Activation of Fibrinolysis and of Plasma-Kinin System during Venostasis*

Buluk, K; Malofiejew, M; Czokało, M

doi:10.1055/s-0038-1654886

Cited by 12 publications

(7 citation statements)

References 4 publications

(6 reference statements)

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“…Buluk et al (5) reported that in the plasma of stagnant blood, activators of tissue origin activated plasminogen to plasmin which in turn activated kallikreinogen to kallikrein (25). Plasma kallikreinogen may also be activated by lowering the pH to less than 6.0 (10) , a phenomenon that would occur in the muscle cell during application of the tourniquet, and by a drop in temperature of the blood (2, 16) from 37° C to 21° C during application of the tourniquet.…”

Section: Discussionmentioning

confidence: 99%

“…The relationship between the decrease in kinin forming activity of the cell particle fractions (Table 5) and the increase in kinin forming activities in plasma (5,24) leads to the possibility that the kinin forming activity in ischemic muscles might participate by enhancing its activity in plasma after release of the tourniquet. In view of the fact that the kinin forming enzymes of mitochondrial and lysosomal fractions are acidheat-resistant (comments on materials and methods) , while plasma kallikrein is not (4) , it is possible to distinguish kinin forming enzymes from the mitochondrial and lysosomal fractions from plasma kallikrein.…”

Section: Discussionmentioning

confidence: 99%

“…After the last cen t rifugation and decantation, the erythrocyte fraction was h e molysed by adding distilled water in a proportion of 1.0 ml per 10 6 erythrocytes. The supernatant was stored at -20° C. 5…”

Section: For Determination Of Erythrocyte Kininase and Ei•ythrocytementioning

confidence: 99%

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The Effect of a Tourniquet on the Kinin-Kininogen System in Blood and Muscle

Nakahara¹

1971

Thromb Haemost

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SummaryDogs had tourniquet applied to their hind limbs for 4 h. Plasma kinin, plasma kininase, plasma kininogen, erythrocyte kininase, sarcoplasm kininase, sarcoplasm kinin forming enzymes, kininase from mitochondrial and lysosomal fractions, and kinin forming enzyme in mitochondrial and lysosomal fractions were examined for relationships between muscle and plasma kinins, before and after application of the tourniquet. The characteristics of kininase and kinin forming enzymes in extracts of mitochondrial and lysosomal fractions were stable to acid-heating. However, sarcoplasm kininase was unstable. A kinin forming enzyme which is stable to acid-heating was found in the plasma obtained after release of the tourniquet. A substance which acts as an accelerator of plasma kininase was present also in extracts from mitochondrial and lysosomal fractions. An increase in plasma kinin after release of the tourniquet was followed by a decrease in plasma kininogen content and by an increase in the activities of plasma kininase and erythrocyte kininase. From the results obtained, it appears that kinin forming enzymes may be released from ischemic muscle into the circulating blood after the release of the tourniquet, along with accelerators of plasma kininase. A mechanism to explain the increase in plasma kinin content is discussed.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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The Effect of a Tourniquet on the Kinin-Kininogen System in Blood and Muscle

Nakahara¹

1971

Thromb Haemost

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“…The vascular endothelium of veins and venules is now considered to be a major source of tissue activator as well as of blood activator (Todd, 1959;Astrup & Buluk, 1963;Fearnley, 1965). Urokinase, extractable from urine, was once considered to be filtered blood activator, but has now been shown to originate in the kidney and urinary tract (Williams, 1951;Ladehoff, 1960;Painter & Charles, 1962;Buluk & Malofiejew, 1963;Ali & Lack, 1965;Holemans, McConnell & Johnstone, 1966). If the various activators were available in a purified form their biochemical and physical characterization would show whether they were similar enzymes.…”

Section: Discussionmentioning

confidence: 99%

Purification of rabbit kidney cytokinase and a comparison of its properties with human urokinase

Ali

Evans

1968

Biochemical Journal

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1. The cytokinase (tissue activator of plasminogen) content of several mammalian tissues was evaluated by a quantitative casein hydrolysis method. 2. An alkaline (pH10.5) extraction of cytokinase from rabbit kidney lysosome-microsome fraction, followed by chromatography on DEAE-cellulose at pH7.6 with stepwise or linear increase in concentration of phosphate buffer, gave an 86-fold purification of the enzyme. The purified material was non-proteolytic against casein and heated fibrin and was freeze-dried without significant loss of activity or solubility. 3. Cytokinase is a protein with E(0.1%) (1cm.)=0.87 at 280mmu, and does not possess sufficient hexose or sialic acid to be classified as a glycoprotein. It has S(20,w) 2.9-3.1s and molecular weight 50000 when measured on a calibrated Sephadex G-100 column. It has an isoelectric point between pH8 and pH9, and is maximally active and stable at pH8.5. It is inactivated by heat at 78 degrees . 4. Cytokinase and human urokinase have the same K(m) value and are inhibited in a partially competitive manner by in-aminohexanoic acid and aminomethylcyclohexanecarboxylic acid. They are also inhibited by cysteine and arginine, but are unaffected by iodoacetamide and p-chloromercuribenzoate. 5. On the basis of this and other evidence it is suggested that rabbit kidney cytokinase and human urokinase are similar, if not identical, enzymes.

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“…We have been able to demonstrate significant activity in the occluded vein, which is maintained by repeated occlusions of 20 min duration, in 60% of the patients. This has been demonstrated to be clinically effective (79,80). Systemic activity was demonstrated in only 10% of these individuals.…”

Section: Physical Means O F Producing In Vivo Fibrinolytic Activitymentioning

confidence: 99%

Possibilities of Development of Fibrinolytic Activity with New and Projected Agents

Ee¹

1968

J Vasc Res

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Activation of Fibrinolysis and of Plasma-Kinin System during Venostasis*

Cited by 12 publications

References 4 publications

The Effect of a Tourniquet on the Kinin-Kininogen System in Blood and Muscle

The Effect of a Tourniquet on the Kinin-Kininogen System in Blood and Muscle

Purification of rabbit kidney cytokinase and a comparison of its properties with human urokinase

Possibilities of Development of Fibrinolytic Activity with New and Projected Agents

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