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:3.4.21.7 (plasmin)
9,023 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The release of beta-lysin, which followed the intravenous injection of antigen-antibody complexes, did not take place when these complexes were added to citrated whole blood but did occur in heparinized blood. beta-Lysin release in heparinized blood was inhibited by citrate but were reversed by the addition of calcium ions that implicated complement reactions. Fourteen different enzymes were added to platelet-rich plasma (PRP). Streptokinase, neuraminidase, papain, phospholipase C, sulfatase, and trypsin caused platelets to release significant quantities of beta-lysin, whereas elastase, phosphatase, protease, ribonuclease A, hyaluronidase, lipase, and pepsin caused little or no increase in the plasma beta-lysin concentration. One enzyme, fibrinolysin, inactivated beta-lysin faster than it was released. The enzyme-induced release of beta-lysin from PRP was often accompanied by a reduction in the number of platelets. The intravenous injection of streptokinase, neuraminidase, and sulfatase caused in vivo releases of beta-lysin into the plasma. The platelet-aggregating substances collagen, arachidonic acid, and adenosine 5'-diphosphate caused beta-lysin to be released from PRP. The platelet-aggregating substances L-epinephrine, zymosan, fibrinogen, reserpine, and serotonin caused little or no release of beta-lysin from platelets. The results of this study indicate that the release of beta-lysin during antigen-antibody-complement reactions, blood coagulation, phagocytosis, and inflammation could be enzyme mediated.
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PMID:Release of beta-lysin from platelets caused by antigen-antibody complexes, purified enzymes, and platelet-aggregating substances. 84 4

When human granulocytes were stimulated with the chemotactic peptide FNLPNTL (N-formyl-norleucyl-leucyl-phenylalanyl-norleucyl-tyrosinyl- lysin; in the presence of cytochalasin B), proteolytic enzymes were released which prevented activation of tumor-cell derived pro-uPA by plasmin. Elastase was identified by use of eglin C (elastase inhibitor) and an inhibitory monoclonal antibody to elastase as the functional proteolytic enzyme in these granulocyte supernatants. Purified human granulocyte elastase cleaves pro-uPA at amino acid position lle159-lle160 thus generating an enzymatically inactive two-chain form of uPA, as judged by N-terminal amino acid sequence analysis. An additional minor elastase-mediated cleavage site was detected at position Thr165-Thr166. This form of uPA was indistinguishable by SDS-PAGE from plasmin-generated enzymatically active HMW-uPA. Action of plasmin on the proenzyme form of uPA (pro-uPA) generates an enzymatically active uPA-molecule (high molecular weight form; HMW-uPA) which is cleaved at amino acid position Lys158-lle159 (Mr = 33,000 (B-chain) and 22,000 (A-chain). Thus elastase cannot substitute for plasmin in the proteolytic activation of pro-uPA to enzymatically active HMW-uPA. Enzymatically active HMW-uPA, however, was not affected by elastase. Elastase-containing granulocytes were identified by immunohistochemical staining of elastase in breast cancer tissue. Granulocytes were located close to the tumor cells and also in the tumor stroma surrounding the tumor nests. These tumor cells contain pro-uPA. Evidently, the conversion of tumor cell pro-uPA into enzymatically active HMW-uPA is controlled by elastase released from granulocytes into the tumor tissue.
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PMID:Human tumor cell urokinase-type plasminogen activator (uPA): degradation of the proenzyme form (pro-uPA) by granulocyte elastase prevents subsequent activation by plasmin. 183 19

The effects of protease inhibitors(PI), t-AMCHA, gabexate, aprotinin and heparin on the growth of mouse MM2 ascites tumor (MAT) and on several components of fibrinolysis were studied. The drugs were administered intraperitoneally one time daily for 12 days, one day after the tumor transplant. The volumes of ascites, total packed cell volume (TPCV) and fibrinolytic parameters (FDP, whole plasmin, plasminogen activator (PA)) were measured on the 8, 10 and 12th days of therapy. Fibrinolytic activity was assayed by the lysin sepharose affinity chromatography-radio caseinolytic method. Fibrinolytic activity in the ascites increased during the tumor growth. The ascites accumulation as well as levels of FDP, whole plasmin and PA in the drug treated group were significantly decreased when compared to the control group. In these drug-treated groups, MAT cells agglutinated in the abdominal cavity, but in contrast to this, no agglutination was observed in the control group. It was uncertain whether PI directly inhibited tumor growth. The fact that PI inhibited the ascites accumulation and also decreased fibrinolytic activity suggest the involvement of protease in the neoplastic process and indicates another therapeutic approach to malignant ascites tumors.
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PMID:[Studies on fibrinolysis and ascites accumulation associated with peritonitis carcinomatosa--effects of protease inhibitors (PI) on MM2 ascites tumor growth, ascites accumulation and fibrinolysis]. 242 22

Plasminogen preparation from donor blood and fibrinolytically active blood plasma from humans after sudden death were obtained using affinity chromatography on Lysin-sepharose 4B. The plasminogen preparation from donor blood was shown to be highly purified native plasminogen (Glu-plasminogen). The preparation containing activated plasminogen (Lys-plasminogen), plasmin, plasminogen activator, alpha 2-macroglobulin, alpha 1-antitrypsin, fibrin/fibrinogen was obtained from the blood plasma of humans after sudden death. The appearance of proteins lacking biological specificity to lysin-sepharose in the plasminogen preparation shows the ability of activated plasminogen and plasmin to form complexes with these proteins and demonstrates the retention of the functional activity in lysin-binding regions on their molecules. Monospecific sera to the isolated preparations were obtained, demonstrating the presence of the same immunochemical determinants in native and activated plasminogen.
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PMID:[Effect of endogenous fibrinolysis activation on human plasminogen]. 243 67

Hydrolysis of plasminogen permits obtaining its nine fragments. The method of differential scanning microcalorimetry reveals seven domains in plasminogen, and the affinity chromatography--three lysin- and three arginyl-binding sites. The lysin-binding sites of domains (Kringles) K1 and K4 differ in ligand specificity. Benzamidine-binding sites of domain K5 and of plasmin light chain are simultaneously arginine-binding ones. The third arginyl-binding site differing from the benzamidine-binding one is found in fragment K1-3. In the plasminogen-fibrin interaction only lysin-binding sites of plasminogen take part; in the plasminogen fragments-fibrinogen fragments interaction both types of plasminogen sites participate. The heavy chain of plasmin interacts with the E-fragment of fibrinogen by the lysin-binding sites, and the light chain of plasmin interacts with D-fragment of fibrinogen by arginyl-binding sites. Sites complementary to arginyl binding sites of plasminogen are located on the DH-fragment and sites of interaction with lysin- and arginyl-binding sites--on the DL-fragment. The plasmin-fibrin interaction mediated by sites of the first four cringles is not associated with changes in the catalytic function of the active centre. Interaction of Lys-plasminogen with fibrin accelerates polymerization of the latter. The effect of Lys-plasminogen is conditioned by the lysin-binding sites. Glu-plasminogen has no effect on the polymerization process.
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PMID:[Lysine- and arginyl-binding sites of plasminogen domains]. 293 24

Bovine and human blood plasma contains alpha 2-antiplasmin which possesses affinity to lysin-binding sites in plasmin and inhibits the human plasmin. Its isolation was conducted for two stages: separation of plasminogen on lysin-cellulose, fractionation by ammonium sulphate, desalination on molselector G-25, chromatography on DEAE-Sephadex A-50 and affinity chromatography on plasmin-sepharose with the blocked active site.
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PMID:[Alpha 2-antiplasmin in bovine plasma]. 403 96

The heavy and light chains of human plasmin were separated by affinity 1-lysin-cellulose column chromatography. The S-carboxymethyl light chain derivative of human plasmin was imobilized by aminogroups by the insoluble matrices. Insoluble derivatives cf plasmin light chain retain an insignificant proteolytic activity, human plasminogen activator activity and capacity to form complexes with streptokinase. The activator activity of the immobilized light chain-streptokinase complex increases 5-10-fold with respect to the human plasminogen. When adding the light chain preparation to immobilized streptokinase its activator activity relative to the human plasminogen is twice as high. The both complexes: immobilized light chain-streptokinase and light chain-immobilized streptokinase are stable and may be reused for plasminogen activation.
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PMID:[Immobilization of the human plasmin light chain and analysis of its complexes with streptokinase]. 622 27

It was demonstrated that plasminogen and the plasmin heavy chain form a complex with an immobilized fibrinogen fragment E. The E-fragment interacts, in its turn, with the immobilized heavy chain; this interaction is provided for by the lysin binding sites of the plasminogen molecule. The plasmin light chain having no lysin binding sites is specifically absorbed on the immobilized fragment D, whereas the D-fragment--on the immobilized light chain. The elution is caused by arginine or benzamidine; 6-aminohexanoic acid does not affect this interaction. It is assumed that the interaction of plasminogen and plasmin with fibrin is provided for not only by the lysine binding but also by the benzamidine binding sites of the plasminogen molecule.
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PMID:[Interaction of heavy and light chains of plasmin with fibrinogen E and D fragments]. 624 Sep 93

In previous studies we observed the presence of an antigen reacting with anti-plasminogen serum on tumor cells found in sections of human colorectal and mammary carcinomas, using immunofluorescence. This antigen could be plasminogen, or plasmin or both. These results led us to surmise that carcinoma cells, and not normal epithelial cells, had a receptor for plasmin and plasminogen. We demonstrated the existence of such a receptor on cells of established tumor cell lines of colonic and mammary origin. We observed that binding of plasmin(ogen) to its receptor was inhibited by lysin and its analogs. We undertook to characterize the plasmin receptor on sections of human mammary carcinomas (18 series of sections, originating from 15 infiltrating ductal carcinomas). In our immunofluorescence studies, we observed that the fluorescence induced by anti-plasminogen serum was suppressed by pre-treatment of the sections with tranexamic acid, a lysin analog. Furthermore, when parallel sections were incubated with tranexamic acid, then with solutions of plasminogen, tumor cells were made fluorescent again. Another important finding was the strong increase of labelling observed when sections were incubated with plasminogen or plasmin before reaction with anti-plasminogen serum. This labelling disappeared when tranexamic was added to plasminogen. As a whole, these results confirm the existence of plasmin receptors on tumor cells in mammary carcinoma sections. They also show that these receptors are not saturated in vivo and may bind, in vitro, additional amounts of ligand.
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PMID:Visualization of the plasmin receptor on sections of human mammary carcinoma cells. 767 31

Intrapleural loculation can increase morbidity in hemothoraces or parapneumonic effusions. Intrapleural fibrin precedes visceral-parietal pleural adhesions. We speculated that single-chain urokinase plasminogen activator alone or bound to its receptor could prevent these adhesions by their relative resistance to local inhibition by plasminogen activator inhibitors. We found that recombinant human single-chain urokinase-bound rabbit pleural mesothelial cells or lung fibroblasts with kinetics similar to that reported for human cells (kD of approximately 5 nM). The receptor-bound fibrinolysin maintained in vitro fibrinolytic activity in the presence of pleural fluids from rabbits with tetracycline-induced pleural injury over 24 hours. In rabbits given intrapleural single-chain urokinase 24 and 48 hours after intrapleural tetracycline (n = 10 animals), adhesions were prevented, whereas the receptor-complexed form (n = 12) attenuated adhesions versus vehicle/tetracycline-treated rabbits (n = 22, p <or= 0.005 in both cases). There were more adhesions in the complex than the single-chain urokinase group (p = 0.02). Residual antigenic but not functional evidence of the interventional agents remained in pleural fluids at 72 hours after tetracycline. No local or systemic bleeding occurred because of either interventional agent. The data demonstrate that single-chain urokinase inhibits, whereas lysin-receptor complexes attenuate, adhesion formation in tetracycline-induced pleural injury in rabbits.
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PMID:Single-chain urokinase alone or complexed to its receptor in tetracycline-induced pleuritis in rabbits. 1235 44


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