Some Observations on the Rôle of Hageman Factor in Blood Coagulation

1961 ◽  
Vol 6 (02) ◽  
pp. 261-269 ◽  
Author(s):  
C Haanen ◽  
F Hommes ◽  
Gerdy Morselt
Keyword(s):  
Blood Coagulation ◽  
Clotting Factors ◽  
Sulphated Polysaccharides ◽  
Hageman Factor ◽  
Normal Plasma ◽  
Plasma Factors ◽  
Positively Charged

SummaryThe defective thromboplastin formation in Hageman factor deficient plasma is completely corrected using incubation tubes which have been coated previously with normal plasma. Positively or negatively charged molecules as protamin and sulphated polysaccharides interfere with this correction in a way that gives evidence Hageman factor is a positively charged protein.The defective thromboplastin generation of Hageman factor deficient incubation mixtures is corrected by addition of a purified Hageman factor preparation. Pre-incubation of Hageman factor with HF deficient serum improves the thromboplastin formation further, while pre-incubation of Hageman factor with HF deficient plasma abolishes this correction complete. Possibly here lies the key for the fact that serum clotting factors augment and plasma factors deteriorate during the clotting process.

The Role of Factor XI in a Dilute Thromboplastin Assay of Extrinsic Coagulation Pathway

2001 ◽  
Vol 85 (06) ◽  
pp. 1055-1059 ◽  
Author(s):  
Shilong Xiong ◽  
Xiaofan He ◽  
Fayi Liu ◽  
Jianzhong Han ◽  
Juncheng Li ◽  
...  
Keyword(s):  
Blood Coagulation ◽  
Platelet Rich Plasma ◽  
Critical Role ◽  
Extrinsic Pathway ◽  
Thrombin Inhibition ◽  
Normal Plasma ◽  
Low Concentrations ◽  
Plasma Depletion ◽  
Coagulation Pathway

SummaryBlood coagulation has been thought to be composed of both intrinsic and extrinsic pathways. Recent evidence strongly supports the critical role of the extrinsic pathway in the initiation of blood coagulation. This investigation established an assay that examines the role of FXI in the thromboplastin-initiated (extrinsic) coagulation based on this new concept. Plasma clotting times were measured at different concentrations of thromboplastin with activated FXII inhibited (FXIIa-inhibited Diluted Thromboplastin Time, FXIIaiDTT). Only at low concentrations of thromboplastin was FXIIaiDTT of FXI-deficient plasma significantly prolonged than that of normal plasma. Depletion of FXI from normal plasma prolonged its FXIIaiDTT and replenishment of FXI shortened it. FXIIaiDTTs of both FVIII-deficient and FIX-deficient plasma were remarkably prolonged, and addition of normal plasma dose-dependently shortened it. Furthermore, earlier α-thrombin inhibition was directly correlated with decreasing FXa generation. The amount of FXa production was: platelet-rich plasma > platelet-poor plasma > FXI-deficient plasma. Therefore, our findings from the FXIIaiDTT assays not only support the critical role of extrinsic pathway in blood coagulation initiation, but also demonstrate the importance of FXI as an amplifier of thrombin generation in thromboplastin-initiated coagulation.

Human platelet chemotaxis: requirement for plasma factor(s) and the role of collagen

1978 ◽  
Vol 235 (1) ◽  
pp. H23-H28 ◽  
Author(s):  
R. W. Lowenhaupt
Keyword(s):  
Structural Integrity ◽  
Human Platelet ◽  
Human Platelets ◽  
Factor Xi ◽  
Normal Plasma ◽  
Plasma Factor ◽  
Plasma Factors ◽  
Short Time

Platelets are actively mobile in plasma in vitro and, in addition, they migrate specifically and directionally toward added intact collagen (chemotaxis). Native human, bovine, and equine collagen, suspended in plasma, induce a chemotactic response in human platelets. However, heat-denatured and dinitrofluorobenzene-treated collagen fail to attract platelets. Platelets migrate directionally and specifically to intact native collagen incubated in plasma over a large distance (6 mm) in a very short time (total 15 min), as observed in a newly designed micromaze apparatus. Platelets obtained from donors deficient in plasma factors XII, IX, and VIII showed normal migration and chemotaxis in normal plasma and in their respective factor-deficient plasmas. Although nondirectional movement (mobility) was normal, platelets from a donor deficient in factor XI did not exhibit chemotaxis toward collagen in either factor XI-deficient plasma or in normal plasma. The results indicate that 1) collagen is a physiological substrate for the chemotactic phenomenon, 2) intact chemical and/or structural integrity of collagen is required for the induction of platelet chemotaxis, 3) at least one plasma constituent, factor XI, plays an essential role in the chemotactic phenomenon, and 4) contact between collagen and a plasma factor is essential for normal chemotaxis.

Studies on the Participation of Hageman Factor in Fibrinolysis

1970 ◽  
Vol 24 (01/02) ◽  
pp. 001-009 ◽  
Author(s):  
R.P McDonagh ◽  
J.H Ferguson
Keyword(s):  
Cytochrome C ◽  
Plasminogen Activator ◽  
Specific Inhibition ◽  
Hageman Factor ◽  
One Stage ◽  
Marked Inhibition ◽  
Normal Plasma ◽  
Generation Test

SummaryThe specific inhibition of the kaolin-mediated Hageman factor activation by the polycations : lysozyme, spermine tetrahydrochloride, and cytochrome c was confirmed. These polycations were without any antiplasmin or antiplasminogen-activator activity when tested in a one-stage lysis system. However, marked inhibition of plasminogen-activator generation in normal plasma by these polycations was noted in the activator-generation test. The proposed role of Hageman factor as that of a lysokinase or indirect activator of plasminogen is supported by these experiments.

scholarly journals Assessment of Hageman factor activation in human plasma: quantification of activated Hageman factor-C1 inactivator complexes by an enzyme- linked differential antibody immunosorbent assay

Blood ◽  
1985 ◽  
Vol 66 (3) ◽  
pp. 636-641
Author(s):  
AP Kaplan ◽  
B Gruber ◽  
PC Harpel
Keyword(s):  
Complex Formation ◽  
Immunosorbent Assay ◽  
Time Dependent ◽  
Enzyme Linked Immunosorbent Assay ◽  
Contact Activation ◽  
Hageman Factor ◽  
Normal Plasma ◽  
Dose Dependent Increase ◽  
Dose Dependent

An enzyme-linked immunosorbent assay has been developed for the quantitation of activated Hageman factor-C1 inactivator (HF-C1 INH) complexes. Addition of increasing quantities of either of the major forms of activated Hageman factor (HFa or HFf) to normal plasma or to Hageman factor-deficient plasma leads to a dose-dependent increase in activated HF-C1 INH complexes. As little as 0.5 micrograms/mL of activated HF added to plasma can be detected, corresponding to activation of approximately 2% of plasma HF. The sensitivity of the assay is increased at least tenfold when complexes are formed in HF- deficient plasma, indicating competition between unactivated HF and activated HF-C1 INH complexes for binding to the antibody. Specificity is demonstrated in that addition of activated HF to hereditary angioedema plasma yields less than 1% of the activated HF-C1 INH complex formation obtained with normal plasma. Kaolin activation of HF- deficient plasma yields no detectable complex formation. Kaolin activation of prekallikrein-deficient plasma demonstrates a time- dependent increase in formation of activated HF-C1 INH complex consistent with the ability of HF in this plasma to autoactivate as the time of incubation with the surface is increased. Kaolin treatment of high-molecular weight (HMW) kininogen-deficient plasma yields an even more profound abnormality in the rate of formation of activated HF-C1 INH complexes reflecting the complex role of HMW kininogen in the initiation of contact activation. Although addition of corn inhibitor to plasma prevents activated HF-C1 INH complex formation, it does not inhibit activated HF sufficiently fast to prevent prekallikrein activation.

scholarly journals Assessment of Hageman factor activation in human plasma: quantification of activated Hageman factor-C1 inactivator complexes by an enzyme- linked differential antibody immunosorbent assay

Blood ◽  
1985 ◽  
Vol 66 (3) ◽  
pp. 636-641 ◽  
Author(s):  
AP Kaplan ◽  
B Gruber ◽  
PC Harpel
Keyword(s):  
Complex Formation ◽  
Immunosorbent Assay ◽  
Time Dependent ◽  
Enzyme Linked Immunosorbent Assay ◽  
Contact Activation ◽  
Hageman Factor ◽  
Normal Plasma ◽  
Dose Dependent Increase ◽  
Dose Dependent

Abstract An enzyme-linked immunosorbent assay has been developed for the quantitation of activated Hageman factor-C1 inactivator (HF-C1 INH) complexes. Addition of increasing quantities of either of the major forms of activated Hageman factor (HFa or HFf) to normal plasma or to Hageman factor-deficient plasma leads to a dose-dependent increase in activated HF-C1 INH complexes. As little as 0.5 micrograms/mL of activated HF added to plasma can be detected, corresponding to activation of approximately 2% of plasma HF. The sensitivity of the assay is increased at least tenfold when complexes are formed in HF- deficient plasma, indicating competition between unactivated HF and activated HF-C1 INH complexes for binding to the antibody. Specificity is demonstrated in that addition of activated HF to hereditary angioedema plasma yields less than 1% of the activated HF-C1 INH complex formation obtained with normal plasma. Kaolin activation of HF- deficient plasma yields no detectable complex formation. Kaolin activation of prekallikrein-deficient plasma demonstrates a time- dependent increase in formation of activated HF-C1 INH complex consistent with the ability of HF in this plasma to autoactivate as the time of incubation with the surface is increased. Kaolin treatment of high-molecular weight (HMW) kininogen-deficient plasma yields an even more profound abnormality in the rate of formation of activated HF-C1 INH complexes reflecting the complex role of HMW kininogen in the initiation of contact activation. Although addition of corn inhibitor to plasma prevents activated HF-C1 INH complex formation, it does not inhibit activated HF sufficiently fast to prevent prekallikrein activation.

A Re-Appraisal of the Role of Blood Coagulation and Platelets in the Generalized Shwartzman Phenomenon

1966 ◽  
Vol 15 (03/04) ◽  
pp. 519-538 ◽  
Author(s):  
J Levin ◽  
E Beck
Keyword(s):  
Blood Coagulation ◽  
The State ◽  
Coagulation System ◽  
Renal Lesions ◽  
Intravascular Coagulation ◽  
Renal Glomeruli ◽  
Coagulation Mechanism ◽  
Shwartzman Phenomenon ◽  
Do So

SummaryThe role of intravascular coagulation in the production of the generalized Shwartzman phenomenon has been evaluated. The administration of endotoxin to animals prepared with Thorotrast results in activation of the coagulation mechanism with the resultant deposition of fibrinoid material in the renal glomeruli. Anticoagulation prevents alterations in the state of the coagulation system and inhibits development of the renal lesions. Platelets are not primarily involved. Platelet antiserum produces similar lesions in animals prepared with Thorotrast, but appears to do so in a manner which does not significantly involve intravascular coagulation.The production of adrenal cortical hemorrhage, comparable to that seen in the Waterhouse-Friderichsen syndrome, following the administration of endotoxin to animals that had previously received ACTH does not require intravascular coagulation and may not be a manifestation of the generalized Shwartzman phenomenon.

The Formation of Intermediate Product I in a Purified System The Role of Factor IX or of its Precursor and of a Hageman Factor-PTA Fraction

1961 ◽  
Vol 6 (02) ◽  
pp. 224-234 ◽  
Author(s):  
E. T Yin ◽  
F Duckert
Keyword(s):  
Intermediate Product ◽  
Factor Ix ◽  
Assay Method ◽  
Lag Phase ◽  
Factor X ◽  
Haemophilia B ◽  
Hageman Factor ◽  
One Stage ◽  
The One

Summary1. The role of two clot promoting fractions isolated from either plasma or serum is studied in a purified system for the generation of intermediate product I in which the serum is replaced by factor X and the investigated fractions.2. Optimal generation of intermediate product I is possible in the purified system utilizing fractions devoid of factor IX one-stage activity. Prothrombin and thrombin are not necessary in this system.3. The fraction containing factor IX or its precursor, no measurable activity by the one-stage assay method, controls the yield of intermediate product I. No similar fraction can be isolated from haemophilia B plasma or serum.4. The Hageman factor — PTA fraction shortens the lag phase of intermediate product I formation and has no influence on the yield. This fraction can also be prepared from haemophilia B plasma or serum.

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