A HEP ARINE-LIKE ANTICOAGULANT IN A PATIENT WITH WEGENER’S GRANULOMATOSIS

1987 ◽  
Author(s):  
L Chrobák ◽  
V Rozsíval ◽  
V Herout
Keyword(s):  
Wegener’S Granulomatosis ◽  
Wegener's Granulomatosis ◽  
Thrombin Time ◽  
Protamine Sulphate ◽  
Normal Limits ◽  
Significant Prolongation ◽  
Lysis Time ◽  
Coagulation Tests

In a 23-year-old man with Wegener’s granulomatosis and mild bleeding coagulation studies revealed a significant prolongation of the coagulation time (CT) prothrombin time (PT), activated partial thromboplastin time (aPTT), thrombin time (TT), failure of TT and aPTT to correct in a 1:1 mixture with pooled normal plasma (PNP), correction of the prolonged TT with toluidine blue and correction of TT and aPTT both in vitro and in vivo^protamine sulphate (P.S.).All other coagulation tests, i.e.,bleeding time, platelet count? fibrinogen level, euglobulme lysis time were within normal limits. The patient did not receive heparine. TT after administration of 5ml of protamine sulphate i.v. to the patient became normal - 18,2 s (19,7 s).In summary a patient with Wegener s granulomatosis associated with an endogenous heparine-like anticoagulant is reported. The anticoagulant could be corrected both in vitro and in vivo by protamine sulphate.

ASPIRIN ACETYLATES FIBRINOGEN AND ENHANCES FIBRINOLYSIS IN VIVO. FIBRINOLYTIC EFFECT IS INDEPENDENT OF CHANGES IN PLASMINOGEN ACTIVATOR LEVELS

1987 ◽  
Author(s):  
D Thorir ◽  
M D Bjornsson ◽  
Henry Berger
Keyword(s):  
Plasminogen Activator ◽  
Time Course ◽  
Clot Lysis ◽  
Thrombin Time ◽  
Lysis Time ◽  
Coagulation Tests ◽  
Clot Lysis Time ◽  
Increased Susceptibility

In addition to its antiplatelet effect, aspirin has been reported to have fibrinolytic and hypoprothrombinémie effects. The objective of this study was to investigate possible mechanisms underlying the enhanced fibrinolysis observed after aspirin. Five healthy subjects received 650 mg of aspirin ql2hr for five days. Blood samples were collected before aspirin (control) and immediately before (0 hr) and two hours after (2 hr) the last dose for determinations of clot lysis time, time course of thrombin-induced fibrin aggregation, tissue plasminogen activator (tPA), intrinsic pathway fibrinolytic activity (IPFA), plasminogen, fibrinogen, aspirin and salicylic acid, and the coagulation tests activated partial thromboplastin time, thrombin time and prothrombin time. Clot lysis time was shorter after aspirin, control: 9.1±12.4 min (mean±s.d.), 0 hr: 4.6±4.0 min, 2 hr: 5.7±6.2 min (p:0.04), and the fibrin aggregation curves showed increased turbidity (expressed as AUC over 10 min), control: 72.7±17.8 mnumin, 0 hr: 94.6±1.6 mnumin, 2 hr: 112.8±45.1 mnumin (p:0.02). Control values of tPA (0.11±0.04 IU/ml), IPFA (2.20±0.59 IU/ml), plasminogen (10.9±1.0 mg/dl), fibrinogen (288±37 mg/dl), and the coagulation tests were not differnet from those after aspirin. Plasma aspirin concentrations were below detection limits at 0 hr and averaged 1.63±0.97μg/ml at 2 hr. In vitro studies using fibrinogen-free plasma and added acetylated fibrinogen sfiowed an inverse relationship between the extent of acétylation and clot lysis time. Studies using 14C-acetyl-labeled aspirin and fibrinogen showed that fibrinogen is acetylated to form ε-N-acetyl-lysine on both D and E domains of the molecule (50.6±2.0 and 49.4±2.0%, respectively) and on α β and γchains of the molecule (34.4±1.6, 30.7±3.4 and 34.9±4.7%, respectively), with preferential acétylation on the E domain. On the average, 2.88±1.49 ε-N-acetyl-lysyl residues were formed on each fibrinogen molecule. These results suggest that N-acetylation of lysyl residues of fibrinogen is responsible for the increased susceptibility of fibrin clots to lysis after aspirin.

Anticoagulant Properties of Three Mucopolysaccharides Used in Rheumatology

1983 ◽  
Vol 50 (03) ◽  
pp. 652-655 ◽  
Author(s):  
F Bauer ◽  
P Schulz ◽  
G Reber ◽  
C A Bouvier
Keyword(s):  
Factor Xa ◽  
Degenerative Joint Disease ◽  
Joint Disease ◽  
Thrombin Time ◽  
Coagulation Tests ◽  
Amplification System ◽  
Relative Potencies ◽  
In Vivo Administration

SummaryThree mucopolysaccharides (MPS) used in the treatment of degenerative joint disease were compared to heparin to establish their relative potencies on 3 coagulation tests, the aPTT, the antifactor X a activity and the dilute thrombin time. One of the compounds, Arteparon®, was one fourth as potent as heparin on the aPTT, but had little or no influence on the 2 other tests. Further in vitro studies suggested that Arteparon® acted at a higher level than factor Xa generation in the intrinsic amplification system and that its effect was independent of antithrombin III. In vivo administration of Arteparon® confirmed its anticoagulant properties, which raises the question of the clinical use of this MPS.

scholarly journals Neutrophil activation in vitro and in vivo in Wegener's granulomatosis

1994 ◽  
Vol 45 (4) ◽  
pp. 1120-1131 ◽  
Author(s):  
Elisabeth Brouwer ◽  
Minke G. Huitema ◽  
A.H. Leontine Mulder ◽  
Peter Heeringa ◽  
Harry van Goor ◽  
...  
Keyword(s):  
Wegener’S Granulomatosis ◽  
Wegener's Granulomatosis ◽  
Neutrophil Activation

Effects of Bradykinin on Coagulation and Fibrinolysis Study in Vitro and in Vivo

1965 ◽  
Vol 14 (03/04) ◽  
pp. 508-518 ◽  
Author(s):  
G. G Neri Serneri ◽  
P. L Rossi Ferrini ◽  
P Paoletti ◽  
A Panti ◽  
G D’Ayala Valva
Keyword(s):  
Thrombin Generation ◽  
Thrombin Time ◽  
Lysis Time ◽  
Time Determination ◽  
Recalcification Time ◽  
Generation Test ◽  
Coagulation And Fibrinolysis

SummaryThe effects of bradykinin on coagulation and fibrinolysis have been studied both “in vitro” and “in vivo” in man. “In vitro” bradykinin employed at different concentrations does not affect the coagulation and fibrinolysis processes in any appreciable way. Bradykinin, intraarterially injected in man in the dose of 10 y, does not modify coagulation studied both with global investigations (thrombelastogram, recalcification time) and with analytical researches (Quick’s time, activation test of intrinsic thromboplastin, thrombin generation test and thromboplastin test, thrombin time, determination of antithrombin II and III). Bradykinin instead produces an activation of fibrinolysis both in the thrombelastographic investigation and in the lysis time of euglobulins. The decrease in the activity of the proactivator and of plasminogen supports our view that bradykinin produces an activation of the fibrinolytic system by liberating tissue kinases which act on the proactivator. The authors have discussed the physiological and physiopathological significance of the observed findings.

Effects of Heparin Oligosaccharides with High Affinity for Antithrombin III in Experimental Venous Thrombosis

1982 ◽  
Vol 47 (03) ◽  
pp. 244-248 ◽  
Author(s):  
D P Thomas ◽  
Rosemary E Merton ◽  
T W Barrowcliffe ◽  
L Thunberg ◽  
U Lindahl
Keyword(s):  
Antithrombin Iii ◽  
Specific Activity ◽  
High Specific Activity ◽  
Factor Xa ◽  
Blood Levels ◽  
Thrombin Time ◽  
High Affinity ◽  
Very High

SummaryThe in vitro and in vivo characteristics of two oligosaccharide heparin fragments have been compared to those of unfractionated mucosal heparin. A decasaccharide fragment had essentially no activity by APTT or calcium thrombin time assays in vitro, but possessed very high specific activity by anti-Factor Xa assays. When injected into rabbits at doses of up to 80 ¼g/kg, this fragment was relatively ineffective in impairing stasis thrombosis despite producing high blood levels by anti-Xa assays. A 16-18 monosaccharide fragment had even higher specific activity (almost 2000 iu/mg) by chromogenic substrate anti-Xa assay, with minimal activity by APTT. When injected in vivo, this fragment gave low blood levels by APTT, very high anti-Xa levels, and was more effective in preventing thrombosis than the decasaccharide fragment. However, in comparison with unfractionated heparin, the 16-18 monosaccharide fragment was only partially effective in preventing thrombosis, despite producing much higher blood levels by anti-Xa assays.It is concluded that the high-affinity binding of a heparin fragment to antithrombin III does not by itself impair venous thrombogenesis, and that the anti-Factor Xa activity of heparin is only a partial expression of its therapeutic potential.

scholarly journals Coagulation under Mild Hypothermia Assessed by Thromboelastometry

2021 ◽  
pp. 1-7
Author(s):  
Tobias Nitschke ◽  
Philipp Groene ◽  
Alice-Christin Acevedo ◽  
Tobias Kammerer ◽  
Simon T. Schäfer
Keyword(s):  
Mild Hypothermia ◽  
Onset Time ◽  
Rotational Thromboelastometry ◽  
Lysis Time ◽  
Sample Data ◽  
In Vivo Testing ◽  
Fibrinolytic Capacity ◽  
Clot Formation Time

<b><i>Introduction:</i></b> While previous studies have shown a significant impact of extreme hypo- and hyperthermia on coagulation, effects of much more frequently occurring perioperative mild hypothermia are largely unknown. This study therefore aimed to analyze the effects of mild hypothermia using rotational thromboelastometry in vitro. <b><i>Materials and Methods:</i></b> Twelve healthy volunteers were included in this study. Standard thromboelastometric tests (EXTEM, INTEM, FIBTEM) were used to evaluate coagulation in vitro at 39, 37, 35.5, 35, and 33°C. Beyond standard thromboelastometric tests, we also evaluated the effects of mild hypothermia on the TPA-test (ClotPro, Enicor GmbH, Munich, Germany), a new test which aims to detect fibrinolytic capacity by adding tissue plasminogen activator to the sample. Data are presented as the median with 25/75th percentiles. <b><i>Results:</i></b> Extrinsically activated coagulation (measured by EXTEM) showed a significant increase in clot formation time (CFT; 37°C: 90 s [81/105] vs. 35°C: 109 s [99/126]; <i>p</i> = 0.0002), while maximum clot firmness (MCF) was not significantly reduced. Intrinsically activated coagulation (measured by INTEM) also showed a significant increase in CFT (37°C: 80 s [72/88] vs. 35°C: 94 s [86/109]; <i>p</i> = 0.0002) without significant effects on MCF. Mild hypothermia significantly increased both the lysis onset time (136 s [132/151; 37°C] vs. 162 s [141/228; 35°C], <i>p</i> = 0.0223) and lysis time (208 s [184/297; 37°C] vs. 249 s [215/358; 35°C]; <i>p</i> = 0.0259). <b><i>Conclusion:</i></b> This demonstrates that even under mild hypothermia coagulation is significantly altered in vitro. Perioperative temperature monitoring and management are greatly important and can help to prevent mild hypothermia and its adverse effects. Further investigation and in vivo testing of coagulation under mild hypothermia is needed.

scholarly journals Anticoagulant Properties of a Green Algal Rhamnan-type Sulfated Polysaccharide and Its Low-molecular-weight Fragments Prepared by Mild Acid Degradation

Marine Drugs ◽  
2018 ◽  
Vol 16 (11) ◽  
pp. 445 ◽  
Author(s):  
Xue Liu ◽  
Peng Du ◽  
Xiao Liu ◽  
Sujian Cao ◽  
Ling Qin ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Anticoagulant Activity ◽  
Sulfated Polysaccharide ◽  
Low Molecular Weight ◽  
Thrombin Time ◽  
Acid Degradation ◽  
Molecular Weights ◽  
Green Algal

The active sulfated polysaccharide from seaweed possesses important pharmaceutical and biomedical potential. In the study, Monostroma sulfated polysaccharide (MSP) was obtained from Monostroma angicava, and the low-molecular-weight fragments of MSP (MSP-Fs: MSP-F1–MSP-F6) were prepared by controlled acid degradation. The molecular weights of MSP and MSP-F1–MSP-F6 were 335 kDa, 240 kDa, 90 kDa, 40 kDa, 24 kDa, 12 kDa, and 6.8 kDa, respectively. The polysaccharides were sulfated rhamnans that consisted of →3)-α-l-Rhap-(1→ and →2)-α-l-Rhap-(1→ units with partial sulfation at C-2 of →3)-α-l-Rhap-(1→ and C-3 of →2)-α-l-Rhap-(1→. Anticoagulant properties in vitro of MSP and MSP-F1–MSP-F6 were evaluated by studying the activated partial thromboplastin time, thrombin time, and prothrombin time. Anticoagulant activities in vivo of MSP and MSP-F4 were further evaluated; their fibrin(ogen)olytic activities in vivo and thrombolytic properties in vitro were also assessed by D-dimer, fibrin degradation products, plasminogen activator inhibitior-1, and clot lytic rate assays. The results showed that MSP and MSP-F1–MSP-F4 with molecular weights of 24–240 kDa had strong anticoagulant activities. A decrease in the molecular weight of MSP-Fs was accompanied by a decrease in the anticoagulant activity, and higher anticoagulant activity requires a molecular weight of over 12 kDa. MSP and MSP-F4 possessed strong anticoagulant activities in vivo, as well as high fibrin(ogen)olytic and thrombolytic activities. MSP and MSP-F4 have potential as drug or helpful food supplements for human health.

scholarly journals Effect ofToona microcarpaHarms Leaf Extract on the Coagulation System

2014 ◽  
Vol 2014 ◽  
pp. 1-7 ◽  
Author(s):  
Hao Chen ◽  
Min Jin ◽  
Yi-Fen Wang ◽  
Yong-Qing Wang ◽  
Ling Meng ◽  
...  
Keyword(s):  
Leaf Extract ◽  
Factor Xa ◽  
Adenosine Diphosphate ◽  
Coagulation System ◽  
Dependent Manner ◽  
Thrombin Time ◽  
Antithrombotic Agent ◽  
Thrombin Activity

Toona microcarpaHarms is a tonic, antiperiodic, antirheumatic, and antithrombotic agent in China and India and an astringent and tonic for treating diarrhea, dysentery, and other intestinal infections in Indonesia. In this study, we prepared ethyl-acetate extract from the air-dried leaves ofToona microcarpaHarms and investigated the anticoagulant activitiesin vitroby performing activated partial thromboplastin time (APTT), prothrombin time (PT), and thrombin time (TT) assays. Antiplatelet aggregation activity of the extract was examined using adenosine diphosphate (ADP), collagen, and thrombin as agonists, and the inhibitions of factor Xa and thrombin were also investigated. Bleeding and clotting times in mice were used to determine its anticoagulant activitiesin vivo. It is found thatToona microcarpaHarms leaf extract (TMHE) prolonged APTT, PT, and TT clotting times in a dose-dependent manner and significantly inhibited platelet aggregation induced by thrombin, but not ADP or collagen. Clotting time and bleeding time assays showed that TMHE significantly prolonged clotting and bleeding timesin vivo. In addition, at the concentration of 1 mg/mL, TMHE inhibited human thrombin activity by 73.98 ± 2.78%. This is the first report to demonstrate that THME exhibits potent anticoagulant effects, possibly via inhibition of thrombin activity.

COAGULATION ABNORMALITIES IN LEAD EXPOSED RATS

1987 ◽  
Author(s):  
Narendra Kumar Satija ◽  
Har Bhajan Singh ◽  
Anjana Grover ◽  
Ram Mohan Rai
Keyword(s):  
Modern Technology ◽  
Environmental Pollutant ◽  
The Body ◽  
Albino Rats ◽  
Thrombin Time ◽  
Significant Prolongation ◽  
Lysis Time ◽  
Industrial Material ◽  
Euglobulin Lysis Time ◽  
Plasma Recalcification Time

The accelerated rate of development of modern technology has greatly expanded the range of health hazards. Lead, a widely used industrial material, is a significant environmental pollutant that contaminates food, water, soil and air. Although much progress has been made in elucidating its adverse effects on various systems of the body like hepatic, CNS, renal etc., its effect on coagulation remains to be established. In view of this an experimental study was carried out in animals to understand how lead influences hemostasis.Male albino rats were exposed to lead either acutely by administering 20 mg lead acetate per kg body weight daily i.p. for 3 days or chronically by administering lead through drinking water containing 5 ppm lead for 150 days. Acute exposure to lead caused severe coagulopathy characterized by significant prolongation of plasma recalcification time, decrease in platelet count and decreased wall adherence of blood, decreased fibrinogen and euglobulin lysis time and significant increase in prothrombin time, thrombin time, and partial thromboplastin time. Similar observations were found in chronically exposed animals. It is concluded that exposure to heavy metals like lead may lead to a state of hypocoagulability.

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