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)

GHR-P63 ('growth hormone-regulated protein of 63,000 daltons') is an acidic glycoprotein secreted by rat hepatocytes whose synthesis is abolished upon hypophysectomy. The sequence of its mRNA including the entire coding and 3' untranslated regions was determined from a nearly full-length lambda gt11-cDNA clone. The sequence contained two ATGs in frame giving rise to two overlapping coding regions which could encode precursor polypeptides of 416 and 406 amino acid residues (MrS = 46549 and 45371). These potential translation initiation codons appeared to be functional both in vitro and in intact cells since two precursors of the correct size were immunoprecipitated as products of mRNA translation. The unglycosylated precursors were converted into intermediate intracellular forms of about 56,000 daltons containing N-linked oligosaccharide side chains and thereafter into the secretory form of approximately equal to 63,000 daltons. Strong sequence homologies, both at the nucleotide and the amino acid levels were found between GHR-P63 and several serum protease inhibitors, more particularly mouse contrapsin and human alpha 1-antichymotrypsin. In agreement with sequence data, GHR-P63 purified from rat blood by affinity chromatography was found to carry an anti-trypsin activity. GHR-P63 mRNA, virtually undetectable in hepatocytes from hypophysectomized rats, could be hormonally re-induced to subnormal levels both in vivo by treating animals with hormones and in vitro by incubating the defective cells with hormones. Growth hormone was absolutely required but had a weak effect when used alone. Glucocorticoids which had no effect per se, strongly potentiated the action of growth hormone. Nuclear run-off experiments suggest that hormones regulated GHR-P63 mRNA levels by acting mostly, if not exclusively, on gene transcription.
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PMID:Study of a growth hormone-regulated protein secreted by rat hepatocytes: cDNA cloning, anti-protease activity and regulation of its synthesis by various hormones. 244 Jun 72

Proteolytic enzymes were tested for improving histochemical localization of tissue antigens. Sections, 2-4 micron in thickness, were prepared on sodium-silicate coated slides from formalin-fixed, paraffin-embedded human biopsies. A modification of the Sternberger technique (PAP) and the indirect immunofluorescence method were used for the localization of 15 various antigens: heavy chain immunoglobulins, light chain immunoglobulins, alpha 1-fetoprotein, alpha 1-antichymotrypsin, myoglobin, fibronectin, factor VIII (ass. ag), fibrinogen, lysozyme and cytokeratin. The ability of different proteolytic enzymes (trypsin, pronase, pepsin) to unmask antigen in formalin-fixed sections were tested by variation of concentration, incubation time, temperature and pH. Although proteolytic unmasking to some extent is reliable, good restoration of antigenicity is not always possible. Best results were obtained with pronase E (Serva, FRG).
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PMID:[The proteolytic pretreatment of formalin-fixed tissue in immunohistochemical diagnosis]. 245 12

Extrapancreatic findings at computed tomography (CT), performed within 24 h in 42 consecutive episodes of acute pancreatitis, were classified according to a scoring system (EP score) and were correlated to Ranson's prognostic signs, to duration of hospital stay, biochemical changes in plasma and pancreatic ischaemia found at CT with contrast enhancement. Increasing EP score was found to be related to increasing number of positive Ranson's signs, longer hospital stay and pancreatic ischaemia. Plasma levels of immunoreactive cationic trypsin and amylase were not proportional to EP score. alpha 1-protease inhibitor, antichymotrypsin but not immunoreactive pancreatic secretory trypsin inhibitor increased proportionally to EP score. No changes related to EP score were seen in alpha 2-macroglobulin levels. Serum levels of trypsin-alpha 1-protease inhibitor complex were maximal after 3 days and most pronounced in cases with high EP scores. Plasma levels of factor X, alpha 2-antiplasmin and C1-esterase inhibitor were found to be inversely proportional to EP score.
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PMID:Pathobiochemistry and early CT findings in acute pancreatitis. 248 91

Two new human cell lines, RCM-1 and CoCM-1, have been established from primary colorectal adenocarcinomas. Both cell lines were unique in that the cultures secreted trypsin inhibitors in vitro. The activities of these inhibitors were accumulated in serum-free media of both cell lines over a period of several days. Two inhibitors (PI-1 and PI-2) were isolated from serum-free conditioned medium in which RCM-1 was grown by anion-exchange and gel filtration high-performance liquid chromatography. PI-1 inhibited trypsin and chymotrypsin strongly, and pancreatic elastase weakly. Its molecular weight was about 57 kilodaltons (Kd) as determined by gel filtration chromatography. It cross-reacted with the antiserum elicited against human alpha 1-antitrypsin in double immunodiffusion. PI-1 corresponding to alpha 1-antitrypsin was also demonstrated immunohistochemically in both cell lines. PI-2 inhibited trypsin strongly, and chymotrypsin, kallikrein and plasmin weakly. It had higher molecular weight (200-300 Kd) than that of PI-1, and did not cross-react with antisera against human alpha 1-antitrypsin, alpha 2-macroglobulin, alpha 1-antichymotrypsin, alpha 2-plasmin inhibitor, inter-alpha-trypsin inhibitor and urinary trypsin inhibitor. RCM-1 and CoCM-1 are the first colorectal adenocarcinoma cell lines that secrete functionally active trypsin inhibitors, including alpha 1-antitrypsin in vitro, and are useful for the study of tumor-cell derived proteinase inhibitors.
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PMID:New human colorectal carcinoma cell lines that secrete proteinase inhibitors in vitro. 257 Apr 82

We measured the concentrations of trypsin, elastase, and three anti-proteases-alpha 1-macroglobulin, alpha 1-antitrypsin, and alpha 1-antichymotrypsin-in serum from 10 patients with pancreatic carcinoma. All 10 showed increased elastase and decreased alpha 2-macroglobulin concentrations, nine had increased alpha 1-antichymotrypsin, and eight had increases in alpha 1-antitrypsin and trypsin. Serial studies during chemotherapy of one patient showed that the protease concentrations decreased during treatment but the concentrations of the anti-proteases remained abnormal.
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PMID:Concentrations of protease and anti-protease in serum of patients with pancreatic cancer. 258 24

We have isolated three cDNA clones for human alpha 2-plasmin inhibitor (alpha 2-PI). Two clones are from human hepatoma cell line, Hep G2, and cover the entire protein coding region plus the 3'-flanking region up to the poly(A) sequence, and the other clone is from human liver and contains the carboxyl-terminal half. The total length of the cDNAs is 2.29 kb, corresponding to more than 95% of the full-length mRNA. alpha 2-PI seems to consist of 452 amino acid residues plus 39 amino acid residues for the signal peptide. The amino acid sequence shows 23 to 28% homology to those of five other protease inhibitors, plasminogen activator inhibitor (PAI), protein C inhibitor (PCI), alpha 1-antitrypsin (alpha 1-AT), antithrombin III (AT III), and alpha 1-antichymotrypsin (alpha 1-AC). alpha 2-PI seems to be the most distantly related among these inhibitors. Comparison of the phylogenetic trees of proteases and their inhibitors indicates that four proteases, namely elastase (or trypsin), chymotrypsin, plasminogen activator, and thrombin, may have evolved concurrently with the corresponding inhibitors. However, alpha 2-PI and PCI seem to have evolved asynchronously from their substrates. The data suggest that alpha 2-PI may originally have inhibited some protease other than plasmin, and protein C may have had an inhibitor different from the present one early in its evolutionary history.
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PMID:Structure of human alpha 2-plasmin inhibitor deduced from the cDNA sequence. 283 Feb 48

In our previous research, we found that the level of the plasminogen activity in the plasma from Duchenne-type patients with progressive muscular dystrophy was higher than of the normal boys, though the level of the plasmin inhibitors was lower. Therefore, in the present study, we investigated the differences in the fractions of plasmin inhibitors. The subjects were nine patients (the average age being 17.1 years) who had been diagnosed, by clinical and biochemical tests, as having PMD; serving as controls were normal boys (the average age being 15 years), the patients' mothers, and the mothers of the normal boys. The plasmin inhibitors were separated from plasma using lysine-Sepharose columns according to the method of Urita et al. The determination was performed based on the method of Aoyagi et al. and an immunoreactive assay. The results were as follows: (1) No significant differences were seen between patients with PMD and control subjects with respect to either alpha 1-antichymotrypsin, antithrombin III, and alpha 1-antitrypsin or alpha 2-macroglobulin and inter-alpha-trypsin inhibitors. These results suggested that the low level of plasmin inhibitors in patients was due to the low activity of the C1 inactivator. (2) The patients with PMD showed lower values than the normal boys in the levels of C1 inactivator in plasma; similarly, the mothers of these patients showed lower values than the normal mothers.
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PMID:Plasma plasmin inhibitors in Duchenne-type progressive muscular dystrophy. 316 Mar 43

We have found that degranulation from mast cells is specifically inhibited by the inhibitors of chymase (10). Among the natural serine protease inhibitors tested, Bowman-Birk soybean protease inhibitor, Eglin C, and human alpha 1-antichymotrypsin inhibited chymase more strongly than did chymostatin, Kunitz soybean protease inhibitor, and phosphatidylserine. Of the inhibitors tested, Bowman-Birk soybean protease inhibitor was the strongest inhibitor of chymase, its Ki value being 13.2 X 10(-9) M. Kinetic studies showed that these inhibitors were all noncompetitive inhibitors of chymase. Bowman-Birk and Kunitz soybean protease inhibitors inhibited both chymotrypsin-type and trypsin-type serine proteases but Eglin C specifically inhibited chymotrypsin-type proteases.
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PMID:Kinetic studies on the inhibitions of mast cell chymase by natural serine protease inhibitors: indications for potential biological functions of these inhibitors. 347 19

Highly purified functional cytotrophoblasts have been prepared from human term placentae by adding a Percoll gradient centrifugation step to a standard trypsin-DNase dispersion method. The isolated mononuclear trophoblasts averaged 10 microns in diameter, with occasional cells measuring up to 20-30 microns. Viability was greater than 90%. Transmission electron microscopy revealed that the cells had fine structural features typical of trophoblasts. In contrast to syncytial trophoblasts of intact term placentae, these cells did not stain for hCG, human placental lactogen, pregnancy-specific beta 1-glycoprotein or low mol wt cytokeratins by immunoperoxidase methods. Endothelial cells, fibroblasts, or macrophages did not contaminate the purified cytotrophoblasts, as evidenced by the lack of immunoperoxidase staining with antibodies against vimentin or alpha 1-antichymotrypsin. The cells produced progesterone (1 ng/10(6) cells . 4 h), and progesterone synthesis was stimulated up to 8-fold in the presence of 25-hydroxycholesterol (20 micrograms/ml). They also produced estrogens (1360 pg/10(6) cells . 4 h) when supplied with androstenedione (1 ng/ml) as a precursor. When placed in culture, the cytotrophoblasts consistently formed aggregates, which subsequently transformed into syncytia within 24-48 h after plating. Time lapse cinematography revealed that this process occurred by cell fusion. The presumptive syncytial groups were proven to be true syncytia by microinjection of fluorescently labeled alpha-actinin, which diffused completely throughout the syncytial cytoplasm within 30 min. Immunoperoxidase staining of cultured trophoblasts between 3.5 and 72 h after plating revealed a progressive increase in cytoplasmic pregnancy-specific beta 1-glycoprotein, hCG, and human placental lactogen concomitant with increasing numbers of aggregates and syncytia. At all time points examined, occasional single cells positive for these markers were identified. RIA of the spent culture media for hCG revealed a significant increase in secreted hCG, paralleling the increase in hCG-positive cells and syncytia identified by immunoperoxidase methods. We conclude that human cytotrophoblasts differentiate in culture and fuse to form functional syncytiotrophoblasts.
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PMID:Purification, characterization, and in vitro differentiation of cytotrophoblasts from human term placentae. 351 58

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


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