MODIFICATION OF COAGULATION AND FIBRINOLYSIS DURING TRANSLUMINAL ANGIOPLASTY IN PATIENTS RECEIVING HEPARIN OR PENTOSAN POLYSULFATE (HEMOCLAR)

1987 ◽  
Author(s):  
N Bel Lakhal ◽  
J M Pernes ◽  
D Lichtenstein ◽  
M Roncato ◽  
J C Gaux ◽  
...  
Keyword(s):  
Degradation Products ◽  
Transluminal Angioplasty ◽  
Thrombin Time ◽  
Pentosan Polysulfate ◽  
Heparin Group ◽  
Lysis Time ◽  
Before And After ◽  
Euglobulin Lysis Time ◽  
Thrombotic Complications ◽  
To Receive

Twenty patients with high stenosis of iliac or femoral artery were randomely allocated to receive by intra arterial route (IA) either 5,000 IU heparin or 50 mg Hemoclar immediately before starting the angioplasty. Those receiving Hemoclar were given a second IA 50 mg bolus at the end of the dilatation.Two blood samples were obtained by venous punction 1) after an initial 30 min resting (V1), 2) at the end of the procedure (V2)- Arterial punction by the dilatation catheter was also performed immediately before and after the dilatation leading to two other samples A1 and A2 The coagulation studies include activated partial thromboplastin time (APTT), thrombin time (TT), hep test (Hemachem, St-Louis, USA), anti Xa activity (Stachrom heparin, Diagnostica-Stago Asnieres, France). There was a significant increase in APTT, TT, and hep test between A1 and A2 as well as V1 and V2 in both groups of patients. However, the prolongation was significantly higher for heparin. Anti Xa activity significantly increased only in heparin group.Fibrinolysis was studied by measuring tPA by the SOFIA assay described by Angles-Cano (Anal. Biochem. 1985, 153, 201), euglobulin lysis time (ELT) and a new plasma ELISA assay specific for fibrinogen degradation products (FDPs) using monoclonal antibody described at the Gaubius Institute (Blood 1985, 66, 503). A significant increase in tPA was observed during the dilatation (A2/A1) and V2/V1) only in the patients receiving Hemoclar. The slight increase of the fibrinolytic activity was further corroborated by a significant increase in FDPs (A2/A1). In both groups, but only in the venous samples (V2/V1), ELT was shortened (p<0.05) and fibrinogen was decreased (p<0.05)No thrombotic complications were observed during the procedure in both groupsConclusion: This study confirms that Hemoclar has an inhibiting effect on coagulation by inhibiting thrombin and thrombin generation, but no anti Xa activity. However, the anticoagulant potency is much reduced when compared to heparin. The profibrinolytic effect seems to be related to the release of free tPA.

Lack of fibrin formation in exercise-induced activation of coagulation

1979 ◽  
Vol 236 (4) ◽  
pp. H577-H579 ◽  
Author(s):  
A. Vogt ◽  
V. Hofmann ◽  
P. W. Straub
Keyword(s):  
Physical Exercise ◽  
Degradation Products ◽  
Bicycle Ergometer ◽  
Strenuous Exercise ◽  
Thrombin Time ◽  
Fibrinopeptide A ◽  
Lysis Time ◽  
Exercise Period ◽  
Euglobulin Lysis Time ◽  
Exercise Induced

Strenuous physical exercise leads to a significant shortening of blood clotting in various test systems. Such short times are also characteristic of those observed in sedentary patients with thrombosis or disseminated intravascular coagulation, and of those observed in experimental animals after thrombin infusion. The patients exhibit an increase in circulating fibrinopeptide A, which is attributed to thrombin action on circulating fibrinogen, and to an increase of fibrinogen degradation products, which is thought to indicate reactive fibrinolysis. To check whether physical exercise leads to fibrinemia, 10 healthy male volunteers were subjected to strenuous exercise on a bicycle ergometer. Blood samples were taken immediately before and on completion of the exercise period. Despite a significant shortening of the activated partial thromboplastin time, the thrombin time, and the Reptilase time, no increase of fibrinopeptide A could be demonstrated and the ethanol gelation test remained consistently negative. Simultaneously, the euglobulin lysis time was significantly shortened, whereas the fibrin(ogen) degradation products did not increase. The results indicate that the shortening of the coagulation times associated with physical exercise must be explained by mechanisms other than thrombin-mediated conversion of fibrinogen to fibrin.

The Amidolytic Activity of the SK-Plasminogen Complex Is Enhanced by a Potentiator which Is Generated in the Presence of Vascular Plasminogen Activator - Role of Fibrin Degradation Products

1982 ◽  
Vol 47 (03) ◽  
pp. 193-196 ◽  
Author(s):  
J Soria ◽  
C Soria ◽  
O Bertrand ◽  
F Dunn ◽  
M Samama ◽  
...  
Keyword(s):  
Plasminogen Activator ◽  
Degradation Products ◽  
Venous Stasis ◽  
Amidolytic Activity ◽  
Fibrin Degradation Products ◽  
Lysis Time ◽  
Before And After ◽  
Euglobulin Lysis Time ◽  
High Responders

SummaryIn the presence of an excess of streptokinase (SK) the amidolytic activity of the plasminogen-SK complex on chromogenic substrates is 12% lower in serum than in the corresponding plasma. However, in subjects in whom venous stasis lead to a shortening of the euglobulin lysis time to less than 60 min (high responders), the amidolytic activity of the plasminogen-SK complex in serum was 60% higher than in the corresponding plasma. Attempts to find alterations of the plasminogen molecule itself which would account for the enhanced activity in high responder serum were negative. No free plasmin was present and the plasminogens isolated from plasma and serum before and after venous stasis had the same amidolytic activity as glu-plasminogen in the presence of an excess of SK. N-terminal analysis of these four plasminogens revealed in each instance glutamic acid.The enhancement of the amidolytic activity of the SK-plasminogen complex in serum of high responders (potentiator activity) could be reproduced by adding purified tissue plasminogen activator (TA) to native blood before clotting, but not if TA was added to plasma or to prestasis serum. Removal of fibrin degradation products from poststasis serum resulted in the disappearance of potentiator activity. These experiments suggest that fibrin degradation products, generated during clotting in the presence of vascular or tissular plasminogen activator act as a potentiator of the amidolytic activity of the plasminogen SK-complex.

Coagulation Abnormalities in Dogs with Neoplastic Disease

1980 ◽  
Vol 44 (01) ◽  
pp. 035-038 ◽  
Author(s):  
Bruce R Madewell ◽  
Bernard F Feldman ◽  
Sharron O’Neill
Keyword(s):  
Clinical Evidence ◽  
Degradation Products ◽  
Blood Film ◽  
Neoplastic Disease ◽  
Thrombin Time ◽  
Laboratory Methods ◽  
Fibrin Degradation Products ◽  
Lysis Time ◽  
Coagulation Tests ◽  
Euglobulin Lysis Time

SummaryConventional laboratory methods were used to screen untreated tumor-bearing dogs for hemostatic abnormalities. Excluded from study were dogs with clinical evidence of bleeding. The primary site for neoplastic disease in 100 dogs studied included hemolymphatic system, skin, bone, thyroid gland, oropharynx, mammary gland, and nasal cavity.Eighty-three percent of the dogs had one or more abnormal coagulation tests. Thrombocytopenia occurred in 36 dogs and 3 had thrombocytosis. Twenty-five dogs had hypofibrinogenemia, and 25 had hyperfibrinogenemia. There were 32 dogs with prolongation of the activated partial thromboplastin time, 10 dogs with shortened prothrombin time, and 6 dogs with prolongation of the thrombin time. Sixteen dogs had positive protamine sulfate (paracoagulation) reaction, and 8% had increased plasma fibrin degradation products. The euglobulin lysis time was accelerated in 24% of the dogs, and 15% had schistocytes on blood film.These data indicate that the majority of dogs with advanced neoplasms are likely to have abnormal coagulation tests.

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.

Warfarin Induced Fibrinolysis: The Effect Of Recovery With And Without Vitamin K

1981 ◽  
Author(s):  
N A Marsh
Keyword(s):  
Prothrombin Time ◽  
Plasminogen Activator ◽  
Vitamin K ◽  
Dynamic Equilibrium ◽  
Degradation Products ◽  
Direct Action ◽  
Plasma Fibrinogen ◽  
Clotting Factors ◽  
Lysis Time ◽  
Euglobulin Lysis Time

We have previously shown that fibrinolysis in the rat is enhanced by levels of warfarin administration sufficient to produce moderate anticoagulation. This effect is mediated largely by an increase in plasma plasminogen activator. Plasminogen levels are decreased and fibrin(ogen) degradation products raised confirming the presence of a systemic hyperfibrinolytic state. In order to investigate this phenomenon further we have measured fibrinolytic components in rats recovering from warfarin administration. Groups of male Hooded rats received 14 yg warfarin/100 g body weight /day by mouth for one to two weeks. The animals were then allowed to recover without further treatment or following a single 50 μg dose of vitamin K1. Euglobulin lysis time, one stage prothrombin time, plasma plasminogen activator (fibrin plate method), plasma plasminogen (caseinolytic method), plasma fibrinogen (clot weight method) and plasma fibrinolytic inhibitors were measured at intervals after the end of the warfarin treatment. In animals recovering without vitamin K prothrombin time returned to normal within one week. However fibrinolysis remained elevated with plasma plasminogen activator concentrations of more than twice the control value. Plasma inhibitor levels were depressed and fibrinogen levels elevated. After two weeks all fibrinolytic components had returned to normal. Following vitamin Kj administration a different pattern emerged; prothrombin time returned to normal within 24 hours but fibrinolysis was diminished. The latter effect was due to a marked increase in plasma fibrinogen and moderate fall in plasma plasminogen activator both of which contributed to a prolonged euglobulin lysis time. These results indicate that fibrinolysis and coagulation in the rat are not linked in a 'dynamic equilibrium' like that proposed for man. The enhanced fibrinolysis rather than being a result of the fall in vitamin K dependant clotting factors may be due to the direct action of warfarin. The 'fibrinolytic shutdown' following vitamin K remains unexplained .

scholarly journals Blood Coagulation, Fibrinolytic Activity, Platelet Function and Immunoglobulins in Frostbite

1977 ◽  
Author(s):  
I.S. Chohan ◽  
I. Singh
Keyword(s):  
Blood Coagulation ◽  
Fibrinolytic Activity ◽  
Degradation Products ◽  
Western Himalayas ◽  
Platelet Adhesiveness ◽  
Intravascular Thrombosis ◽  
Lysis Time ◽  
Coagulation Defects ◽  
Euglobulin Lysis Time

Fifteen males, 19-45 years old, stationed between altitudes 3690 and 5540 m in the Western Himalayas who were frostbitten were studied within 24 hours of the injury and then 4 weeks and 1 year after for blood coagulation defects. The following disturbances were found: fibrinogen degradation products and factor VIII-related antigen were increased; fibrinogen, platelet counts and haematocrit were decreased; platelet adhesiveness was increased; euglobulin lysis time was prolonged; antithrombin III,α-1 antitrypsin and α-2 macroglobulin were markedly decreased; IgG and IgA immunoglobulins and cryoglobulins were increased; serum albumin was decreased and IgM immunoglobulin consumption was increased.These abnormalities increase platelet adhesiveness and diminish fibrinolytic activity and promote intravascular thrombosis.Furosemide increases fibrinolytic activity and suppresses platelet adhesiveness in vivo (I. Singh and I.S. Chohan, Int. J. Biometeor. 17, 73, 1973). Its use in the prevention of frostbite is under investigation.

Plasminogen Activity in Plasma and in Serum Before and After Venostasis

1979 ◽  
Author(s):  
C. Soria ◽  
A. Rodriguez-Zeballos ◽  
J. Soria ◽  
G. Kartalis
Keyword(s):  
Biological Activity ◽  
Synthetic Substrate ◽  
Lysis Time ◽  
Before And After ◽  
Euglobulin Lysis Time ◽  
Antigen Activity ◽  
Fibrin Clots

When venostasis is applied in men for 10 minutes at a pressure half-way between diastolic and systolic, various results may be obtained as far as fibrinolysis is concerned, normally the euglobulin lysis time reduced from above 3 hours to less than one hour. In these conditions, after venostasis the estimation of plasminogen after activation by Streptokinase (S.K.) on synthetic substrate S2251, shows 20-80% greater activity in serum than in plasma. In some patients at high risks of thrombosis, the euglobulin lysis time 15 unchanged after venostasis. In these cases, the biological activity of plasminogen is slightly greater in plasma than in serum, as is observed before venostasis in all subjects.In order to explain these observations, experiments were performed using placental or plasmatic (glu or lys) plasminogen ; these show that for the same antigen activity, the biological activity of placental plasminogen previously activated by S.K. is greater than that of plasmatic plasminogen. We suggest a modification of the structure of plasminogen in the presence of activators and of fibrin clots. Further experiments will be necessary to explain the modification of plasminogen structure

Venostasis but not DDAVP Infusion Provokes the Plasma Fibronectin Increase

1990 ◽  
Vol 64 (02) ◽  
pp. 294-296 ◽  
Author(s):  
M Letowska ◽  
K Bykowska ◽  
J Sablinski ◽  
S Lopaciuk ◽  
M Kopeć
Keyword(s):  
Von Willebrand Factor ◽  
Vessel Wall ◽  
Blood Donors ◽  
Plasma Fibronectin ◽  
Lysis Time ◽  
Before And After ◽  
Euglobulin Lysis Time ◽  
Von Willebrand ◽  
Willebrand Factor ◽  
Factor Antigen

SummaryPlasma fibronectin (pFN), von Willebrand factor antigen (vWf: Ag), factor VIII procoagulant activity, fibrinogen, euglobulin lysis time (ELT) and hematocrit were determined in healthy blood donors before and after venostasis as well as after intravenous infusion of l-deamino-8-D-arginine vasopressin (DDAVP). Both venostasis and DDAVP provoked an increase in vWf : Ag and shortening in the ELT. In contrast, venostasis only but not DDAVP induced an increase in pFN levels which was statistically significant with and without correction for a concomitant hematocrit increment. The results indicate that there is a distinct difference in the patterns of venostasis and DDAVP mediated release of proteins from the vessel wall.

The Effects of Infusing Thrombin and Its Acetylated Derivative

1968 ◽  
Vol 20 (01/02) ◽  
pp. 190-201 ◽  
Author(s):  
L Pechet ◽  
A. M Engel ◽  
C Goldstein ◽  
B Glaser
Keyword(s):  
Degradation Products ◽  
Hypercoagulable State ◽  
Factor Vii ◽  
Fibrinogen Degradation Products ◽  
Fibrin Monomer ◽  
Lysis Time ◽  
Factor Ii ◽  
Euglobulin Lysis Time ◽  
Fibrin Monomers

Summary and ConclusionsDogs and rabbits were infused with acetylated thrombin (thrombin E) and clotting thrombin (thrombin C). Similar effects were noted in both animal series. Very large amounts of thrombin E could be tolerated, but resulted in defibrination. Following a transient hypercoagulable state, the blood became unclottable. The platelets and factors I, V, and VIII were markedly decreased. Factor II was moderately affected and factor VII-X showed no significant changes in most experiments. The presence of fibrinogen degradation products was indicated by a delay in the polymerization of fibrin monomers.Based on the shortening of the euglobulin lysis time, a decrease in the proactivator, and the appearance of inhibitors of fibrin monomer polymerization, it is concluded that transient fibrinolysis is induced by the infusion of thrombin. Its immediate mechanism could not be determined.

scholarly journals Exchange Between Intra- and Extravascularly Injected Radioiodinated Fibrinogen

1977 ◽  
Author(s):  
R. Rüegg ◽  
P.W. Straub
Keyword(s):  
Half Life ◽  
Degradation Products ◽  
Plasma Fibrinogen ◽  
Lysis Time ◽  
Euglobulin Lysis Time ◽  
Cautious Interpretation ◽  
Plasma Half Life

To test the hypothesis that in certain diseases plasma fibrinogen may be degraded extra-vascular ly and that circulating fibrin/-ogen degradation products (FDP) may stem from extra-vascular ly degraded fibrin/-ogen, 8 patients with pleural or peritoneal effusions (4 transudate, 4 exudate) were given 125I-fibrinogen i.v. and simultaneously 131I-fibrinogen intraca-vitarily. Measurements of plasma and effusion volumes allowed quantitation of the exchange of fibrinogen and its protein-bound derivatives. Plasma t/2 was shortened in 6/7 patients. At 48 hrs 7.6 ± 3.9% of i.v. injected radioactivity was found in the effusion (18% of it clottable, 24% protein-bound but unclottable), 4.8% ± 2.2% of intracavitarily injected radioactivity was found in plasma (29% clottable and 28% protein-bound unclottable). Iramunoreactive serum FDP were elevated in 7/8, plasma euglobulin lysis time normal in all 7/7 patients. Effusion fluids were fibrinolytically active, usually showing higher FDP concentrations than serum. It is concluded that 1) the shortened plasma half-life of fibrinogen is due in part to loss into the effusion, 2) fibrinogen is degraded in effusions and 3) plasma FDP in patients with ‘effusions may stem partly from extravascular fibrinogen proteolysis. The findings suggest cautious interpretation of FDP levels and fibrinogen turnover results in patients with suspected DIC and effusions.

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