FIBRINOLYSIN ACTIVITY TEST. A SIMPLE SCREENING LABORATORY PROCEDURE FOR THE DIFFERENTIATION OF FIBRINOLYSIN AND THE DEFIBRINATION SYNDROME.
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Afibrinogenemia↗
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[The clinical value of fibrinolysin determination. I. Fibrinolysin determination in diseases of the liver and biliary tract].
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Biliary Tract↗
[Effect of a combination of fibrinolysin, heparin and a fibrinolysin-heparin complex with dihydroergotoxine on thrombolysis].
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Animals↗
[Pneumonitis in a patient who inhaled a fibrinolysin-deoxyribonuclease mixture].
A 56-year-old man was transferred to our department from the department of oral surgery, with a high fever and a cough. He had inhaled a fibrinolysin-deoxyribonuclease mixture (Elase) to treat inflammation in the oral cavity after resection of an oral tumor. A chest X-ray film showed diffuse patchy shadows in both lung fields. Bronchoalveolar lavage fluid had an abnormally high number of lymphocytes and transbronchial lung biopsy revealed interstitial infiltration by lymphocytes and histiocytes, with granulomatous lesions. The patient was treated with steroids, and his clinical condition improved markedly. He accidentally inhaled the drug again, and the coughing and fever began again. The drug lymphocyte stimulation test was positive only for the fibrinolysin-deoxyribonuclease mixture. Based on these findings, we diagnosed pneumonitis induced by this fibrinolysin-deoxyribonuclease mixture. To our knowledge, this is the first reported case of pneumonitis caused by this fibrinolysin-doxyribonuclease mixture.
Administration, Inhalation↗
Molar concentrations of fibrinolytic components, especially free fibrinolysin, in vivo.
The levels of fibrinogen and of profibrinolysin (plasminogen) in urokinase-treated plasma as a function of time of incubation were measured. The profibrinolysin concentration was estimated through its complete conversion to fibrinolysin and the inhibition of the enzyme by crystalline soybean trypsin inhibitor. The dissociation constant of the FL-STI complex was determined to be 7 times 10-9 M. The average concentration of profibrinolysin in normal human citrated plasma was found to be 8 times 10-7 M. From the decrease of fibrinogen with time in the urokinase-treated plasma, the free fibrinolysin was calculated. Free fibrinolysin in normal human blood in vivo was estimated from the half-life of fibrinogen and other data obtained in this study to be present at a concentration of 1.7 times 10-10 M. The plasmakinase activity in vivo, expressed as urokinase molarity, is also about 2 times 10-10 M.
Fibrinogen↗
Studies on the fibrinolysin-antifibrinolysin system in serum. I. Action of the anterior pituitary, adrenal cortex, and spleen.
Injection of ACTH or cortisone has no effect on the amount of fibrinolysin resulting from the activation of profibrinolysin by peptone. Antifibrinolytic activity of serum is significantly increased by ACTH or cortisone but not by desoxycorticosterone or corticosterone. No increase in anti-fibrinolytic power of serum is produced, however, by the injection of ACTH or cortisone in splenectomized guinea pigs. Splenin A has the same action on fibrinolysin inactivation as ACTH or cortisone. Splenin B has the opposite effect. This action on the antifibrinolytic power of serum appears to be due to an acceleration of the rate of combination between the enzyme and its inhibitor and not to an actual increase in antifibrinolysin. The possible significance of these observations is discussed.
Adrenal Cortex↗
Fibrinolysin therapy of thrombophlebitis and pulmonary embolism--a double-blind study.
Thrombophlebitis and pulmonary embolism are major causes of disability and death in both medical and surgical patients. Etiological factors are still poorly understood. Preventive measures as currently practised are non-specific and based on questionable premises. Diagnostic measures to predict the silent fatal embolus are inadequate. Currently accepted treatment measures are designed to prevent extension of the thrombus but have no effect on the existing clot. Theoretically, thrombolytic preparations now being marketed offer some hope for dissolution of preformed thrombi. An experimental study was carried out on artificially induced thrombi in jugular and femoral veins of mongrel dogs. Human fibrinolysin (Actase, Ortho) was infused locally and systemically in varying doses. No thrombi were successfully lyzed by either method. Thirty-six cases of acute deep thrombophlebitis in the leg, one of axillary thrombosis, three of chronic postphlebitis of a lower limb with massive edema and eight of pulmonary emboli were observed and carefully documented clinically. All these patients received anticoagulants unless there was a contraindication. Fibrinolysin infusions in varying dosages were administered to 27 patients; 10 served as controls. The observers were unaware of the identity of those receiving the actual drug or of those given the placebo until completion of the study. Progress of the disease was judged by the rate of dis-appearance of symptoms and signs. No significant benefit could be noted in the treated as compared to the control group, in terms of rate of recovery or incidence of embolus.
Acute Disease↗
[Effect of fibrinolysin and heparin on the kinetic properties of the thrombocytes and the oxidation-reduction processes in myocardial infarct].
Complex study of blood platelet adhesion and aggregation, blood coagulation activity and oxidation-reduction processes was conducted in dynamics in 340 patients with myocardial infarction. in 53 of them before and after treatment with fibrinolysin and heparin. It is shown that in patients with myocardial infarction, particularly in the first days of the disease and with the development of cardiogenic shock and pulmonary edema, the adhesion and aggregation of blood platelets increase with parallel increase in the content of incompletely oxidized products in the blood. A definite parallelism was found between the changes in the kinetic properties of platelets and the oxidoreduction processes. A decrease in the platelet kinetic properties and improvement in the oxidation-reduction processes due to the effect of fibrinolysin and heparin were observed.
Adult↗
[The mutual transmission of Staphylococcus aureus between humans and cattle and the environmental adaptation of hemolysin and fibrinolysin formation].
In an ecological investigation in 20 dairy herds of cattle we compared the characteristics of strains isolated from nasal swabs of milkers, from the udder of cows and from cases of mastitis in cows. In 7 herds we found definite strains in the nasal flora of the milkers and in the udder-flora of the cows which only differ in the formation of hemolysin and of fibrinolysin. In the other checked characteristics strains from man and strains from cattle show identical patterns. In 5 herds these strains correspond to the host-specific variety hominis, in 2 herds to the hostspecific--variety bovis. These results refer to an environmental adaptation of the phenotypically detectable formation of hemolysins and fibrinolysin. From the ecological point of view an exchange of strains between man and cattle is likely. The origin of strains which can not be alloted to one ot the known host-specific varieties can be explained by an environmental adaptation. Besides the facts that strains of the host-specific variety bovis occur only very rarely in man and that strains of the host-specific variety hominis occur occasionally in cattle the clinical significance of the reported results has to be clarified by further investigations.
Adaptation, Biological↗
[Specific proteolysis by fibrinolysin-coagulase from Yersinia pestis of Yersinia pseudotuberculosis outer membrane proteins coded by the Ca(2+)-dependence plasmid].
The pesticinogenicity 9.5 kb plasmid from Yersinia pestis strain EV76 has been marked by the kanamycin phosphotransferase gene inserted into PstI site and designated pP3. The obtained plasmid pP3 determines the synthesis of 45 kd pesticin, alpha and beta-forms of fibrinolysin coagulase (37 and 35 kd) and the 29, 19 and 13 kd proteins in Escherichia coli mini cells. When transferred into Yersinia pseudotuberculosis strain 6933 the plasmid causes the proteolysis of outer membrane proteins. The 150 kd protein is reduced to 138 kd, the 48.5 kd protein is reduced to 45 kd. The proteins secreted into the cultural medium (51 and 38 kd) are also cleaved. The proteolysis of the 150 kd protein was found to occur at the stage of secretion via the inner membrane. The purified fibrinolysin coagulase from Escherichia coli strain JM83 harbouring the plasmid pP3 induces the proteolysis in vitro of the isolated membrane proteins from Yersinia pseudotuberculosis strain 6953 similar to the proteolysis registered in vivo.
Autoradiography↗
Enhancement of the radiation effect by fibrinolysin and quantitative pattern of the change of tumor radiosensitivity.
Radiomodifying action of fibrinolysin was studied during radiation treatment in experimental transplanted tumors. It has been established that the application of fibrinolysin prior to radiation increases the inhibition of the growth rate of Pliss lymphosarcoma and Sarcoma 45, as evidenced by the decrease of the tumor volume, the increase of the dose change factor and the animals survival.
Animals↗
[Effect of bioresolving microspheric preparations of immobilized fibrinolysin on the fibrinolysis system].
The effect of microspheric preparations of immobilized fibrinolysin on the fibrinolysis system has been studied in dog experiments. It was shown that the fibrinolytic activity of whole blood increases in the region where the preparation is applied due to the presence of the introduced enzyme and to the increase in the activity of natural plasminogen activator. The application of immobilized fibrinolysin causes predominantly an increase in the activity of the plasminogen activator rather than in the fibrinolytic activity itself. The data obtained suggest the therapeutic importance of the method of immobilized thrombolytic preparation application under investigation.
Animals↗
[Thrombolytic effect of plasmin, miniplasmin and fibrinolysin in simulated intraocular hemorrhage].
The fibrinolytic properties of the preparations of plasmin (Pm), mixture of plasminogen and streptokinase (Pg+Sk), miniplasmin (m-Pm) and fibrinolysin have been investigated on the models of rabbit's hyphema. The action of preparations of Pm and Pg+Sk had approximately equal therapeutic index--the total destruction of clots proceeded for 12.0 days, that was 6.6 days less than in the control group. The therapeutic effect for m-Pm was 3.6 days. The dose of preparation of m-Pm, necessary for total destruction of clots, was 15-20% greater than for the same dose of Pg+Sk. The preparation of fibrinolysin, used in the same quantities of proteolytic activity, as Pg and m-Pg, (16 caseinolytic units per 1 injection) had no therapeutic effect.
Animals↗
Prevention of peritoneal adhesions in the rat. The effects of dexamethasone, methylprednisolone, promethazine, and human fibrinolysin.
Peritoneal adhesions were created in rats by brisk scrubbing of the terminal part of the ileum. Adhesions were graded by total number and the presence of small bowel obstruction. Adhesion prophylaxis was evaluated using dexamethasone, methylprednisolone sodium succinate, promethazine hydrochloride, and human fibrinolysin (Thrombolysin) in various combinations, doses, and routes of administration. Methylprednisolone and dexamethasone, depending on the route of administration, modified the total number of adhesions but did not modify their severity when compared to control animals. Promethazine by itself modified peritoneal adhesions in the rat. Used together, methylprednisolone and promethazine also modified adhesions, but were not substantially better than the combination of dexamethasone and promethazine. Methylprednisolone, promethazine, and human fibrinolyzin, when used in combination intraperitoneally, virtually eliminated adhesion formation.
Animals↗
Matrix metalloproteinases regulate neovascularization by acting as pericellular fibrinolysins.
During angiogenesis, endothelial cells penetrate fibrin barriers via undefined proteolytic mechanisms. We demonstrate that the fibrinolytic plasminogen activator (PA)-plasminogen system is not required for this process, since tissues isolated from PA- or plasminogen-deficient mice successfully neovascularize fibrin gels. By contrast, neovessel formation, in vitro and in vivo, is dependent on fibrinolytic, endothelial cell-derived matrix metalloproteinases (MMP). MMPs directly regulate this process as invasion-incompetent cells penetrate fibrin barriers when transfected with the most potent fibrinolytic metalloproteinase identified in endothelium, membrane type-1 MMP (MT1-MMP). Membrane display of MT1-MMP is required, as invasion-incompetent cells expressing a fibrinolytically active, transmembrane-deleted form of MT1-MMP remain noninvasive. These observations identify a PA-independent fibrinolytic pathway wherein tethered MMPs function as pericellular fibrinolysins during the neovascularization process.
Animals↗
Two fragments from fibrinolysin digests of ovine prolactin: characterization and recombination to generate full immunoreactivity.
The action of fibrinolysin (plasmin; EC 3.4.21.7) on ovine prolactin has been investigated. It was found that the enzyme selectively cleaves the bond between Met-53 and Ala-54. The two fragments, PRL-(1-53) and PRL-(54-199), have been purified and characterized. A recombinant molecule has been obtained by noncovalent interaction of PRL-(1-53) and PRL-(54-199). The recombined protein behaves nearly identically to the parent hormone in circular dichroism spectra and exclusion chromatography. The recombinant possesses full immunoreactivity, as revealed by gel double-diffusion and complement fixation. However, the recombined protein exhibits low prolactin activity in the pigeon crop-sac test.
Amino Acids↗
Radioimmunoreactivity and receptor-binding activity of the recombined molecule obtained by complementation of two fibrinolysin fragments of ovine prolactin.
The recombined molecule obtained by complementation of two fibrinolysin fragments of ovine prolactin (oPRL) has been characterized by radioimmunoassay and radioreceptor assay. The recombinant alone exhibits very low radioimmunoreactivity and radioreceptor activity. However, in the presence of excess fragment oPRL-(1-53), which does not compete with oPRL in either assay, the recombinant has 101% of the radioimmunoreactivity and only 13% of the radioreceptor activity. The result shows that the low activity of the recombinant when assayed alone is due to dissociation of the molecule. When the molecule is completely in the recombined form in the presence of excess oPRL-(1-53), it retains full immunoreactivity but only part of the radioreceptor activity.
Animals↗
Ovine prolactin: equilibrium characteristics of the recombinant molecule formed by noncovalent interaction of two fibrinolysin fragments by fluorescence polarization.
The equilibrium characteristics of the recombined molecule formed by noncovalent interaction of two fibrinolysin fragments of ovine prolactin (oPRL) have been studied with fluorescence polarization. Fluorescein isothiocyanate (isomer I) was used to label oPRL-(1-53), creating a fluorescent peptide indistinguishable from the unlabeled fragment in the complementation reaction with oPRL-(54-199). The dissociation constant of the recombinant prolactin was 0.144 microM at 30 degrees C, with a free energy of dissociation of 9.50 kcal/mol.
Animals↗