Fibrinogen and fibrin induce synthesis of proinflammatory cytokines from isolated peripheral blood mononuclear cells.

Fibrinogen in plasma includes three main fractions; high-molecular-weight (HMW)-fibrinogen, low-molecular-weight (LMW)-fibrinogen, and very-low-molecular-weight (LMW')-fibrinogen. During acute-phase conditions, plasma fibrinogen levels and the HMW-/LMW-fibrinogen ratio increase rapidly due to increased synthesis of HMW-fibrinogen. The consequences of elevated plasma fibrinogen levels and local deposition of fibrin in inflammatory tissues observed during acute-phase conditions are not clear.

A daily glass of red wine induces a prolonged reduction in plasma viscosity: a randomized controlled trial.

Moderate red wine consumption has been associated with decreased risk of coronary heart disease. Reduced plasma viscosity and fibrinogen levels have been launched as possible contributors to this risk reduction. The effect of moderate red wine consumption on plasma viscosity, however, has not been investigated in a prospective, randomized trial.

The viscosity of fibrinogen subfractions and of EDTA denatured fibrinogen do not differ from that of native fibrinogen.

Introduction: Fibrinogen is a major determinant of plasma viscosity. The increased risk of atherothrombotic disease associated with a high fibrinogen concentration may partly be attributed to its effect on viscosity. Since the ratio between the three main fibrinogen subfractions high molecular weight (HMW)-, low molecular weight (LMW)-, and very low molecular weight (LMW')-fibrinogen is altered during acute phase conditions, and an increased HMW/LMW-fibrinogen ratio is associated with increased thromboembolic risk, we have examined how these subfractions affect viscosity.

Influence of freeze-drying on the clotting properties of fibrinogen in plasma.

Freeze-dried plasma standards are often used to calibrate fibrinogen assays. Little is known, however, about the effect of freeze-drying on the clotting properties of fibrinogen. If these properties are altered, the use of freeze-dried calibration standards might influence the results obtained when applying clotting assays to determine fibrinogen concentrations.

Discrepancy between fibrinogen concentrations determined by clotting rate and clottability assays during the acute-phase reaction.

Assays based on clotting rate are commonly used as a routine method for determining the fibrinogen concentration in plasma. However, little is known about the influence of the acute-phase reaction on this assay. In order to disclose discrepancies between the fibrinogen concentrations obtained by a clotting rate assay (as described by Clauss) and a reference assay for total clottable protein (according to Jacobsson), we compared the fibrinogen concentrations determined by these two methods in plasma-samples collected preoperatively and on postoperative days 1, 3, and 5 in patients undergoing major elective surgery.

Degradation of fibrinogen and cross-linked fibrin by human neutrophil elastase generates D-like fragments detected by ELISA but not latex D-dimer test.

Recently, we observed that D-dimers are degraded by human neutrophil elastase (HNE) into two D-like fragments, reacting with the monoclonal antibody in an ELISA D-dimer test but not reacting with the corresponding latex D-dimer test. To investigate this in more detail, we studied the degradation of cross-linked fibrin and fibrinogen by plasmin and HNE to see if this resulted in D-fragments or D-like fragments. Degradation of fibrinogen, both by plasmin and HNE, resulted in D- and D-like fragments, respectively, detected by the ELISA D-dimer test.

Discrepancy between latex and ELISA D-dimer values in sepsis may be caused by human neutrophil elastase.

We have recently shown that D-dimers are degraded by human neutrophil elastase (HNE) in vitro, causing rapid decrease in the D-dimer levels measured by a Latex test, but not with an ELISA test employing the same monoclonal antibody against D-dimer. To see if such discrepant D-dimer concentrations occurred in patients with high HNE concentration, we examined 80 plasma samples from 8 patients with sepsis with a Latex and an ELISA test and calculated the ratio between the D-dimer values obtained with the two tests. Twenty healthy pregnant and twenty pre-eclamptic patients, who are known to have raised D-dimer but low HNE concentrations, were chosen as controls.

D-dimers are degraded by human neutrophil elastase.

To see if D-dimers were degraded by human neutrophil elastase (HNE), cross-linked fibrin was obtained by adding thrombin to purified fibrinogen in the presence of calcium ions and factor XIII, and the fibrin clot subsequently degraded by plasmin. Thereafter, the supernatant containing fibrin degradation products was removed and incubated with HNE. D-dimer levels were measured by two rapid semiquantitative tests, a latex agglutination test and the Nycocard immunofiltration test, and a quantitative ELISA-method.

Disseminated intravascular coagulation (DIC) in adult patients with acute leukaemia.

In 71 patients with acute leukaemia admitted for remission induction, disseminated intravascular coagulation (DIC) was looked for in 50 patients and diagnosed in 10 (20%). Of 10 patients with acute lymphoblastic leukaemia, 3 had DIC, and of 40 patients with acute myeloblastic leukaemia, 7 had DIC. The presence of DIC was related to bleeding manifestations within the first 2 weeks.

Degradation of the alpha-chain of fibrin by human neutrophil elastase reduces the stimulating effect of fibrin on plasminogen activation.

Unlabelled: The degradation of fibrin by human neutrophil elastase (HNE) and the interference of such degradation on the stimulating effect of fibrin on plasminogen activation by tissue plasminogen activator (t-PA) was studied. By using SDS electrophoresis and Western blotting with subsequent immunostaining with monoclonal antibodies, degradation of the fibrin molecule was monitored. This degradation was related to the stimulating effect on plasminogen activation.

Comparison of three D-dimer assays for the diagnosis of DVT:ELISA, latex and an immunofiltration assay (NycoCard D-Dimer).

Ninety-two consecutive patients referred for suspicion of deep venous thrombosis (DVT) were analyzed for D-dimer using ELISA, latex test, and a new immunofiltration method (NycoCard D-Dimer). Contrast venography verified the diagnosis in 40, and excluded the diagnosis in 52 patients. The sensitivity, negative predictive values, specificity and positive predictive values were, for ELISA 98%, 95%, 38% and 54, for NycoCard D-Dimer 100%, 100%, 42% and 57% and for the latex test 73%, 78%, 75%, and 69%, respectively.

Impaired coagulation of fibrinogen due to digestion of the C-terminal end of the A alpha-chain by human neutrophil elastase.

Human neutrophil elastase (HNE) possesses fibrinogenolytic capacity, with a high susceptibility towards degradation of the A alpha-chain. To study the influence of HNE digestion of the A alpha-chain on the coagulation of fibrinogen by thrombin, fibrinogen was incubated with human neutrophil elastase (HNE). At intervals, thrombin clotting time (TCT) and clottability were determined and compared with the patterns obtained with SDS electrophoresis and Western blotting with subsequent immunostaining, using monoclonal antibodies against the N-terminal end and C-terminal half of the A alpha-chain.

Thrombin treated plasma employed as a standard for determination of soluble fibrin.

The Coa-set Fibrin Monomer test (CFM-test) is a quantitative method for determination of soluble fibrin in plasma. The fibrin standard of the CFM-test is produced by bathroxobin conversion of purified fibrinogen to fibrin. Plasma treated with minute amounts of thrombin may be considered as a more physiological way of preparing fibrin monomers.

The stimulatory capacity of soluble fibrin prepared from high and low molecular weight fibrinogen on plasminogen activation.

High molecular weight, low molecular weight and very low molecular weight fibrinogen were purified from human plasma, and converted partially or completely to fibrin by the action of thrombin or batroxobin. The stimulatory effects of these fibrin(ogen) preparations on plasminogen activation by tissue plasminogen activator were studied. When only 3-30% of the fibrinogen molecules were converted to fibrin, the high molecular weight fibrin had a greater stimulatory effect on plasminogen activation than equal amounts of low and very low molecular weight fibrin.

Does Lp(a) lipoprotein inhibit the fibrinolytic system?

Lp(a) lipoprotein contains a unique apolipoprotein, apolipoprotein (a), that has a striking homology with plasminogen. This homology has brought forward speculations as to an inhibitory effect of Lp(a) lipoproteins on fibrinolysis. The present investigation was undertaken to study the influence of Lp(a) lipoprotein on the fibrinolytic system.

Fibrinolytic activity as a predictor of the outcome of prolapsed intervertebral lumbar disc surgery with reference to background variables: results of a prospective cohort study.

In a prospective study 122 patients with a slipped lumbar disc and no previous surgery were preoperatively examined for fibrinolytic activity. Surgical results for these patients were evaluated 12 months postoperatively by clinical overall assessment. In a multiple linear regression analysis fibrinolytic variables, euglobulin clot lysis time and plasminogen activator inhibitor 1, were shown to have predictive value regarding outcome of surgery; that is, normal fibrinolytic activity favors a satisfactory outcome and vice versa.

A novel principle for assessment of stimulated fibrinolysis.

After venous occlusion (VO), D-dimer levels were measured by means of an ELISA technique, in citrated plasma clotted by thrombin and in serum from whole blood. D-dimer levels increased with duration of incubation (30 min to 24 hours). D-dimer values, both in clotted plasma and in serum (n = 12), incubated 4 hours at room temperature, correlated well with euglobulin clot lysis time (ECLT) (r = -0.

The stimulatory effect of soluble fibrin on plasminogen activation by tissue plasminogen activator as studied by the Coa-set Fibrin Monomer test.

The stimulatory effect of various fibrin preparations on plasminogen activation by tissue plasminogen activator, was studied by the Coa-set Fibrin Monomer test (Kabi). Fibrin obtained by complete conversion of purified fibrinogen demonstrated a greater stimulatory effect on plasminogen activation than did equal amounts of fibrin obtained by partial conversion of fibrinogen. Soluble fibrin generated by treating human plasma with minute amounts of thrombin or bathroxobin, resembled partially converted purified fibrinogen.

Comparison of thrombin-antithrombin complex (TAT) levels and fibrinopeptide A following thrombin incubation of human plasma using hirudin as an inhibitor of TAT formation.

Following incubation of citrated plasma with human thrombin, the interaction of thrombin with antithrombin III was measured as thrombin-antithrombin complex (TAT) concentration. Comparison was made to thrombin activity on fibrinogen, assayed as fibrinopeptide A (FPA). Light scattering studies were included to evaluate polymerization of fibrin.

Comparison of methods for detecting soluble fibrin in plasma. An in vitro study.

The ability of the COA-SET Fibrin monomer (COA-SET FM) test to detect soluble fibrin was evaluated by comparing the results of the COA-SET FM test with fibrinopeptide A (FPA) determinations following thrombin incubation of plasma or whole blood. In addition, two semiquantitative tests (erythrocytes-agglutination test (FM-test) and ethanol gelation test (EGT] were included in the study. Under the experimental conditions used, the COA-SET FM test proved less sensitive than the FPA-assay.