Coagulation and fibrinolysis in capybara (Hydrochaeris hydrochaeris), a close relative of the guinea-pig (Cavia porcellus).

Fibrinolytic and coagulation properties of capybara (Hydrochaeris hydrochaeris, LINNAEUS, 1766) plasma were analysed and the results compared to the guinea-pig (Cavia porcellus), a close relative. Capybara fibrinogen was isolated and fibrinolysis of its plasma was carried out in a homologous system and with bovine fibrin. Undiluted plasma did not have fibrinolytic activity on fibrin plates; euglobulins gave a dose-related response. Zymography of capybara and guinea-pig plasma gave the same patterns of activity as human or bovine plasma. Human urokinase (UK) and tissue plasminogen activator (t-PA) produced lysis in capybara fibrin plates. Streptokinase (SK) (500 IU/ml) did not activate capybara or guinea-pig plasma. In this system, human plasma was extensively activated. Coagulation tests for both species of rodent were prolonged. The capybara showed values for prothrombin time (PT) shorter than activated thromboplastin time (APTT). The guinea-pig, as already shown, had longer PT values. Factors X and VII were very low for capybara and guinea-pig when tested using reference curves and diagnostic kits for human plasma. It is suggested that the capybara could be a valuable laboratory animal considering its size and closeness to the guinea-pig, and this could allow for the provision of materials from one single animal when convenient or necessary.

Dextran sulfate-dependent fibrinolysis in whole human plasma.

This study shows that Flu-beta-Ala can reduce the ability of human plasma to inhibit plasmin. This observation was utilized to develop a method for generating detectable fibrinolytic activity in whole human plasma as assessed on a radiolabeled fibrin plate. Plasma was pretreated with Flu-beta-Ala to remove inhibitors of fibrinolysis: then dextran sulfate was added and the mixture was further incubated at 4 degrees C. When normal plasma was treated in this manner, the rate of generation of fibrinolytic activity after 0.75 hr incubation with radiolabeled fibrin was equivalent to that of 35 ng/ml plasmin. The plasminogen dependence of this activity was tested by pretreating plasma with antibodies against plasminogen. The generation of fibrinolytic activity was totally blocked by this treatment, indicating that the observed fibrinolytic activity was plasminogen-dependent. When plasmas deficient in prekallikrein, factor XII, or high-molecular-weight kininogen were treated with Flu-beta-Ala and dextran sulfate, the initial rate of fibrinolytic activity was less than normal. But after 3 hr incubation with radiolabeled fibrin, the rate of fibrinolytic activity in these deficient plasmas approached that of normal plasma. Thus this dextran sulfate-dependent fibrinolytic activity is dependent on factor XII, prekallikrein, and high-molecular-weight kininogen, but the requirement is not absolute.

Fibrinolytic activity evoked in the plasma of the normal and adrenalectomized rat by cellulose sulphate.

1. Cellulose sulphate, a kinin-releasing agent, produced fibrinolytic activity in plasma when administered intravenously to the rat but not when added to fresh rat plasma in vitro. The in vivo effect was maximal within 1 min and disappeared within 10-20 minutes. It was retained in plasma taken 1 min after the injection and kept at room temperature for 30 minutes.2. A decrease of anti-fibrinolytic potency measured against urokinase-activated bovine plasmin, was shown to occur in plasma of rats given cellulose sulphate.3. Activated rat plasma lysed heat-denatured fibrin: it probably contains free plasmin as well as plasminogen activator.4. Adrenalectomized rats did not exhibit fibrinolytic activity nor statistically significant benzoyl-arginine ethyl ester-esterase activation in plasma after cellulose sulphate treatment.5. Adrenalectomized rats had significantly increased levels of plasma kininogen, but were normally sensitive to the kininogen-depleting action of cellulose sulphate.6. The increased plasma kininogen of adrenalectomized rats seems to be a consequence of the impairment of the plasminogen activating mechanism.