide generation and revealed an additional factor which inactivated neutral peptide.
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PMID:A neutrophil-dependent pathway for the generation of a neutral peptide mediator: partial characterization of components and control by alpha-1-antitrypsin. 454 25

Serum trypsin, total trypsin-inhibitor capacity, alpha-1-antitrypsin and alpha-2-macroglobulin were analyzed daily in ten patients hospitalized as a result of acute pancreatitis. Markedly raised serum trypsin concentrations were found in all patients. Alpha-1-antitrypsin and the trypsin-inhibitor capacity were also significantly increased as compared to post-illness values, but alpha-2-macroglobulin tended to decrease during acute pancreatitis. The post-illness values of all these parameters were in the normal range. It is concluded that a deficiency of alpha-1-antitrypsin, trypsin-inhibitor capacity of alpha-2-macroglobulin is not present in patients with acute pancreatitis which could render the pancreas more vulnerable to its own proteases. During acute pancreatitis trypsin is released into the circulation, but it is effectively inactivated by serum protease inhibitors, mainly alpha-1-antitrypsin, which can be seen as an increased trypsin-inhibitor capacity in these patients. The use of protease inhibitors in the treatment of acute pancreatitis seems to be unnecessary against this background. Increased serum trypsin values can be used when confirming the diagnosis of acute pancreatitis.
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PMID:Serum immunoreactive trypsin and trypsin inhibitors during acute pancreatitis. 616 88

Proteolytic enzyme inhibitor activity has been measured in the rheumatoid knee by 2 different techniques. The inactivation rate of trypsin injected into the joint in 13 patients was compared with synovial fluid levels of alpha-1-antitrypsin (apha 1AT), alpha-2-macroglobulin (alpha 2M) and trypsin inhibitory capacity (TIC). The lack of correlation and the fact that an inverse relationship was shown between the T1/2 to inactivation and joint damage suggests that additional mechanisms are involved in the inactivation of destructive enzymes. Serum levels of alpha 1AT and TIC were elevated in 36 rheumatoid arthritis (RA) patients when compared with control values and RA synovial fluid inhibitor levels elevated by comparison with osteoarthritic figures. The synovial fluid alpha 1AT and TIC correlated with the activity of the lysosomal enzyme beta-acetyl glucosaminidase (beta AGA) but only trace amount of neutral protease activity was detected probably because of the large concentration of inhibitors present. The deficient Pi phenotype MZ was rarely encountered.
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PMID:Antitrypsin activity and enzyme inhibitors in the rheumatoid joint. 617 Jul 54

The sera of human, cattle, horse, sheep, goat, pig, dog, rabbit, guinea pig, rat, hamster, and mouse were assayed for total trypsin-inhibiting capacity, and for concentrations of alpha-1-antitrypsin and alpha-macroglobulin. The rodents examined showed striking species differences: the alpha-1-antitrypsin levels of mouse, rat, and guinea pig were more than twice the human level, while the alpha-macroglobulin levels of hamster and guinea pig were 340 and 40%, respectively, of the human level. On the other hand, little variations were found among the large domestic animals, their levels of the two inhibitors being similar to those of the human.
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PMID:Comparative studies on the serum levels of alpha-1-antitrypsin and alpha-macroglobulin in several mammals. 619 Feb 64

The demembranation and reactivation of ejaculated rabbit spermatozoa have been studied. ATP, Mg, glutamate, dithiothreitol (DTT), and Tris-HCl were found to be essential for a good reactivation. With this experimental model, we investigated the effects of protease inhibitors on the reinitiation of movement by ATP and on the movement of already motile spermatozoa. Soybean trypsin inhibitor (STI) prolonged the length of reactivation by 7- to 8-fold, whereas pepstatin, antithrombin III, phenylmethylsulfonyl fluoride (PMSF), and alpha-1-antitrypsin had no significant effect. Aprotinin (1.5 micrograms/ml) and leupeptin (50 micrograms/ml) completely prevented the reinitiation of movement by ATP; aprotinin at the same concentration even blocked the movement of motile spermatozoa. A tissue-specific seminal plasma factor could also prevent both the reinitiation of movement and the movement of motile spermatozoa. However, it took 2-3 times the amount of seminal plasma to stop the movement than to prevent the reinitiation of movement. The inhibitor in the seminal plasma is most probably not a protease or an aprotinin-like protease inhibitor since a partially purified preparation of the seminal plasma inhibitor does not hydrolyze a trypsin substrate, is not inhibited by protease inhibitors and has no significant capacity to inhibit trypsin. The data suggest that aprotinin and the seminal plasma inhibitor block movement through different mechanisms. Aprotinin and the seminal plasma inhibitor represent two new tools to study the regulation of sperm movement.
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PMID:Aprotinin and a seminal plasma factor inhibit the motility of demembranated reactivated rabbit spermatozoa. 619 May 16

Three blood protease inhibitors were immunochemically quantitated in normo- and hypertensive subjects divided according to their plasma renin activity. As inflammatory reactions could be suspected in many subjects, the inflammatory state was estimated on the basis of three acute phase reactants and allowed one to conclude that total inter-alpha-trypsin-inhibitor and inter-alpha-trypsin-inhibitor derivative, as well as alpha-1-antitrypsin levels were increased in inflammation. Involvement of either protease inhibitor tested in the control of plasma renin activity is unlikely as no relationship between plasma renin activity and protease inhibitor levels could be demonstrated in non-inflammatory conditions. Finally, there was no particular distribution of alpha-1-antitrypsin (PI) phenotypes in the overall population.
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PMID:Quantitative study of human blood alpha-1-antitrypsin, alpha-2-macroglobulin and inter-alpha-trypsin-inhibitor with respect to plasma renin activity. 619 11

Various strains of black-pigmented Bacteroides species were grown on horse blood agar and suspended in human serum. After various times of incubation the effect of the bacteria on the serum was evaluated by polyacrylamide gel electrophoresis and "rocket" immunoelectrophoresis. The formation of trichloroacetic acid-soluble material in the suspensions and the capacity of the treated sera to inhibit the activity of trypsin were also determined. The two tested strains of Bacteroides gingivalis (W83, H185) degraded most serum proteins, including the plasma proteinase inhibitors alpha-1-antitrypsin and alpha-2-macroglobulin. They did not, however, degrade alpha-1-antichymotrypsin. Bacteroides intermedius NCTC 9336, Bacteroides asaccharolyticus NCTC 9337, and an asaccharolytic oral strain different from B. gingivalis (BN11a-f) did not degrade the plasma proteinase inhibitors. These strains were, however, able to inactivate the capacity of serum to inhibit the activity of trypsin.
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PMID:Degradation of the human proteinase inhibitors alpha-1-antitrypsin and alpha-2-macroglobulin by Bacteroides gingivalis. 619 82

Contrapsin and alpha-1-antitrypsin have been recently characterized as major protease inhibitors in mouse plasma (Takahara, H. & Sinohara, H. (1982) J. Biol. Chem. 257, 2438-2446). We have studied the effects of the two inhibitors upon various serine proteases prepared from mouse tissues. Trypsin, plasmin and trypsin-like proteases of the submaxillary gland were inhibited by contrapsin but not by alpha-1-antitrypsin. On the other hand, chymotrypsin, elastase, and thrombin were inactivated by alpha-1-antitrypsin but not by contrapsin. Thus, their inhibitory spectra did not overlap each other in spite of their broad specificities. The inhibition of trypsin, chymotrypsin, and elastase was rapid and stoichiometric, whereas the inhibition of the other proteases was relatively slow. Contrapsin accounted for almost the total capacities of mouse plasma to inhibit both trypsin and submaxillary gland trypsin-like proteases, whereas alpha-1-antitrypsin was responsible for nearly all the capacities of plasma to inhibit both chymotrypsin and elastase.
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PMID:Inhibitory spectrum of mouse contrapsin and alpha-1-antitrypsin against mouse serine proteases. 622 76


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