Cold Promoted Activation of Factor VII

SummarySeveral known activators of the plasma kallikrein system were tested for the ability to induce cold promoted activation of factor VII.All the prekallikrein activators tested (EACA, trypsin, acetone, urokinase, kaolin, Liquoid, ellagic acid) revealed generation of factor VII activator activity (CPA). Simultaneously the plasma kallikrein system was activated. A good correlation was demonstrated between the factor VII activation and the kallikrein activity.Glandular kallikrein, bradykinin, or kallidin revealed no effect on the coagulation system. Thus, the correlation between the factor VII activation and the kallikrein system seemed to be restricted to plasma kallikrein.

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Cold Promoted Activation of Factor VII VI. Effect of Inhibitors

Thrombosis and Haemostasis ◽

10.1055/s-0038-1648105 ◽

1973 ◽

Vol 29 (03) ◽

pp. 633-643

Author(s):

H Gjønnæss

Keyword(s):

Soya Bean ◽

Factor Vii ◽

Plasma Kallikrein ◽

Contact Activation ◽

Activation Reaction ◽

Hexadimethrine Bromide ◽

Bean Trypsin Inhibitor ◽

Plasma Arginine ◽

Kallikrein Activity ◽

Effect Of Inhibitors

SummaryThe cold promoted activation of factor VII occurs in parallel with an activation of a plasma arginine esterase, and, on inhibition of the cold activation of factor VII, the esterase activation also decreased. The inhibitor pattern supported our theory that the arginine esterase that is activated in the cold activation of factor VII is plasma kallikrein.The cold activation of factor VII was completely inhibited with soya bean trypsin inhibitor in doses that did not interfere with the contact activation. On the other hand, inhibition of the contact activation with hexadimethrine bromide did not interfere with the cold activation of factor VII except when this was kaolin induced. Contact and cold activation therefore appear to represent two different pathways for the activation of factor VII. The cold activation reaction is probably mediated by the activation of plasma prekallikrein, and inhibition of the plasma kallikrein activity correlates with the inhibition of the cold promoted activation of factor VII.

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Plasma Kallikrein Contributes to Coagulation in the Absence of Factor XI by Activating Factor IX

Arteriosclerosis Thrombosis and Vascular Biology ◽

10.1161/atvbaha.119.313503 ◽

2020 ◽

Vol 40 (1) ◽

pp. 103-111 ◽

Cited By ~ 3

Author(s):

Mayken Visser ◽

René van Oerle ◽

Hugo ten Cate ◽

Volker Laux ◽

Nigel Mackman ◽

...

Keyword(s):

Complex Formation ◽

Ellagic Acid ◽

Thrombin Generation ◽

Factor Ix ◽

Coagulation System ◽

Plasma Kallikrein ◽

Factor Xia ◽

The Difference ◽

Long Chain

Objectives: FXIa (factor XIa) induces clot formation, and human congenital FXI deficiency protects against venous thromboembolism and stroke. In contrast, the role of FXI in hemostasis is rather small, especially compared with FIX deficiency. Little is known about the cause of the difference in phenotypes associated with FIX deficiency and FXI deficiency. We speculated that activation of FIX via the intrinsic coagulation is not solely dependent on FXI(a; activated FXI) and aimed at identifying an FXI-independent FIX activation pathway. Approach and Results: We observed that ellagic acid and long-chain polyphosphates activated the coagulation system in FXI-deficient plasma, as could be demonstrated by measurement of thrombin generation, FIXa-AT (antithrombin), and FXa-AT complex levels, suggesting an FXI bypass route of FIX activation. Addition of a specific PKa (plasma kallikrein) inhibitor to FXI-deficient plasma decreased thrombin generation, prolonged activated partial thromboplastin time, and diminished FIXa-AT and FXa-AT complex formation, indicating that PKa plays a role in the FXI bypass route of FIX activation. In addition, FIXa-AT complex formation was significantly increased in F11 −/− mice treated with ellagic acid or long-chain polyphosphates compared with controls and this increase was significantly reduced by inhibition of PKa. Conclusions: We demonstrated that activation of FXII leads to thrombin generation via FIX activation by PKa in the absence of FXI. These findings may, in part, explain the different phenotypes associated with FIX and FXI deficiencies.

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Activation of purified plasma factor VII by human plasmin, plasma kallikrein, and activated components of the human intrinsic blood coagulation system

Thrombosis Research ◽

10.1016/0049-3848(74)90119-4 ◽

1974 ◽

Vol 5 (6) ◽

pp. 759-772 ◽

Cited By ~ 46

Author(s):

K. Laake ◽

B. Österud

Keyword(s):

Blood Coagulation ◽

Factor Vii ◽

Coagulation System ◽

Plasma Kallikrein ◽

Blood Coagulation System ◽

Plasma Factor

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Evidence that Fitzgerald factor counteracts inhibition by kaolin or ellagic acid of the amidolytic properties of a plasma kallikrein

Blood ◽

10.1182/blood.v47.2.243.bloodjournal472243 ◽

1976 ◽

Vol 47 (2) ◽

pp. 243-251

Author(s):

OD Ratnoff ◽

H Saito

Keyword(s):

Cytochrome C ◽

Ellagic Acid ◽

Factor Vii ◽

Plasma Kallikrein ◽

High Molecular Weight Kininogen ◽

Intrinsic Pathway ◽

Fletcher Factor ◽

The Relationship ◽

Plasma Reactions

Fitzgerald trait, an asymptomatic disorder, is associated with abnormalities of surface-mediated plasma reactions, including coagulation via the intrinsic pathway, augmentation of the clot- promoting properties of factor VII, kaolin-mediated fibrinolysis, kinin generation, and enhancement of vascular permeability by diluted plasma (PF/Dil). These abnormalities can be corrected by Fitzgerald factor, an agent probably identical with high molecular weight kininogen found in normal, but not Fitzgerald-trait plasma. Our preparations of Fitzgerald factor possessed a second property. Amidolysis of alpha-N-benzoyl-L- proline-L-phenylalanine-L-arginine-pnitroanilide by a plasma kallikrein (activated Fletcher factor) was inhibited by kaolin or solutions of ellagic acid. Addition of preparations of Fitzgerald factor to kaolin or to solutions of ellagic acid counteracted their inhibitory properties. The action of these preparations was duplicated by solutions of cytochrome C or IgG, suggesting that these agents may inhibit the negative charges of kaolin or ellagic acid. Fitzgerald factor enhanced amidolysis of both normal and Fitzgerald-trait plasmas exposed to kaolin, effects not duplicated by cytochrome C or IgG. Whether or not the two properties of our preparations of Fitzgerald factor are related to the same agent is not yet certain. The relationship between these observations and the biologic role of Fitzgerald factor remains to be investigated.

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Evidence that Fitzgerald factor counteracts inhibition by kaolin or ellagic acid of the amidolytic properties of a plasma kallikrein

Blood ◽

10.1182/blood.v47.2.243.243 ◽

1976 ◽

Vol 47 (2) ◽

pp. 243-251 ◽

Cited By ~ 7

Author(s):

OD Ratnoff ◽

H Saito

Keyword(s):

Cytochrome C ◽

Ellagic Acid ◽

Factor Vii ◽

Plasma Kallikrein ◽

High Molecular Weight Kininogen ◽

Intrinsic Pathway ◽

Fletcher Factor ◽

The Relationship ◽

Plasma Reactions

Abstract Fitzgerald trait, an asymptomatic disorder, is associated with abnormalities of surface-mediated plasma reactions, including coagulation via the intrinsic pathway, augmentation of the clot- promoting properties of factor VII, kaolin-mediated fibrinolysis, kinin generation, and enhancement of vascular permeability by diluted plasma (PF/Dil). These abnormalities can be corrected by Fitzgerald factor, an agent probably identical with high molecular weight kininogen found in normal, but not Fitzgerald-trait plasma. Our preparations of Fitzgerald factor possessed a second property. Amidolysis of alpha-N-benzoyl-L- proline-L-phenylalanine-L-arginine-pnitroanilide by a plasma kallikrein (activated Fletcher factor) was inhibited by kaolin or solutions of ellagic acid. Addition of preparations of Fitzgerald factor to kaolin or to solutions of ellagic acid counteracted their inhibitory properties. The action of these preparations was duplicated by solutions of cytochrome C or IgG, suggesting that these agents may inhibit the negative charges of kaolin or ellagic acid. Fitzgerald factor enhanced amidolysis of both normal and Fitzgerald-trait plasmas exposed to kaolin, effects not duplicated by cytochrome C or IgG. Whether or not the two properties of our preparations of Fitzgerald factor are related to the same agent is not yet certain. The relationship between these observations and the biologic role of Fitzgerald factor remains to be investigated.

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Cold Promoted Activation of Factor VII

Thrombosis and Haemostasis ◽

10.1055/s-0038-1649053 ◽

1972 ◽

Vol 28 (02) ◽

pp. 169-181 ◽

Cited By ~ 9

Author(s):

H Gjønnæss

Keyword(s):

Low Temperature ◽

Oral Contraceptives ◽

Fold Increase ◽

Factor Vii ◽

Plasma Kallikrein ◽

Factor Xii ◽

Overnight Incubation ◽

Esterolytic Activity

SummaryThe activating principle (CPA) of the factor VII activation seen in plasmas of women taking oral contraceptives after overnight incubation of the plasmas at 0° C was investigated. The reaction was dependent on low temperature, and factor XII was indispensable. Concomitant with the activation of factor VII a 10–30 fold increase in TAME esterolytic activity was observed together with a near 100 per cent drop in plasma kininogen concentration. The results indicated that the activation of factor VII is linked to activation of the kallikrein system, and that the activator may be plasma kallikrein.

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Cold Promoted Activation of Factor VII

Thrombosis and Haemostasis ◽

10.1055/s-0038-1649052 ◽

1972 ◽

Vol 28 (02) ◽

pp. 155-168 ◽

Cited By ~ 20

Author(s):

H Gjønnæs

Keyword(s):

Coagulation Factors ◽

Oral Contraception ◽

Factor Vii ◽

Coagulation System ◽

Plasma Coagulation ◽

Main Effect

SummaryThe cold promoted shortening of the thrombotest-times occuring in the plasmas of the majority of women on oral contraception or in the last trimester of pregnancy when incubated overnight at 0°–4° was investigated.The short thrombotest-times were caused by activation of factor VII in a time consuming reaction. Activation was also revealed in the intrinsic coagulation system, but the changes in the activities of coagulation factors other than factor VII were small.Comparison was made between clot promoting effects of cooling and contact, and it was concluded that while contact apparently exerted its main effect in the intrinsic system, cooling predominately activated the extrinsic plasma coagulation system.The cold promoted activation of factor VII seemed to be brought about by an activator.

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Interaction of Human Tumor Cells with Human Platelets and the Coagulation System

Thrombosis and Haemostasis ◽

10.1055/s-0038-1665296 ◽

1983 ◽

Vol 50 (03) ◽

pp. 726-730 ◽

Cited By ~ 11

Author(s):

Hamid Al-Mondhiry ◽

Virginia McGarvey ◽

Kim Leitzel

Keyword(s):

Tumor Cell ◽

Tumor Cells ◽

Cell Lines ◽

Human Tumor ◽

Human Platelets ◽

Factor Vii ◽

Coagulation System ◽

Breast Adenocarcinoma ◽

Activate Factor ◽

Tumor Cell Lines

SummaryThis paper reports studies on the interaction between human platelets, the plasma coagulation system, and two human tumor cell lines grown in tissue culture: Melanoma and breast adenocarcinoma. The interaction was monitored through the use of 125I- labelled fibrinogen, which measures both thrombin activity generated by cell-plasma interaction and fibrin/fibrinogen binding to platelets and tumor cells. Each tumor cell line activates both the platelets and the coagulation system simultaneously resulting in the generation of thrombin or thrombin-like activity. The melanoma cells activate the coagulation system through “the extrinsic pathway” with a tissue factor-like effect on factor VII, but the breast tumor seems to activate factor X directly. Both tumor cell lines activate platelets to “make available” a platelet- derived procoagulant material necessary for the conversion of prothrombin to thrombin. The tumor-derived procoagulant activity and the platelet aggregating potential of cells do not seem to be inter-related, and they are not specific to malignant cells.

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