Congenital Factor II Deficiency

2018 ◽  
pp. 183-199
Author(s):  
Yadollah Farshi ◽  
Akbar Dorgalaleh ◽  
Shadi Tabibian
Keyword(s):  
2012 ◽  
Vol 35 (4) ◽  
pp. 416-420
Author(s):  
S. Imane ◽  
Z. Laalej ◽  
S. Faez ◽  
B. Oukkache
Keyword(s):  

1977 ◽  
Author(s):  
H. Beeser ◽  
R. Kulzer

As patients who are congenitally deficient in factor X are extremely rare natural substrate plasma for the specific one-stage factor X assay is only poorly available. Asbestos-filtered or charcoal-filtered ox plasma deficient both in factor X and VII is instead widely used as artificial factor X substrate plasma with Russel’s viper venom (BW) and cephalin or lecithin as the thromboplastic agent.We studied the practicability of removing separately factor X from the plasma of different species (man, horse, ox, sheep, swine) by several chromatographic procedures. Chromatography of swine plasma on DEAE-Sephadex A 25 yielded a substrate virtually free of factor X while containing adequate concentrations of fibrinogen and factor II, V and VII, Using different brands of commercial tissue thromboplastins the so prepared swine plasma has proved to be a specific artificial substrate plasma for the one-stage factor X assay. Calibration curves obtained by plotting the clotting times of various dilutions of pooled normal human plasma determined with this factor X assay system against the percentages showed a linear relationship from 100% to about 2% on log/log paper. Factor X determinations with our method on various patients’ plasmas (i.e. coumarin treatment, congenital factor X deficiency, liver disease) performed in parallel to the RVV-cephalin and the congenital factor X deficient plasma methods gave comparable results.As our specific artificial factor X deficient swine plasma is fairly simple prepared with a good yield, it has to be considered as an appropriate reagent to overcome the shortness of the rare congenital factor X deficient substrate plasma.


1974 ◽  
Vol 31 (01) ◽  
pp. 040-051 ◽  
Author(s):  
Gustav Gaudernack ◽  
Åse Gladhaug Berre ◽  
Bjarne Østerud ◽  
Hans Prydz

SummaryMonospecific antisera against the human coagulation factor X have been raised in rabbits by injections of purified antigen. Such antiserum was used to study the cross-reacting material without factor X activity which is present in the blood of warfarin-treated patients and animals as well as to study the changes in factor X during coagulation. One patient with congenital factor X deficiency was also studied.A complete identity was found between factor X in Macaca mulatta and human blood. During warfarin treatment antigenically cross-reacting material appeared in plasma. This was not adsorbed on BaSO4, and inhibited the coagulation activity of normal factor X.Both this material, normal factor X and the cross-reacting material in plasma from a patient congenitally deficient in factor X gave rise to split products during coagulation by the intrinsic pathway, i. e. all of them served as substrates for the intrinsic activator of factor X.


1968 ◽  
Vol 20 (03/04) ◽  
pp. 534-541 ◽  
Author(s):  
O Egeberg

SummarySevere hemorrhagic disorder due to congenital factor XIII deficiency is described in two unrelated Norwegian girls.Plasma cephalin time was for both patients extraordinarily short during episodes of bleeding and hematomas. No such hyperactivity reaction was demonstrable in unaffected condition some months later.Estimations of blood factor XIII levels revealed a partial defect in the parents of both children, and also in some other family members, consistent with an autosomal incompletely recessive inheritance of the defect. Some of the presumptive heterozygotes had a history of light bleeding phenomenons; whether this was related to their partial lack of factor XIII is so far uncertain.


1995 ◽  
Vol 74 (02) ◽  
pp. 686-692 ◽  
Author(s):  
René W L M Niessen ◽  
Birgit A Pfaffendorf ◽  
Augueste Sturk ◽  
Roy J Lamping ◽  
Marianne C L Schaap ◽  
...  

SummaryAs a basis for regulatory studies on the influence of hormones on (anti)coagulant protein production by hepatocytes, we examined the amounts of the plasma proteins antithrombin III (AT III), protein C, protein S, factor II, factor X, fibrinogen, and prealbumin produced by the hepatoma cell line HepG2, into the culture medium, in the absence and presence of insulin, β-estradiol, dexamethasone and thyroid hormone. Without hormones these cells produced large amounts of fibrinogen (2,452 ± 501 ng/mg cell protein), AT III (447 ± 16 ng/mg cell protein) and factor II (464 ± 31 ng/mg cell protein) and only small amounts of protein C (50 ± 7 ng/mg cell protein) and factor X (55 ± 5 ng/mg cell protein). Thyroid hormone had a slight but significant effect on the enrichment in the culture medium of the anticoagulant protein AT III (1.34-fold) but not on protein C (0.96-fold) and protein S (0.91-fold). This hormone also significantly increased the amounts of the coagulant proteins factor II (1.28-fold), factor X (1.45-fold) and fibrinogen (2.17-fold). Insulin had an overall stimulating effect on the amounts of all the proteins that were investigated. Neither dexamethasone nor ß-estradiol administration did substantially change the amounts of these proteins.We conclude that the HepG2 cell is a useful tool to study the hormonal regulation of the production of (anti)coagulant proteins. We studied the overall process of protein production, i.e., the amounts of proteins produced into the culture medium. Detailed studies have to be performed to establish the specific hormonal effects on the underlying processes, e.g., transcription, translation, cellular processing and transport, and secretion.


1964 ◽  
Vol 11 (02) ◽  
pp. 497-505 ◽  
Author(s):  
O de Bastos ◽  
R. S Reno ◽  
O. T Correa

SummaryThree cases of true congenital hypoprothrombinaemia are presented.Studies were made to prove the deficiency of prothrombin in the patient’s plasma and to rule out deficiency of other clotting factors or the presence of abnormal anti-thrombin substances.All the patients were of group B.The results obtained confirm that the patients have a real prothrombin deficiency as the cause of a severe haemorrhagic disease.


1981 ◽  
Vol 46 (03) ◽  
pp. 670-670 ◽  
Author(s):  
G Follea ◽  
B Coiffier ◽  
J P Viale ◽  
M Dechavanne
Keyword(s):  

1963 ◽  
Vol 10 (02) ◽  
pp. 295-308 ◽  
Author(s):  
Clarence Merskey ◽  
Herbert Wohl

Summary1. Groups of rats were fed thrombogenic diets and the effects on blood coagulation and fibrinolysis assessed.2. Animals fed a diet containing cholesterol, thiouracil and cholic acid developed high levels of coagulation factors I, II, V, VII—X, VIII, IX and X.3. Animals fed a similar diet with additional 40% beef fat developed even greater elevation of V, VII—X, VIII and X, similar elevation of factor II, and lesser (but still significant) elevation of factors I and IX. In addition marked elevation of blood platelets occurred.4. Euglobulin lysis time of the group not fed the additional fat was longer than in controls. Significant prolongation of euglobulin lysis time was not found in the group fed additional fat.5. If the increased levels of plasma fibrinogen were taken into account, it was found that a larger amount of fibrin was lysed per unit time in the euglobulin lysis test with plasma from rats fed either atherogenic diet compared with controls.6. Defective thromboplastin generation was present in both groups of rats fed an atherogenic diet. The defect was present in the serum and was not due to lack of a factor required for thromboplastin generation. An inhibitor was present in the serum which was capable of preventing the action of normal serum.7. No good correlation was found between the occurrence of changes in blood coagulation or fibrinolysis and the presence or absence of thrombosis and infarction.8. The exact cause of these anomalies remains unexplained, as does the cause of the thrombosis in these animals. Starvation per se does not account for these abnormal findings. They could not adequately be explained on the basis of “hypercoagulability” of the blood.


1969 ◽  
Vol 21 (03) ◽  
pp. 573-579 ◽  
Author(s):  
P Fantl

SummaryTreatment of human and dog oxalated plasma with 0.2 to 1.0 × 10−1 M 2.3-dithiopropanol (BAL) or dithiothreitol (DTT) at 2–4° C for 30 min results in the reduction of the vitamin-K dependent clotting factors II, VII, IX and X to the respective-SH derivatives. The reaction is pH dependent. Under aerobic conditions the delayed one stage prothrombin time can be partly reversed. Under anaerobic conditions a gradual prolongation of the one stage prothrombin time occurs without reversal.In very diluted plasma treated with the dithiols, prothrombin can be converted into thrombin if serum as source of active factors VII and X is added. In contrast SH factors VII, IX and X are inactive in the specific tests. Reoxidation to active factors II, VII, IX and X takes place during adsorption and elution of the SH derivatives. The experiments have indicated that not only factor II but also factors VII, IX and X have active-S-S-centres.


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