Effect of physical exercise on blood clotting and fibrinolysis

1963 ◽  
Vol 18 (2) ◽  
pp. 337-344 ◽  
Author(s):  
Sotirios G. Iatridis ◽  
John H. Ferguson
Keyword(s):  
Blood Clotting ◽  
Normal Subjects ◽  
Factor Vii ◽  
Strenuous Exercise ◽  
Factor Xii ◽  
Factor V ◽  
Factor X ◽  
Plasma Factor ◽  
Deficient Subject ◽  
Direct Activator

The effect of strenuous exercise on the clotting and fibrinolytic systems was studied on 1 Hageman-deficient and 59 normal subjects (males aged 18–37 years). In the normal subjects there was a significant shortening of the whole-blood clotting time and of the partial thromboplastin time both in glass and in siliconized tubes. Plasma factor VIII (AHF or AHG) assays rose to 188% (average), but the specificity of the test is questioned. Factor XII (HF) increased to 318% (average) unequivocally. A postexercise increased heparin tolerance was also noted. There was no significant increase in the levels of fibrinogen, prothrombin, factor V (AcG), or factor VII (proconvertin) and factor X (Stuart). Fibrinolytic activity as measured by the euglobulin lysis and plasma plate methods increased significantly in most of the normal subjects. The data suggest that the fibrinolytic factor which increases after exercise is not active plasmin, but is related to the “activator” mechanisms. A plasma lysokinase (indirect activator) seems to preponderate in over half the cases. In 20% of cases a plasminoplastin (direct activator) may be involved. In the Hageman-deficient subject there was no improvement in clotting, and the slight changes in some of the fibrinolysis tests were nonsignificant. Submitted on October 16, 1962 Submitted on October 16, 1962

Pathways of Blood Clotting Initiation by Cancer Cells

1979 ◽  
Author(s):  
N. Semeraro
Keyword(s):  
Cancer Cells ◽  
Blood Clotting ◽  
Coagulation Factor ◽  
Factor Vii ◽  
Ehrlich Carcinoma ◽  
Factor V ◽  
Factor X ◽  
Experimental Tumors ◽  
Activate Coagulation Factor ◽  
Available Information

Although available information indicates that cancer cells may activate blood coagulation, the precise mechanism remains still uncertain. A procoagulant with characteristics of tissue thromboplastin has been found in human benign and malignant tissues and in some experimental tumors. On the other hand it has been reported that extracts from malignant tissues directly activate coagulation factor X, due to the presence of a serine protease. We have investigated the procoagulscitic fluid. Cells from Lewis lung carcinoma (primary and metastasis), Ehrlich carcinoma ascites and JW sarcoma ascites were able to shorten markedly the recalcification time of normal, factor VIII and factor VII-deficient, not of factor X-deficient human plasma. The same cells did generate thrombin when mixed with a source of prothrombin and factor X, absorbed bovine serum (as a source of factor V), phospholipid and CaCl2.Cells from Sarcoma ISO ascites were completely inactive in both test systems. It was a included that cells from some experimental tumors, similarly to normal platelets, possess the capacity to directly activate coagulation factor X. This suggests the existence of an alternative “cellular” pathway in blood clotting initiation distinct from both the intrin sic and extrinsic mechanisms.(Supported by Italian CNR and NIH, NCI, USA).

Generation Of Coagulation Factors By The Isolated Rat Liver Perfused With A Synthetic Blood Substitute

1981 ◽  
Author(s):  
C A Owen ◽  
E J W Bowie
Keyword(s):  
Factor Viii ◽  
Rat Liver ◽  
Blood Substitute ◽  
Factor Ix ◽  
Factor Vii ◽  
Clotting Factor ◽  
Isolated Perfused Rat Liver ◽  
Factor Xii ◽  
Factor V ◽  
Factor X

Measuring the release of small amounts of a clotting factor from an isolated perfused rat liver is difficult if the perfusate already contains some of the factor. Further, platelet-containing perfusates generate a coagulant activity that may invalidate clotting assays.We have successfully employed a completely synthetic blood substitute for rat liver perfusions. The perfusate is “Fluosol-43” generously furnished by Alpha Therapeutic Corporation. The oxygen-carrying perfluorochemical is FC-43 (perfluorotributylamine) and the substitute for albumin is hydroxyethyl starch. Using the Brauer perfusion technique, we found that rat livers in 5 hours released an average of 2.3% of the normal plasma concentration of prothrombin, 8.4% factor V, 16.2% factor VII, 7.0% factor IX, 3.7% factor X, 28.3% factor XI and 12.3% factor XII. Antithrombin III and plasminogen were also generated.Only minute amounts of factor VIII were released unless serum, cryoprecipitate or cryoprecipitate-free plasma was added; then the yield was 8.8% on average. The more “venom factor” (platelet aggregability with Bothrops alternata venom) added to the synthetic perfusate, the more factor VIII was released.

Kinetics of Human Blood Coagulation Induced by Trypsin

1964 ◽  
Vol 12 (01) ◽  
pp. 307-330 ◽  
Author(s):  
E. T Yin
Keyword(s):  
Human Serum ◽  
Trypsin Inhibitor ◽  
Soybean Trypsin Inhibitor ◽  
Factor Vii ◽  
Factor V ◽  
Factor X ◽  
Serum Factor ◽  
Clotting System ◽  
Plasma Factor ◽  
Kinetics Of

Summary1. Trypsin is a potent activator of purified human serum factor X. In the presence of calcium the activation was greatly enhanced.2. Trypsin did not activate purified human serum factor VII or crude human plasma factor V, with or without calcium.3. A new trypsin inhibitor, Benzamidine-HCl (shown to be superior to soybean trypsin inhibitor) was used. The Benzamidine-HCl - trypsin complex did not interfere in the clotting system, whereas the soybean trypsin inhibitor-trypsin complex did.4. Benzamidine-HCl was used to inactivate the trypsin at any desired stage during the activation of factor X.5. The trypsin activated factor X was found to be very stable.6. In the presence of activated factor X, factor V, cephalin and calcium, a very potent prothrombin activator was formed.7. An apparent time-consuming reaction was observed when activated factor X was incubated with factor V in the presence of calcium, which required the subsequent addition of cephalin to convert prothrombin to thrombin.8. The trypsin clotting mechanism is analogous to the clotting of blood by Russell’s viper venom.

Some Effects of Factor VII on Rates of Thrombin Production and one Stage Pi’s

1979 ◽  
Author(s):  
D. J. Baughman ◽  
A. Lytwyn
Keyword(s):  
Plasma Concentrations ◽  
Factor Vii ◽  
Thrombin Inhibitor ◽  
Factor V ◽  
Factor X ◽  
One Stage ◽  
Feedback Scheme ◽  
Plasma Factor ◽  
Initial Generation ◽  
Tissue Thromboplastin

Attempts to automate a chromogenic one stage PT assay required hastening the onset of thrombin production without altering the rate of production. Assays were performed by combining 0.25ml chromogenic substrate S-2238 (2mM), 0.40ml tissue thromboplastin,0.050ml plasma, and 0.050ml diluted serum (40%v/v) in 1.35ml TRIS buffer (pH=8-5,I=0.15). Sera were prepared by using the supernatant of a) whole blood, b) recalcified plasma, c) recalc fied plasma and tissue thromboplastin, d)recalcified plasma and partial thromboplastin (cephalin and ellagic acid) and e) thrombin clotted plasma. The results indicated that S-2238, a potent thrombin inhibitor, delayed the onset and altered the rate of thrombin; production. Small amounts of thrombin shortened the initial generation of thrombin without altering its rate. Sera from a), c) and d) but not b) and e) resulted in immediate thrombin production at most plasma concentrations without affecting the rate, had no residual prothrombin, and had similar residual S-2238 activity not reduced by hirudin or At III-heparin. In particular, scrum b) had ~80% plasma Factor X which could be adsorbed without affecting thrombin production, had ~40% Factor V and ~300% Factor VII. These results suggest that when Factor VII activity is greater than ~7% there is an effect on the time but not on the rate of thrombin production via positive thrombin feedback scheme. Thus, the standard PT can measure the time of thrombin appearance, and/or the rate of thrombin production, and/or fibrin polymerization.

Coagulability of Blood and Fibrinolysis Related to Age and Lipids

1975 ◽  
Author(s):  
T. Matsuda
Keyword(s):  
Factor Viii ◽  
Antithrombin Iii ◽  
Normal Subjects ◽  
Factor Vii ◽  
Factor V ◽  
Factor X ◽  
Progressive Decline ◽  
Cholesterol Levels ◽  
Α2 Macroglobulin ◽  
Older Subjects

Levels of factor VIII, factor VII-X, factor X, factor V, fibrinogen, antithrombin III, euglobulin lysis times, plasminogen, α2-macroglobulin, α1-antitrypsin and FDP were determined in 487 healthy normal subjects from age 20 to 94. In subjects over age 60, serum lipids were determined simultaneously.In the subjects over age 60, levels of factor VIII, fibrinogen, antithrombin III, α2-maeroglobulin, α1-antitrypsin and FDP were higher, factor V activity was lower, and euglobulin lysis times were shorter than in subjects under age 50. In the older subjects, levels of factor VII-X, factor X fibrinogen, antithrombin III, plasminogen and FDP showed slight but progressive decline with age. In these subjects over age 60, serum cholesterol levels were significantly correlated with levels of factor VII-X, factor X, antithrombin III, plasminogen and FDP; antithrombin III concentration was significantly correlated with factor X activity but not with factor VII-X activity; euglobulin lysis times were correlated with obesity.

Very Low Activated Factor VII and Reduced Factor VII Antigen in Familial Abetalipoproteinaemia

1998 ◽  
Vol 80 (08) ◽  
pp. 233-238 ◽  
Author(s):  
K. A. Mitropoulos ◽  
M. N. Nanjee ◽  
D. J. Howarth ◽  
J. C. Martin ◽  
M. P. Esnouf ◽  
...  
Keyword(s):  
Plasma Concentrations ◽  
Positive Association ◽  
Factor Ix ◽  
Factor Vii ◽  
Unesterified Fatty Acid ◽  
Factor Xii ◽  
Factor X ◽  
Factor Xi ◽  
Activated Factor Vii ◽  
Normal Mean

SummaryAbetalipoproteinaemia is a rare disorder of apolipoprotein B metabolism associated with extremely low plasma concentrations of triglyce-ride. To discover whether the general positive association between factor VII and triglyceride levels extends to this condition, 5 patients were compared with 18 controls. All patients had a triglyceride below 100 μmol/l. Plasma unesterified fatty acid concentration was normal. Although factor IX activity was only slightly reduced (mean 88% standard) and factor IX antigen was normal, mean activated factor VII in patients was strikingly reduced to 34% of that in controls, a level similar to that found in haemophilia B. The patients’ mean factor VII activity and factor VII antigen were also significantly reduced to 54% and 63% of those in controls, respectively. Mean factor XI activity and tissue factor pathway inhibitor activity were reduced in patients to 70% and 75% of control values respectively, while factor XII, factor XI antigen, factor X, prothrombin and protein C were normal.

Self-Damping Mechanism in Blood Coagulation

1974 ◽  
Vol 32 (01) ◽  
pp. 057-064 ◽  
Author(s):  
Y Nemerson ◽  
S.A Silverberg ◽  
J Jesty
Keyword(s):  
Tissue Factor ◽  
Blood Coagulation ◽  
Calcium Ions ◽  
Control Mechanism ◽  
Factor Vii ◽  
Damping Factor ◽  
Factor V ◽  
Factor X ◽  
Extrinsic Pathway ◽  
Two Systems

SummaryTwo reactions of the extrinsic pathway of coagulation, the activations of Factor X and prothrombin, have been studied in purified systems and shown to be self-damping. Factor X was activated by the tissue factor - Factor VII complex, and prothrombin by two systems: the coagulant protein of Taipan venom, and the physiological complex of activated Factor X, Factor V, lipid, and calcium ions. In each case the yield of enzyme, activated Factor X or thrombin, is a function of the concentration of activator. These and other observations are considered as a basis for a control mechanism in coagulation.

Heparin and Low Molecular Weight Heparins Inhibit Prothrombinase Formation but not its Activity in Plasma

1994 ◽  
Vol 72 (06) ◽  
pp. 862-868 ◽  
Author(s):  
Frederick A Ofosu ◽  
J C Lormeau ◽  
Sharon Craven ◽  
Lori Dewar ◽  
Noorildan Anvari
Keyword(s):  
Factor Xa ◽  
Catalytic Efficiency ◽  
Thrombin Inhibitor ◽  
Lag Phase ◽  
Factor V ◽  
Factor X ◽  
Normal Plasma ◽  
Plasma Factor ◽  
Prothrombin Activation ◽  
Plasma Heparin

SummaryFactor V activation is a critical step preceding prothrombinase formation. This study determined the contributions of factor Xa and thrombin, which activate purified factor V with similar catalytic efficiency, to plasma factor V activation during coagulation. Prothrombin activation began without a lag phase after a suspension of coagulant phospholipids, CaCl2, and factor Xa was added to factor X-depleted plasma. Hirudin, a potent thrombin inhibitor, abrogated prothrombin activation initiated with 0.5 and 1.0 nM factor Xa, but not with 5 nM factor Xa. In contrast, hirudin did not abrogate prothrombin activation in plasmas pre-incubated with 0.5,1.0 or 5 nM α-thrombin for 10 s followed by the coagulant suspension containing 0.5 nM factor Xa. Thus, thrombin activates plasma factor V more efficiently than factor Xa. At concentrations which doubled the clotting time of contact-activated normal plasma, heparin and three low Mr heparins also abrogated prothrombin activation initiated with 0.5 nM factor Xa, but not with 5 nM factor Xa. If factor V in the factor X-depleted plasma was activated (by pre-incubation with 10 nM a-thrombin for 60 s) before adding 0.5,1.0, or 5 nM factor Xa, neither hirudin nor the heparins altered the rates of prothrombin activation. Thus, none of the five anticoagulants inactivates prothrombinase. When 5 or 10 pM relipidated r-human tissue factor and CaCl2 were added to normal plasma, heparin and the three low Mr heparins delayed the onset of prothrombin activation until the concentration of factor Xa generated exceeded 1 nM, and they subsequently inhibited prothrombin activation to the same extent. Thus, hirudin, heparin and low Mr heparins suppress prothrombin activation solely by inhibiting prothrombinase formation.

Plasma Contact Activation and Decrease of Factor V Activity on Negatively-Charged Polyelectrolytes

1984 ◽  
Vol 51 (01) ◽  
pp. 061-064 ◽  
Author(s):  
M C Boffa ◽  
B Dreyer ◽  
C Pusineri
Keyword(s):  
Time Dependent ◽  
Initial Contact ◽  
Factor Xii ◽  
Factor V ◽  
Contact Activation ◽  
Polyelectrolyte Complexes ◽  
Plasma Factor ◽  
Fresh Plasma ◽  
Direct Adsorption

SummaryThe effect of negatively-charged polymers, used in some artificial devices, on plasma clotting and kinin systems was studied in vitro using polyelectrolyte complexes.Contact activation was observed as an immediate, transient and surface-dependent phenomenon. After incubation of the plasma with the polymer a small decrease of factor XII activity was noticed, which corresponded to a greater reduction of prekallikrein activity and to a marked kinin release. No significant decrease of factor XII, prekallikrein, HMW kininogen could be detected immunologically. Only the initial contact of the plasma with the polyelectrolyte lead to activation, subsequently the surface became inert.Beside contact activation, factor V activity also decreased in the plasma. The decrease was surface and time-dependent. It was independent of contact factor activation, and appeared to be related to the sulfonated groups of the polymer. If purified factor V was used instead of plasma factor V, inactivation was immediate and not time-dependent suggesting a direct adsorption on the surface. A second incubation of the plasma-contacted polymer with fresh plasma resulted in a further loss of Factor V activity.

HAEMOSTATIC CHANGES INDUCED BY TWO LOW DOSE TRIPHASIC ORAL CONTRACEPTIVES

1987 ◽  
Author(s):  
S J Machin ◽  
I J Mackie ◽  
K Walshe ◽  
M D Gillmer
Keyword(s):  
Oral Contraceptives ◽  
Protein C ◽  
Low Dose ◽  
Factor Vii ◽  
Cycle Period ◽  
Factor Xii ◽  
Factor X ◽  
Combined Oral Contraceptives ◽  
First Time ◽  
Protein C Activity

The haemostatic system was investigated in 26 women taking cyclically administered triphasic combined oral contraceptives for the first time during their first six cycles. Fourteen women received Logynon (mean dose 32.4μg ethinyloestradiol, 92pg progestagen) and 12 received SHD 415G (Schering) which contains a mean dosage of 32.4μg ethinyloestradiol and 78pg gestodene, a recently developed progesterone. The Logynon group showed a significant increase (p<0.005) in fibrinogen (pre-mean 284.4 g/1; after 1 cycle 347.3 g/1, after 6 cycles 318.6 g/1) , factor VII (65.8 u/1 to 73.9 u/1 to 83.2 u/1), factor XII (1.74 u/1 to 2.41 u/1, to 2.25 u/1), plasminogen (100.9 u/1 to 135.1 u/1 to 126.3 u/1); decrease in ATIII (115.9 u/1 to 103.1 u/1 to 93.4 u/1) but no significant change in factor X (98.4 u/1 to 108.9 u/1 to 102.4) or protein C (0.85 u/1 to 0.88 u/1 to 0.94 u/1) activity. The SHD 415G group showed similar changes with an increase in fibrinogen (247.9 g/1 to 330.8 g/1 to 373 .1 g/1), factor VII (63.1 u/1 to 73.1 u/1 to 90.3 u/1, factor X (98.3 u/1 to 112.0 u/1 to 124.4 u/1), factor XII (1.46 u/1, to 1.93 u/1, to 2.03 u/1), plasminogen (110.8 u/1 to 125.4 u/1 to 136.7 u/1); decrease in ATIII (113.1 u/1 to 96.3 u/1 to 89.7 u/1), but no change in protein C (0.84 u/1 to - 0.78 u/1 to 0.85 u/1) activity. These changes were apparent after the first cycle of therapy and the differences were maintained over the six cycle period. There was no increase in protein C activity despite changes in the other vitamin K dependent proteins factors VII and X. Both low oestrogen dose triphasic pills caused similar prothrombotic changes which were not modified by the new progesterone, gestodene.

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