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:3.4.24.3 (collagenase)
18,340 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We examined whether the generation of reactive oxygen metabolites (as quantified by measuring luminol-amplified chemiluminescence) by isolated rat glomeruli could be triggered enzymatically. No response was observed with thrombin (1 or 10 U/ml), collagenase (100, 200, or 400 U/ml), or plasmin (0.1 or 1 U/ml). In contrast, chymotrypsin and trypsin caused a dose-dependent (10-200 micrograms/ml) increase in chemiluminescence from glomeruli. The peak response with chymotrypsin (100 micrograms/ml) and trypsin (50 micrograms/ml) was as follows: resting, 16 +/- 2 X 10(3) cpm/mg protein, n = 17; chymotrypsin, 233 +/- 58 X 10(3) cpm/mg protein, n = 17; and trypsin, 221 +/- 38 X 10(3) cpm/mg protein, n = 10. Tubules had only a minor response. Soybean trypsin inhibitor and aprotinin caused marked inhibition, indicating the dependency of the chemiluminescence response on the protease enzyme activity. The chemiluminescence response was by glomeruli rather than by "contaminating" leukocytes, since a similar marked response (n = 6) was observed in glomeruli isolated from cyclophosphamide-treated leukopenic (leukocyte less than 1,000/mm3) rats. Superoxide dismutase, a scavenger of superoxide, and free-radical scavengers benzoate and tryptophan inhibited the glomerular chemiluminescence response to trypsin and chymotrypsin. Neutral proteases from infiltrating leukocytes and/or renal tissue have been shown to be released in glomerular diseases; our results, which show the generation of chemiluminescence in response to neutral proteases, suggest a potential mechanism for the production of reactive oxygen metabolites in glomerular diseases.
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PMID:Trypsin- and chymotrypsin-induced chemiluminescence by isolated rat glomeruli. 359 31

We have identified a tissue-kallikrein-binding protein in human serum and in the serum-free culture media from human lung fibroblasts (WI-38) and rodent neuroblastoma X glioma hybrid cells (NG108-15). Purified and 125I-labelled tissue kallikrein and human serum form an approximately 92,000-Mr SDS-stable complex. The relative quantity of this complex-formation is measured by densitometric scanning of autoradiograms. Complex-formation between tissue kallikrein and the serum binding protein was time-dependent and detectable after 5 min incubation at 37 degrees C, with half-maximal binding at 28 min. Binding of 125I-kallikrein to kallikrein-binding protein is temperature-dependent and can be inhibited by heparin or excess unlabelled tissue kallikrein but not by plasma kallikrein, collagenase, thrombin, urokinase, alpha 1-antitrypsin or kininogens. The kallikrein-binding protein is acid- and heat-labile, as pretreatment of sera at pH 3.0 or at 60 degrees C for 30 min diminishes complex-formation. However, the formed complexes are stable to acid or 1 M-hydroxylamine treatment and can only be partially dissociated with 10 mM-NaOH. When kallikrein was inhibited by the active-site-labelling reagents phenylmethanesulphonyl fluoride or D-Phe-D-Phe-L-Arg-CH2Cl no complex-formation was observed. An endogenous approximately 92,000-Mr kallikrein-kallikrein-binding protein complex was isolated from normal human serum by using a human tissue kallikrein-agarose affinity column. These complexes were recognized by anti-(human tissue kallikrein) antibodies, but not by anti-alpha 1-antitrypsin serum, in Western-blot analyses. The results show that the kallikrein-binding protein is distinct from alpha 1-antitrypsin and is not identifiable with any of the well-characterized plasma proteinase inhibitors such as alpha 2-macroglobulin, inter-alpha-trypsin inhibitor, C1-inactivator or antithrombin III. The functional role of this kallikrein-binding protein and its impact on kallikrein activity or metabolism in vivo remain to be investigated.
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PMID:Identification of a new tissue-kallikrein-binding protein. 364 93

Ascitic fluid samples from 14 subjects with liver cirrhosis and from 13 patients with malignancy were investigated. Activated FX was present in ascitic fluid in small quantities with a mean value of 8.7 10(-3) IU/ml. The mean thrombin activity was 70.8 10(-3) IU/ml and the mean plasmin activity was 449.6 10(-3) CU/ml. High levels of fibrin/fibrinogen degradation products (mean 75.4 micrograms/ml) and of antithrombin III (mean 43.4%) were found. No statistically significant differences between values in liver cirrhosis and in malignancy were found. In 15 of 17 experiments 10-fold concentrated ascitic fluid caused irreversible platelet aggregation and [14C] serotonin release of normal platelet-rich plasma similar to collagen. The aggregating effect disappeared after addition of collagenase. These results do not support the concept that the coagulopathy after peritoneovenous shunting is a result of direct and rapid intravenous infusion of procoagulant substances. They rather point to a central role of collagen present in ascitic fluid.
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PMID:Coagulant, fibrinolytic, and aggregating activity in ascitic fluid. 370 62

The experimental modulation of tight junctions (TJ) was studied in the human adenocarcinoma cell line HT 29 by freeze-fracture electron microscopy. The cell line has virtually no TJ when grown in culture. TJ could be induced by mild treatment with a variety of endopeptidases (trypsin, chymotrypsin, collagenase, elastase, plasmin, thrombin, papain, and pronase). Pronase induced the formation of TJ at low (but not at high) concentrations. All exopeptidases studied were unable to induce the formation of TJ. At 0 degree C the trypsin-induced formation of TJ was greatly slowed down although not entirely inhibited. However, when cells were briefly treated with trypsin at 0 degree C and subsequently transferred to 37 degrees C in the presence of protease inhibitors, TJ were rapidly assembled. Thus an induction phase at low temperature and an assembly phase at high temperature could be experimentally separated. When cells were briefly trypsinized at 0 degrees and subsequently kept at 0 degree C without trypsin for several hours, TJ still formed abundantly upon incubation at 37 degrees C. It appears therefore that the effect produced by the protease is retained for long periods in the cold.
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PMID:Formation of tight junctions in epithelial cells. I. Induction by proteases in a human colon carcinoma cell line. 388 Jul 1

In this study, the effect of sixteen different enzymes on serum C1 and its subcomponents was investigated. The sixteen enzymes could be divided into three groups. First, enzymes which activate native C1: trypsin (optimal concentration 2.4 x 10(-4) mM); alpha-chymotrypsin (2.3 x 10(3) mM); thrombin (1.0 x 10(-5) mM); plasmin (1.9 x 10(-5) mM); elastase (5.8 x 10(-5) mM); pronase (3.0 x 10(-6) mM). All these enzymes are serine esterase and activate native serum C1 bound to EAC4 at the given concentration within 10 min at 30 degrees C. Furthermore, native C1 inhibited by a pentosanpolysulfoester, Sp54, is unable to undergo the internal activation but can be externally activated by the serine esterases. Second, enzymes which do not activate native C1 but result in a dose and time-dependent loss of C1 activity: collagenase; pepsin; carboxypeptidase B. Third, enzymes which have no effect on C1 and C1: Lysozyme; neuraminidase; beta-galactosidase; L-amino acid oxidase; arginase; streptokinase, and acetylcholinesterase.
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PMID:Activation of the first component of complement, C1: comparison of the effect of sixteen different enzymes on serum C1. 619 90

A human umbilical cord vein model was used to study the interaction of human blood with vein intima after treatment with certain enzymes. Treatment of the intima with neuraminidase produced little in the way of morphologic change, and studies showed no increase in the retention of platelets labeled with chromium 51. Treatment of vein intima with collagenase produced severe morphologic changes, with exposure of coarse and fine subendothelial fibers, but with the retention of platelets little enhanced, as determined morphologically or radiometrically. On the other hand, treatment of vein intima with trypsin resulted in loss of endothelium in some areas, with exposure of coarse subendothelial fibers that produced a marked increase in platelet retention, as determined both morphologically and radiometrically. Exposure of the vein intima to thrombin produced apparent contraction of endothelial cells, with focal exposure of subendothelium and platelet adhesion.
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PMID:A human model for study of blood-vascular wall interactions. Effects of enzymatic treatment of intima. 625 5

Attempts were made to clarify the mechanism of platelet aggregation and to characterize the platelet aggregating material employing established human cancer cell lines. Eleven out of the nineteen human cancer cell lines investigated showed platelet aggregating activity. The existence of divalent cation was required for the platelet aggregation induced by HMV-1 tumor cells. The platelet aggregations induced by tumor cells (HMV-1, PC-10, 3LL) were not suppressed by specific thrombin inhibitor (MD-805). The platelet aggregating activities of tumor cells (HMV-1, M 7609) were diminished by treatment with trypsin but not with collagenase or neuraminidase. Aggregating activity was preserved with a preparation of membrane from these tumor cells, although it was abolished by heating(100 degrees C 15 min) or sonication. By SDS PAGE (autoradiography), membrane proteins with MW of 20,000 daltons which specifically bound to platelets were commonly found in cells with platelet aggregating activity (HMV-1, M 7609), but were absent in platelet non-aggregating cells (HGC-25). It is therefore concluded that platelet aggregation induced by human tumor cells does not require the coexistence of thrombin, but is evoked by direct interaction of platelets with aggregating proteins (MW 20,000 daltons) on the cell membrane.
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PMID:[Studies on platelet aggregation induced by human cultured carcinoma cell lines]. 632 1

A 140 000 D glycoprotein (140 kD gp), labelled radioactively with surface-specific techniques, remained as the major cell surface glycoprotein in the detergent-resistant cytoskeletal preparations of cultured human fibroblasts. The 140 kD gp was present also in trypsinized cells and was not affected by treatment of the cells either with collagenase, chymotrypsin or thrombin. In density gradient fractionation of whole cells the 140 kD gp was recovered in the plasma membrane fraction together with small amounts of cytoskeletal components. In fractionation of cytoskeletal preparations, on the other hand, the 140 kD gp could not be dissociated from cytoskeletal proteins and together with vimentin it formed the major component of the oligomeric polypeptide complex generated by treating the surface-labelled cytoskeletal preparations with bifunctional cross-linking reagent, dithiobis succinimidyl propionate (DTPS). Moreover, the 140 kD gp seemed to copurify with vimentin upon reconstitution of intermediate filaments from urea-solubilized cytoskeletal preparations. On the other hand, low ionic-induced degradation of vimentin led to a decrease in the amount of the detergent-resistant 140 kD gp on the cell surface. In electron microscopy, a close apposition between bilayer-like plasma membrane remnants of the adherent cytoskeletons and cytoskeletal elements could be seen. The results indicate that the 140 kD gp is a plasma membrane glycoprotein which closely interacts with the detergent-resistant cytoskeleton of cultured human fibroblast. Possible mechanisms of the association are discussed.
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PMID:140 000 Dalton surface glycoprotein. A plasma membrane component of the detergent-resistant cytoskeletal preparations of cultured human fibroblasts. 633 55

Colloidal gold is an electron-dense, lyophobic colloid that readily forms a stable electrostatic interaction with a variety of macromolecules. Monodispersed colloids ranging from 3-150 nm in diameter can be produced to provide the researcher with flexibility in selecting the optimally sized probe. Gold labeling of antibodies and lectins has been extensively used to study surface antigens and cell components. Recently, the use of gold labeling has been extended to study receptor-ligand binding, enzyme-substrate reactions, and transcellular pathways. Published applications include gold labeling of metabolites (low-density lipoproteins), enzymes (DNAase and RNAase, RNA polymerase, thrombin, collagenase, elastase), hormones (insulin, epidermal growth factor, glucagon), circulating plasma proteins (asialoglycoprotein, alpha 2-macroglobulin, factor VIII-von Willebrand factor), and endotoxins (tetanus toxin, cholera toxin). This broad spectrum of applications emphasizes the versatility and usefulness of colloidal gold as a probe in areas of cell biology related to receptors, endocytosis, transport, and functions of proteins.
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PMID:Colloidal gold: a pluripotent receptor probe. 635 33

Uptake and metabolism of arachidonic acid, arachidic acid and oleic acid were investigated in isolated hepatocytes prepared from mouse liver with the collagenase perfusion method. The rate of uptake of arachidonic acid was time- and concentration- dependent. 94-98% of the arachidonic acid was incorporated into the phospholipid and triacylglycerol fractions following a 60 min incubation period at 37 degrees C. In the presence of thrombin-anti-thrombin III complex a change in the distribution of arachidonic acid incorporated into lipid fractions was found, i.e. increased incorporation into phosphatidyl-serine and phosphatidylethanolamine, whereas the uptake was not altered. There was no change in the uptake and incorporation of arachidic acid and oleic acid.
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PMID:Uptake of arachidonic acid, arachidic acid, oleic acid and their incorporation into phospholipids and triacylglycerols of isolated murine hepatocytes. Effect of thrombin-antithrombin III complex. 643 78


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