Interactions of ε-Aminocaproic Acid with the Thrombin Clotting and Fibrinolytic Systems

Maxwell, Richard E.; Allen, Deena

doi:10.1038/209211a0

Cited by 19 publications

(6 citation statements)

References 7 publications

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“…The matter adsorbed out of plasma as well as out of fibrinogen solutions apparently could be removed by factor XII as well as by SK, both demanding the presence of plasma, but while the desorption by factor XII + plasma could not be inhibited by small amounts of EACA, the desorption by SK + plasma could. If further experiments will support our impression that even temporary exposure of a fibrinogen film to EACA will render it less available to plasmin action, a finding which would fit current concepts of the competitive nature of EACA action at the fibrinogen molecule (16) then perhaps the factor XII + plasma system attacks fibrinogen at a different site. At the proportions of SK to plasma that we employed, proteolytic activity of "activator" (8) rather than of plasmin must have been present; its formation would not have been prevented by our concentrations of EACA (13), but since its activity was inhibited, perhaps it competes with EACA even more weakly than plasmin does.…”

Section: Discussionmentioning

confidence: 55%

Possible Involvement of Fibrinogen and Proteolysis in Surface Activation

Vroman¹,

Adams²

1967

Thromb Haemost

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SummaryAmong others, the following events occurring at certain liquid/wettable solid interfaces were studied with the recording ellipsometer :A. removal of fibrinogen films by plasmin, by normal intact plasma, and by Streptokinase plus factor XII deficient plasma ;B. adsorption and desorption of normal plasma, and of factor XII deficient plasma by factor XII or Streptokinase, and the effect of epsilon-aminocaproic acid on these types of desorption ; andC. adsorption of rabbit anti-human fibrinogen serum onto human fibrinogen films and onto films deposited by human plasma and other mixtures. All findings thus far appear compatible with the following interpretation. The wettable surfaces used in this study adsorb fibrinogen out of plasma as well as out of fibrinogen solutions. A few minutes after factor XII is activated, the plasma develops a temporary ability to remove a major part of such a fibrinogen film. The remaining part undergoes further changes without further reduction in thickness.“Activator”, formed by addition of Streptokinase to factor XII deficient plasma, is also able to remove fibrinogen film, whether formed by adsorption out of fibrinogen solutions or out of the factor XII deficient plasma itself. The ‘‘activator” activity is inhibited immediately by epsilon-aminocaproic acid, while the activity created by activated factor XII is not.Relationship of present findings to surface activation of factor XII and to the adhesion of platelets is discussed.

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Section: Discussionmentioning

confidence: 55%

Possible Involvement of Fibrinogen and Proteolysis in Surface Activation

Vroman¹,

Adams²

1967

Thromb Haemost

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“…28 The finding of acceleration of euglobulin clot lysis also after the infusion of EACA prior to injections of nicotinic acid may in part be explained by the fact that, EACA does not, according to our experiments, and in the concentrations used in the present investigation, precipitate with the euglobulin fraction, so that the in vitro test is in fact uninhibited. CONCLUSION The present investigation confirms that physical activity and nicotinic acid are potent liberators of plasminogen activator.…”

Section: Discussionmentioning

confidence: 56%

Studies On Fibrinolytic Activity in Normal Persons and Patients With Atherosclerotic Vascular Dis Ease After Physical Activity and Injections of Nicotinic Acid

Laursen

Gormsen

1970

Angiology

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“…This "antiactivator activity" of the antifibrinolytics was first described by Alkjaersig et al (1959) and repeatedly confirmed later (for review see Markwardt and Landmann 1967). Results from our own laboratory (Landmann 1967) as well as those from others (Donaldson 1964;Godal and Theodor 1965;Egeblad 1966;Maxwell and Allen 1966;Maxwell et al 1968;Ambrus et al 1968;Lukasiewicz et al 1968;Lukasiewicz and Niewiarowski 1968;Iwamoto et al 1968;Abiko and Iwamoto 1970) do not correspond with that generally accepted mechanism of action. The present study was, therefore, undertaken.…”

Section: Introductionmentioning

confidence: 46%

Studies on the Mechanism of Action of Synthetic Antifibrinolytics

Landmann¹

1973

Thromb Haemost

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SummaryWhen compared with derivatives of benzamidine, the synthetic antifibrinolytics EACA, PAMBA, and trans-AMCHA are weak competitive inhibitors of ester hydrolysis by urokinase, of plasminogen activation by urokinase and streptokinase, and of plasmin action on synthetic substrates, casein, and fibrinogen. In contrast, the inhibitory effect of the antifibrinolytics equal or surpass, that of benzamidine derivatives on the process of fibrin dissolution by plasmin and on plasma clot lysis. Degradation of fibrin monomers by plasmin seems to be equally strongly inhibited by the antifibrinolytics. Thus, fibrin and fibrin monomers are plasmin substrates, the hydrolysis of which is inhibited by the antifibrinolytics in a different way from their other inhibitory effects on plasmin. It is concluded that this activity accounts for the strong action of these inhibitors on the whole process of fibrinolysis.Plasmin, in contrast to other proteolytic enzymes, was shown to possess a specific ability to attack fibrin resulting in rapid formation of soluble products from the insoluble substrate. The strong inhibitory effect of the antifibrinolytics is not caused by their reaction with the substrate, fibrin, but by their blocking the specific interaction of plasmin with fibrin.The molecular mechanism of the plasmin-fibrin reaction and its inhibition is discussed.

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Interactions of ε-Aminocaproic Acid with the Thrombin Clotting and Fibrinolytic Systems

Cited by 19 publications

References 7 publications

Possible Involvement of Fibrinogen and Proteolysis in Surface Activation

Possible Involvement of Fibrinogen and Proteolysis in Surface Activation

Studies On Fibrinolytic Activity in Normal Persons and Patients With Atherosclerotic Vascular Dis Ease After Physical Activity and Injections of Nicotinic Acid

Studies on the Mechanism of Action of Synthetic Antifibrinolytics

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