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 proteolytic enzymes contained in the preparation from Streptomyces 771 have been separated by isoelectric focusing in the sucrose density gradient at pH 3-10. The following enzymes have been identified: three multiple forms of neutral metal proteinase (pI 5.1, 6.37, 7.8) each of which splits DNP-Gly-Gly decreases-Val-ArgOMe; elastase-like metal proteinase active with respect to RBB-elestin with pI 10.68; metal-dependent peptidases: leucin aminopeptidase active with respect to L-RBB-elastin with pI 10.68 metal-dependent peptidases: leucin aminopeptidase active with respect to L-leucin n-nitroanilide and L-leucin beta-naphtylamide with pI 7.65, 7.15, 6.67, 6.45, 5.7, 5.35, 5.22, 4.83; carboxy peptidase with pI 5.95, 6.37; serine metal-dependent subtilisin-like proteinase active with respect to 2-Ala-Ala-LeupNA, 2-Gly-Gly-LeupNA, 2-Ala-LeupNA; two multiple forms of serine trypsin-like proteinase active with respect to BAEE and BApNA with pI 4.35, 4.76; serine chymotrypsin-like proteinase with pI 8.68 active with respect to ATEE.
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PMID:[Isoelectric focusing of a preparation of proteolytic enzymes from Streptomyces 771]. 634 61

A cylindrical segment, free of complex atherosclerotic lesions, was resected at autopsy from each of 59 descending human thoracic aortas by cutting just below the level of the first pair of intercostal arteries and 35 mm distal to this incision. Each isolated tunica media was defatted and subjected to successive treatment with EDTA-Tris, 5 M guanidine hydrochloride-Tris, 5 M guanidine hydrochloride-Tris-DTE, collagenase and either trypsin or hot alkali. After each extraction or digestion, the dimensions and weight of the segments were measured and the extracted materials were analyzed and quantitated. This allowed the total content of the various components of the tunica media to be assessed by both gravimetric and analytical means. An age-related rise was observed in the total content of the following components: proteins and glycoproteins soluble in chaotropic solvents (ranging from 24 mg/cm in the youngest samples to 46 mg/cm in the oldest) and collagen (38 mg/cm to 69 mg/cm). In contrast, the total content of elastin remained constant at 70 mg/cm at all ages, but its concentration decreased due to the rise in the concentration of the other tissue components as the tunica media thickened with age. It was also noted that with increasing age there was an accumulation of protein(s) which could not be solubilized by extraction with chaotropic agents or with collagenase, but which could be removed by treatment with either trypsin or hot alkali. Mechanical measurements conducted before and after trypsin digestion on samples previously subjected to purification with the first four agents used suggest that this accumulated protein(s) influenced the elastic response of the tissue to the applied stress by increasing the incremental modulus, the breaking stress, and the hysteresis. After the removal of this additional protein(s), the mechanical behavior of the elastin component was found to be identical in all samples, irrespective of age. It is therefore proposed that the morphological changes and the stiffening observed in the aging aortic wall are not due to degradation of its elastin network but to variations in the supramolecular organization of connective tissue components.
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PMID:Age-related changes in composition and mechanical properties of the tunica media of the upper thoracic human aorta. 682 97

The isolated chymotrypsin-like protease of rat mast cells was shown to cause an increase of vascular permeability in rat skin. Inactivation of the enzymatic activity of the cationic protease abolished the vasoactivity. The smallest effective dose of the maximally active enzyme was estimated to be 0.5 micrograms per injection site, which is less than the amount of the endogenous mast cell enzyme in areas of skin similar to that of an injection site. The smallest effective dose for bovine trypsin was similarly estimated to be 0.3 micrograms per injection site, which is in good agreement with the values previously reported by others. The results suggest that the mast cell protease may act as a mediator of inflammatory vasopermeability. The effect of the enzyme on two potential biological substrates was tested. The enzyme does not hydrolyze elastin, but degrades fibrin clot.
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PMID:The role of chymotrypsin-like protease of rat mast cells in inflammatory vasopermeability and fibrinolysis. 699 62

The presence of zymogen E in bovine pancreatic secretion was demonstrated by activation with trypsin and isolation of protease E. The enzyme, pI = 4.85, has k3 and Km values of 48 s-1 and 4.4 mM, respectively, for acetyl-tri-L-alanine methyl ester and an amino acid composition similar to that of porcine protease E. Gel filtration of the proteins in the secretion provided evidence that bovine zymogen E forms complexes with procarboxypeptidase A, including a ternary complex of these two proteins with chymotrypsinogen C. Taken together with previous observations on porcine zymogen E (Kobayashi, R., Kobayashi, Y., and Hirs, C. H. W. (1978) J. Biol. Chem. 253, 5526-5530) the data suggest that complex formation between procarboxypeptidase A and zymogen E may be a more widespread property of these proteins. The fact that zymogen E occurs as a major constituent in bovine pancreatic secretion in a physiological context n which no requirement for elastolysis exists suggests further that the functional significance of protease E in the digestion of proteins is general and not specific for elastin.
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PMID:Identification of zymogen E in a complex with bovine procarboxypeptidase A. 700 84

Bronchoalveolar lavage (BAL) fluid was obtained from 24 sequentially studied patients with adult respiratory distress syndrome (ARDS) for assessment of potential activating and mediating factors. Proteolytic activity of the fluids was observed by measuring cleavage of radiolabeled proteins of the contact (Hageman factor) and complement systems. Proteolytic activity was observed in 17 of 24 (71%) patients with ARDS, and BAL fluid of the 7 ARDS patients without demonstrable, active, enzyme exhibited inhibitory activity for the proteolytic activity. The enzymes cleaved Hageman factor, prekallikrein, plasminogen, high molecular weight kininogen, C4, C3, C5, and Factor B of the complement system. Cleavage of the contact system proteins producted fragments similar or identical in size to the fragments observed during activation of these molecules, although continued incubation invariably reduced the protein to small peptide fragments. None of 7 normal individuals, and 29 of 99 patients (29%) with other forms of pulmonary disease contained measurable enzymes. The proteolytic activity in BAL fluid of ARDS patients was blocked by diisopropylphosphofluoridate (0.1 mM), Trasylol, soybean trypsin inhibitor, and normal plasma, or plasma deficient in inhibition of the first component of complement. Alpha(1)-proteinase inhibitor (alpha1-PI)-deficient plasma failed to inhibit the proteolytic activity and addition of alpha1-PI to the deficient plasma reconstituted the inhibition. MUCH OF THE PROTEOLYTIC ACTIVITY OF THE BAL FLUID FROM ARDS PATIENTS WAS IDENTIFIED AS NEUTROPHIL ELASTASE: the fluids cleaved elastin and synthetic peptide substrate of neutrophil elastase, neutrophil elastase antigen was present in the BAL fluids as determined immunologically using antineutrophil elastase, alpha1-PI was the major inhibitor in plasma, and the enzyme was inhibited by diisopropylphosphofluoridate but not chelation. In addition, purified neutrophil elastase produced cleavage fragments of proteins of the contact system similar to those of the BAL fluids. In each of the seven BAL fluids of ARDS patients that did not reveal active elastase, alpha1-PI was present in active form (as determined by (125)I-trypsin binding). In 9 of the 17 patients with active elastase in the BAL fluid, alpha1-PI antigen was present in the fluid, but was inactive (no binding of (125)I-trypsin). Immunoelectrophoretic analysis of elastase and alpha1-PI throughout proteins in these BAL fluids revealed the presence of both elastase and alpha1-PI that migrated with the same R(f), suggesting the presence of an enzyme-inhibitor complex. Free, inactive alpha1-PI was also observed in these fluids. The data reveal that in BAL fluids from all 24 patients with ARDS, leukocytic elastase and/or alpha1-PI exist. A complex of elastase and alpha1-PI was observed in BAL fluids, and in some cases where active enzyme and alpha1-PI coexisted, free, but inactive alpha1-PI was present.
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PMID:Studies on the pathogenesis of the adult respiratory distress syndrome. 703 51

In the last several decades, enormous interest has been generated toward understanding the cell as it is controlled by its external physical environment. The purpose of this study was to determine the effects of well-defined applied mechanical stress and time-varying electric fields on the cellular synthesis of connective tissue macromolecules. Chondrocytes harvested by trypsin digestion of 15-day-old chick embryo sternae were randomly dispersed and cultured on elastin membranes in a humidified atmosphere with 10 per cent CO2 and 90 per cent air. Following five days of growth in F12 media and 5 per cent fetal calf serum, the membranes underwent either 1) a 10 per cent cyclic mechanical stretch or 2) 60 Hz A.C. electrical stimulation with current densities of 1 to 1,000 nA/mm2 or 3) control without stimulation, each for an eight-hour period. C14-hydroxyproline incorporation into collagen, and H2 35 SO4 incorporation into glycosaminoglycans (GAGs) were measured by liquid scintillation techniques. Scanning and transmission electron microscopy analysis of control and stimulated cells demonstrated discernable differences. Both mechanically and electrically stimulated chondrocytes showed a two- to three-fold increase in GAG synthesis and a general depression in protein and collagen synthesis over controls. The general similarity in response to both mechanical and electrical stress suggests common processes by which they modulate cellular synthesis of cartilage connective tissue proteins.
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PMID:A comparison of in vitro cellular responses to mechanical and electrical stimulation. 714 72

To understand the balance of proteinase antiproteinase activity and the production of extracellular matrix (ECM) at the site of arterial injury, we analyzed the composition of ECM and proteinase activity in normal internal mammary arteries, tissue samples obtained from atherosclerotic coronary lesions and restenotic lesions obtained during directional coronary atherectomy. Histologically and biochemically, collagen and proteoglycans increased, and elastin decreased in samples from restenotic lesions when compared to samples taken from patients undergoing their first revascularization (de novo). In contrast, cellularity was increased in samples obtained from de novo patients as compared to samples obtained from restenotic lesions. Intrinsic activity of matrix metalloproteinases (MMPs) was measured by using zymography and scanning all the lytic bands in zymographic gel. In these gels, identical amounts of total protein were loaded in each lane. MMP activity was determined as % of the total (latent and active) MMPs after trypsin activation (100%) in the normal artery. Intrinsic MMP activity was reduced to 6% +/- 1% in atherosclerotic lesions and 1% +/- 1% in restenotic lesions, when compared to activity found in normal (10% +/- 3%) arteries. Based on solubilization of fluorescein-conjugated elastin by the extracts, the MMP-mediated elastinolytic activity was 0.2 +/- 0.1, 8.8 +/- 1.5, and 24.0 +/- 3 nmol/min/mg in restenotic, native atherosclerotic and normal tissue, respectively. The results suggested that, in arterial tissue from patients with angiographic restenosis, there is an increased production of ECM collagen and a decrease in MMP activity compared to both normal artery and atherosclerotic samples from de novo patients undergoing an initial revascularization procedure of a significant coronary artery lesion.
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PMID:Proteinases and restenosis in the human coronary artery: extracellular matrix production exceeds the expression of proteolytic activity. 748 32

In vitro human dermal fibroblasts were submitted to normal gravity (1 g) or to chronic hypergravity (20 g) over a period of 8 days. Changes in organization of extracellular matrix molecules were seen by indirect immunofluorescence. In the fibronectin layer, bundles of fibrils were gathered together leading to a disorganisation of the normal parallel pattern of fibers seen in control cultures. Type I collagen fibrils appeared with wooly outlines in controls whereas thick fibers were closely packed in 20-g cultures. A moderate increase of type III collagen fibril density was observed. No elastic fibers were seen in control or in 20-g cultures. In the culture medium, the release of soluble elastin (ELISA) and type I and III collagens (RIA) was undisturbed. Assays of enzymes involved in the remodeling of extracellular matrix showed an increase of cellular elastase activity (10%) and a decrease of the spontaneously active collagenase. Nevertheless, the total collagenase activity, (activated by trypsin), was increased by up to 30%. These data show a significant rise of the latent collagenase activity and suggest that release of the tissue inhibitor of metalloproteinase (TIMP1) was enhanced by hypergravity.
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PMID:Modulation by hypergravity of extracellular matrix macromolecules in in vitro human dermal fibroblasts. 749 74

1. In order to characterize the physiological functions of the domain structure of secretory leukoprotease inhibitor (SLPI), the biological capacities of half-length SLPIs, (Ser1-Pro54)SLPI and (Asn55-Ala107)SLPI, were investigated and compared with those of full-length SLPI. 2. The activities of these inhibitors against several serine proteases were determined using synthetic chromogenic substrates. The inhibitory capacity of the C-terminal domain, (Asn55-Ala107)SLPI, was as strong as that of full-length SLPI against human neutrophil elastase (NE), cathepsin G and chymotrypsin. It possessed less trypsin inhibitory activity than intact SLPI. For the N-terminal domain of SLPI, (Ser1-Pro54)SLPI, no inhibitory activity could be detected against the serine proteases tested in this study. 3. The inhibitory activity of (Asn55-Ala107)SLPI against the proteolysis of the natural substrates elastin and collagen by NE was comparable with that of full-SLPI (elastin, IC50 = 907 +/- 31 nM for SLPI, 767 +/- 33 nM for (Asn55-Ala107)SLPI; collagen, IC50 = 862 +/- 36 nM for SLPI, 727 +/- 47 nM for (Asn55-Ala107)SLPI). 4. The binding affinities of full- and half-length SLPIs for heparin were measured by affinity column chromatography. Full-length SLPI showed high affinity for heparin while the binding capacities of both half-length SLPIs were lower. (Concentration of NaCl for elution, 0.45 M for SLPI, 0.24 M for (Ser1-Pro54)SLPI, 0.27 M for (Asn55-Ala107)SLPI). 5. The effects of full-SLPI and (Asn55-Ala107)SLPI on blood coagulation were measured using the activated partial thromboplastin time (APTT). Full-length SLPI prolonged clotting time dose dependently(1.25, 2.5 and 5.0 microM), whereas (Asn55-AlalO7)SLPI had no effect even at the highest concentration.6. In conclusion, the C-terminal domain of SLPI is a promising candidate for the treatment of inflammatory diseases in which participation of neutrophil proteases has been suggested.
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PMID:Pharmacological activity of the C-terminal and N-terminal domains of secretory leukoprotease inhibitor in vitro. 758 15

The proteolytic activities of homogenates prepared from the second larva (L2) and the third larva (L3) as well as the adult stage of the eel-pathogenic nematode Anguillicola crassus were examined using hemoglobin, azocoll, elastin-orcein, and keratin azure as substrates. Whole bodies of L2 larvae, the anterior third of the bodies of L3 larvae, and the anterior fifth of the bodies of adults were studied. Extracts of L2 contained a trypsin-like proteinase exhibiting a molecular weight of 38,000 Da on gelatin-substrate gel electrophoresis. The proteinase showed a pH optimum at 8 and activity against azocoll and keratin. An apparent molecular weight of 25,000 Da was determined for the trypsin-like proteinase of the L3. This enzyme possessed collagenolytic, keratinolytic and slight elastinolytic activity at an optimal pH of 8. Samples of adults contained an aspartyl proteinase with a molecular weight of 90,000 Da. When hemoglobin was used as the substrate, the enzyme displayed optimal activity at pH 5. It was concluded that the proteinases of the larval stages are penetration enzymes, whereas that of the adult stage is a digestive enzyme.
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PMID:Identification and characterization of the proteolytic enzymes in the developmental stages of the eel-pathogenic nematode Anguillicola crassus. 768 26


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