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:3.4.21.6 (thromboplastin)
13,278 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Various haemostatic analytes were systematically evaluated for four months pre-partum and five months post partum in 14 healthy mares. The plasma fibrinogen concentration and both Factor VIII:C and von Willebrand factor activity showed gradual increases from mid-gestation and reached maximal, or near maximal activity at parturition. These increases were paralleled by an increase in plasma fibronectin concentration, the appearance of fibrinogen degradation products, and a modest rise in antithrombin III concentration. In contrast, the activity of Factor VII and Factor IX, and the one-stage prothrombin (PT) time and the activated partial thromboplastin (APTT) time remained relatively constant throughout the pre- and post parturient period.
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PMID:Evaluation of the haemostatic profile in the pre- and post parturient mare, with particular focus on the perinatal period. 155 43

We found a significantly higher plasma fibronectin concentration in a group of nine cirrhotic patients who underwent surgical treatment for portal hypertension (either shunting and non shunting procedures) when compared to twenty non operated patients. Significantly shorter prothrombin time and activated partial thromboplastin time in the operated patients were found as well. These results might be related to an increased breakdown of fibronectin during consumption coagulopathy taking place in the extended collaterals and reversed in part by surgical treatment of portal hypertension complicating liver cirrhosis.
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PMID:Normal fibronectin levels after surgical treatment of portal hypertension in liver cirrhosis. 169 89

Atherosclerotic lesions have been reported to contain herpes simplex virus (HSV) genomic material. This and other evidence suggests that latent viral infection may be an atherogenic trigger. Moreover, active HSV lesions manifest histologically marked fibrin deposition in microvessels. Our laboratory tested in vitro whether HSV infection would cause human umbilical vein endothelial cells to become procoagulant and attract inflammatory cells. Early infection of human endothelial cells with HSV-1 alters the surface conformation as detected by merocyanine 540 staining. The efficiency of prothrombinase complex assembly increases, resulting in a two- to threefold accelerated rate of thrombin generation on the cell surface of virally infected endothelium. HSV infection of endothelium results in a marked increase in thrombin-induced platelet adhesion with a concomitant decrease in prostacyclin secretion in response to thrombin. Viral infection enhances coagulation by decreasing endothelial thrombomodulin expression and subsequent activation of protein C. Viral infection also induces tissue factor in human endothelial cells within 4 hours of infection. Not only does the endothelial monolayer become procoagulant when infected with HSV, it also becomes a more adherent surface for granulocytes. Resting and stimulated granulocyte adherence is enhanced twofold on virally infected endothelium. Enhanced adhesion is accompanied by excessive granulocyte-mediated lysis of 51Cr-labeled HSV-infected endothelium and endothelial cell detachment from its substrate. Exaggerated endothelial detachment correlated with poor binding of infected endothelial cells to substratum matrix proteins. Resuspended virus-infected cells bound significantly less well to tissue culture containers coated with fibronectin, laminin, and type IV collagen. HSV-infected endothelium alters the anticoagulant properties of the endothelium causing it to become procoagulant.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Proinflammatory and procoagulant effects of herpes simplex infection on human endothelium. 219 Jun 48

Folate deficient murine B16 melanoma cells adhered more rapidly and in higher percentages to plastic plates or dishes coated with laminin or fibronectin than folate replete cells. These changes in the adhesive properties of murine melanoma cells induced by nutritional folate deficiency were not mediated by changes in cell size, proliferative capacity or cell cycle distribution. While melanoma cells served as a suitable surface for prothrombinase complex formation, folate deficiency did not alter this membrane function, suggesting that the membrane changes associated with folate deficiency are relatively specific.
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PMID:Effects of nutritional folate deficiency on the adhesive properties of murine melanoma cells. 226 19

Hemostatic function was determined in 10 ponies at various times after inoculation with Ehrlichia risticii to determine whether equine ehrlichial colitis (EEC) caused changes in the hemostatic system and to determine the prognostic value of hemostatic function tests during EEC. Mean platelet count; plasma fibrinogen, fibronectin, factor VIII: coagulant, alpha 2-antiplasmin, and plasminogen values; and serum concentrations of fibrin/fibrinogen degradation products changed significantly (P less than 0.05) from base line (day 0, before inoculation) during 18 days after inoculation with E risticii. Four ponies that died or were euthanatized because of severe clinical signs of EEC had significantly (P less than 0.05) greater mean plasma fibrinogen concentrations plasma factor VIII:coagulant values, and activated partial thromboplastin times immediately before death than did the 6 surviving ponies. Factor V concentrations were significantly (P less than 0.05) lower on postinoculation days 10 and 20 in nonsurvivors. Seemingly, changes in hemostasis took place during EEC. Ponies that did not survive EEC had greater laboratory evidence of coagulopathy.
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PMID:Effect of equine ehrlichial colitis on the hemostatic system in ponies. 313 29

Six coagulation proteins were measured in 79 consecutive patients referred to the coagulation service for suspected disseminated intravascular coagulation. Antithrombin III, plasminogen, and alpha 2-plasmin inhibitor were measured with fluorescent substrate assays. Fibronectin, prothrombin, and protein C were measured with electroimmunoassays. Using history and physical findings and the results of a coagulation screen (prothrombin time, partial thromboplastin time, fibrinogen, fibrin[ogen] degradation products, platelet count, and peripheral smear), the 79 patients were classified into five categories: no disseminated intravascular coagulation (n = 21), elevated fibrin(ogen) degradation products without other evidence of coagulopathy (n = 44), defibrination syndrome (n = 9), microangiopathic thrombocytopenic purpura (n = 4), and primary fibrinolysis (n = 1). Because the sensitivity and specificity of each of the proteins could not easily be compared, receiver operating characteristic (ROC) curves and areas under the ROC curves were calculated for each of the six proteins as well as for the tests of the coagulation screen. The ROC curves indicated that, apart from plasminogen, the other coagulation proteins provided little additional information about the classification of the coagulopathy.
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PMID:Diagnostic efficacy of six plasma proteins in evaluating consumptive coagulopathies. Use of receiver operating characteristic curves to compare antithrombin III, plasminogen, alpha 2-plasmin inhibitor, fibronectin, prothrombin, and protein C. 376 44

Orgaran is a LMW heparinoid composed of heparan sulphate (83% w/w) of which 4-5% has high affinity for antithrombin, dermatan sulphate (12% w/w) and chondroitin sulphate (5% w/w). To examine the contribution of the low-affinity fraction to Orgaran's antithrombotic activity we have quantitated the binding of plasma proteins to Orgaran and its component fractions in whole, hirudin-anticoagulated human plasma. Antithrombin, largely bound to the high-affinity fraction, and histidine-rich glycoprotein, interacting with low-affinity components, were the dominant proteins bound to Orgaran. Vitronectin, fibrinogen, fibronectin, heparin cofactor II, and apolipoprotein B were also detected in small amounts. The ratio of bound antithrombin, histidine-rich glycoprotein and vitronectin to GAG was negatively correlated with the Orgaran concentration in plasma, implying that the efficacy of Orgaran may not be linearly related to dose. Binding of antithrombin to the high-affinity fraction was not decreased by other plasma proteins or affected by addition of low-affinity material. Moreover, the antithrombin and anti-factor Xa activities of the high-affinity material were unaltered by low-affinity GAGs. On the basis of our results we conclude that the low-affinity material does not contribute to the antithrombotic activity of Orgaran by binding non-anticoagulant plasma proteins and releasing the high-affinity chains to interact with antithrombin and its target proteinases.
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PMID:Low-affinity material does not contribute to the antithrombotic activity of Orgaran (Org 10172) in human plasma. 752 81

This study evaluated the haemostatic profiles of a group of 11 female and seven male calves from the day of birth until they were 60 days of age. Similar results were found for both sexes. At birth the plasma activity of the procoagulant proteins, Factors VII, VIII:C, IX, X and XI and fibrinogen were all close to the adult values. Factors VII, VIII:C and fibriogen increased transiently during the first seven days of life but the increases were not sufficient to influence routine coagulation screening assays such as the activated partial thromboplastin time and the prothrombin time. At birth, the plasma concentration of the protease inhibitor, alpha 2-macroglobulin, was approximately 50 per cent of adult values and increased slowly during the first seven days of life; the plasma concentration of antithrombin III was higher than that of alpha 2-macroglobulin. The changes in the plasma concentration of fibronectin paralleled the changes in fibrinogen and Factor VIII:C from birth to 60 days of age; the concentrations of total plasma protein and plasma albumin remained stable and within the adult ranges throughout the 60 days. The plasma concentration of glucose increased transiently during the first 48 hours after birth.
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PMID:Competency of blood coagulation in the newborn calf. 787 Dec 54

Factor IX is a vitamin K-dependent procoagulant zymogen of a serine protease. In the presence of Ca2+ the active form of factor IX (factor IXa beta) forms a complex with factor VIIIa on suitable phospholipid surfaces such as aggregated platelets. This macromolecular complex rapidly activates factor X. We have previously provided data that suggest an interaction between the NH2-terminal epidermal growth factor (EGF)-like module of factor IXa beta and the substrate factor X. In an alternative approach to study this protein-protein interaction, we have expressed three recombinant baculovirus constructs encoding the EGF-like modules of human factor IX and a truncated form of fibronectin in a system based on the infection of insect cells (Spodoptera frugiperda 21). This strategy allows a simple one-step purification of the recombinant proteins on a gelatin-Sepharose column, followed by removal of the gelatin-binding part derived from fibronectin by proteolytic cleavage. The fusion proteins were isolated at yields of 20-50 micrograms/ml culture medium. The recombinant EGF-like modules contained 0.2-0.4 mol of erythro-beta-hydroxyaspartic acid/mol of protein, i.e. similar to the amount found in factor IX from human plasma, and appeared to be glycosylated at Ser-53. The NH2-terminal EGF-like module, which contained a transamidation acceptor site derived from fibronectin, was cross-linked by factor XIIIa in solution to intact and Gla-domainless factor X. There was no evidence of cross-linking to activated factor X or to factor X fragments containing only the gamma-carboxyglutamic acid module and the two EGF-like modules. The cross-linking results suggest a specific interaction between the NH2-terminal EGF-like module of factor IXa beta and the heavy chain of unactivated factor X. This interaction, albeit weak as judged by competition experiments, may be important for the targeting of factor X to the factor IXa beta-factor VIIIa complex on biological membranes and for the subsequent dissociation of factor Xa from the complex after activation.
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PMID:Baculovirus-mediated expression of the epidermal growth factor-like modules of human factor IX fused to the factor XIIIa transamidation site in fibronectin. Evidence for a direct interaction between the NH2-terminal epidermal growth factor-like module of factor IXa beta and factor X. 790 69

To assess the effect of interleukin-6 (IL-6) on the coagulation and the fibrinolytic systems, we administered a single subcutaneous injection of recombinant glycosylated human interleukin-6 (r-hIL-6) 100 micrograms per kg body weight) to four baboons (Papio ursinus). Four saline injected baboons served as controls. In serial plasma or serum samples collected over a period of seven days we measured several key parameters of the coagulation and the fibrinolytic systems, IL-6 and a set of acute phase proteins. Three hours after the injection, the serum IL-6 levels peaked at 50 ng/ml and then gradually declined with a terminal half-life of around 4 hours. The biological efficacy was demonstrated by the significant increases of several acute phase proteins, circulating platelets and the decrease of prealbumin and fibronectin. Between days 1 and 3, marked effects on the coagulation system were observed with a prolongation of the activated partial thromboplastin time, prothrombin time and thrombin time. Plasma concentrations of fibrinopeptide A and D-dimer increased. The antithrombin III antigen and activity levels decreased, but the thrombin-antithrombin III complex concentrations did not change. The fibrinolytic system rapidly showed striking modifications after 6-8 hours, the concentrations of tissue-type plasminogen activator and of plasminogen activator inhibitor type 1 peaked at respectively four and thirty times the basal concentrations. No changes were seen in the control group. We conclude that besides its well-known acute phase inducing and hematopoietic activities, subcutaneous rhIL-6 also modulates several parameters of the coagulation and the fibrinolytic systems.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:In vivo modulation of coagulation and fibrinolysis by recombinant glycosylated human interleukin-6 in baboons. 794 65


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