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Results for “Factor VII Deficiency”

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PubMed1998

[New possibilities in the management of hemorrhagic diathesis caused by factor deficiency and thrombocytopenia: recombinant active factor VII concentrate].

Recombinant Factor VIIa, a new therapeutic tool to treat severe bleeding caused by inhibitory haemophilia cases, some cases of thrombocytopenia and thrombocytopathy (e.g. severe type III von Willebrand disease) receives growing attention in clinical practice. Exogeneous FVIIa-in a supraphysiological concentration (clearly over 6 U/ml) seems to be able to generate quickly and safely (without thrombotic side effects) thrombin--the final enzyme of clotting--in physiological, or pathological conditions. A concise review about the possible mechanisms of action, indications, monitoring and clinical experience gained sofar with FVIIa is given in this report.

Factor VII↗
PubMed1986

Concurrent production of macrophage agglutination factor and factor VII by antigen-stimulated human peripheral blood mononuclear cells.

We have studied concurrent production of macrophage agglutination factor (MAggF) and procoagulant activity by antigen-stimulated human blood mononuclear cells to gain insight into biochemical mechanisms underlying delayed hypersensitivity inflammatory reactions. After stimulation of cells from tuberculin-sensitive donors with tuberculin, MAggF was present in culture supernatants while the overwhelming majority of procoagulant activity remained cell-associated. Neither MAggF nor procoagulant activity was found in reconstituted control cultures, nor in tuberculin-stimulated cultures of non-sensitive cells. Concanavalin A and lipopolysaccharide elicited both activities from cultured mononuclear cells, regardless of donor sensitivity. Human MAggF bound to insolubilized gelatin, heparin and a monoclonal anti-fibronectin (FN) antibody, and its activity was inhibited by another monoclonal antibody directed against the gelatin-binding domain of FN. Treatment of indicator peritoneal exudate cells with monoclonal anti-FN receptor antibody inhibited their response to human MAggF. These results suggest that human MAggF, like the analogous guinea-pig activity, is FN-associated. Antigen-elicited procoagulant activity shortened the recalcification time of normal, factor VII- and factor IX-deficient plasma, partially corrected prothrombin times of factor VII-deficient plasma, had no effect on recalcification and prothrombin items of factor X- and factor V-deficient plasma, and was inhibited by specific anti-factor VII antibody. Thus, human mononuclear cell procoagulant consists of both tissue factor and factor VII, whether it is induced by antigen or mitogen. Antigen-stimulated blood mononuclear cells are able to provide a signal for local fibrin deposition and a protein mediating fibrin binding to mononuclear phagocytes and collagen at sites of delayed hypersensitivity reactions.

Animals↗
PubMed2002

[Molecular analysis of two pedigrees with hereditary F VII deficiency].

OBJECTIVE: To identify the mutation of coagulation factor VII (F VII) gene in two pedigrees with hereditary F VII deficiency. METHODS: F VII gene mutations were analysed in two propositi and their family members by direct DNA sequencing. Allele specific PCR and PCR combined with restricted enzyme digestion were used to confirm the detected mutations. RESULTS: Two gene mutations were detected in the propositus of pedigree A: G to C transition at position 6390 resulting in Trp40Cys and G to A at 11496 resulting in Arg353Gln, both are heterozygotes. The heterozygosity for polymorphism Arg353Gln was confirmed with the restriction enzyme Msp I digestion in his mother. In the propositus of pedigree B, there was a T to G transition at position 11482 resulting in His348Gln, heterozygosity of which was confirmed with Nsp I digestion in the propositus and his daughter. G to T transition at position 11514 resulting in Thr359Met was also found in the propositus of pedigree B, and the heterozygosity for Thr359Met was confirmed with allele specific PCR in the propositus and his son. CONCLUSION: Three missense mutations were found in two pedigrees with hereditary F VII deficiency. A novel Trp40Cys mutation was reported for the first time.

Factor VII↗
PubMed2004

[Factors VII, VIII, IX, and X: molecular genetics and gene diagnosis].

Molecular genetic aspects of the inherited bleeding disorders haemophilia A and B, deficiencies of factor VII and X are described. The spectrum of the mutations is characterized. For genetic counselling the X-chromosomal inheritance of haemophilia and the principles of the indirect and direct genomic diagnosis are explained. Clinics and genetics of the rare inherited bleeding disorders known as factor VII and factor X deficiency are summarized. The mutations spectrum, the role of polymorphisms, the bleeding pattern and genotype-phenotype relations are described.

Amino Acid Sequence↗
PubMed1971

Identification of a congenital defect of factor VII in a colony of beagle dogs: the clinical use of the plasma.

A severe, pure deficiency of factor VII has been defined in haematological and biochemical terms in the Alderley Park colony of beagle dogs. By modification of the conventional factor VII assay to improve its specificity an apparent low activity of between 1 and 2.5% of the normal beagle has been found. When this plasma is used as a substrate for factor VII assays it compares well with human factor VII-deficient plasma in the measurement of both raised and depressed factor VII activity. It also appears to be a valuable reagent in the quality control of tissue thromboplastin extracts.

Animals↗
PubMed1979

Congenital deficiency of blood clotting factors II, VII, IX, and X.

A patient congenitally deficient in factors II, VII, IX, and X has been further investigated after a follow-up of 15 yr. At birth, these factors, when determined by clotting assays, were undetectable. Following therapy with vitamin K1, the clotting activity of these factors rose but never exceeded 18% of normal. Immunologic assays revealed much higher levels of these factors than did clotting assays, thus suggesting that the vitamin-K-dependent factors were present in abnormal forms. Two-dimensional crossed immunoelectrophoresis showed that at least two forms of prothrombin were present in the patient's plasma. One form was similar to normal prothrombin; the other had the same mobility as acarboxyprothrombin. In addition, the majority of this fast-migrating peak was not adsorbable onto insoluble barium salts. These observations suggested that some molecules of the patient's prothrombin lacked the normal complement of gamma-carboxyglutamic acid residues. This observation was confirmed by a specific assay for gamma-carboxyglutamate. Since malabsorption of vitamin K, warfarin intoxication, and hepatic dysfunction were excluded as causes of this patient's syndrome, this rare congenital abnormality could represent either a defective gamma-carboxylation mechanism within the hepatocyte or faulty vitamin K transport.

Adolescent↗
PubMed1979

Activation of human factor VII in plasma and in purified systems: roles of activated factor IX, kallikrein, and activated factor XII.

Factor VII can be activated, to a molecule giving shorter clotting times with tissue factor, by incubating plasma with kaolin or by clotting plasma. The mechanisms of activation differ. With kaolin, activated Factor XII (XII(a)) was the apparent principal activator. Thus, Factor VII was not activated in Factor XII-deficient plasma, was partially activated in prekallikrein and high-molecular weight kininogen (HMW kininogen)-deficient plasmas, but was activated in other deficient plasmas. After clotting, activated Factor IX (IX(a)) was the apparent principal activator. Thus, Factor VII was not activated in Factor XII-,HMW kininogen-, XI-, and IX-deficient plasmas, but was activated in Factor VIII-, X-, and V-deficient plasmas. In further studies, purified small-fragment Factor XII(a) (beta-XII(a)), kallikrein, and Factor IX(a) were added to partially purified Factor VII and to plasma. High concentrations of beta-XII(a) activated Factor VII in a purified system; much lower concentrations of beta-XII(a) activated Factor VII in normal plasma but not in prekallikrein or HWM kininogen-deficient plasmas. Kallikrein alone failed to activate partially purified Factor VII but did so when purified Factor IX was added. Kallikrein also activated Factor VII in normal, Factor XII-, and Factor IX-deficient plasmas. Purified Factor IX(a) activated partially purified Factor VII and had no additional indirect activating effect in the presence of plasma. These results demonstrate that both Factor XII(a) and Factor IX(a) directly activate human Factor VII, whereas kallikrein, through generation of Factor XII(a) and Factor IX(a), functions as an indirect activator of Factor VII.

Blood Coagulation↗
PubMedDate not supplied

Coagulation factor VII. (Biochemistry, role in blood coagulation, methods of assay, congenital deficiencies and relationship with thrombosis).

Factor VII is a trace plasma protein which is very reactive and can be activated through several enzymatic pathways. It has been postulated that factor VII has all the features of an initiator of the clotting mechanism. The severe congenital deficiency of factor VII is characterized by a clinical picture which is not distinguishable from that observed in hemophilias. The presence of factor alpha-VIIa in the circulation in clinical conditions associated with thrombosis leads to the assumption that this factor, when activated, may play an important role in thrombogenesis. The variants of factor VII congenital deficiency and the methods currently employed to assay factor VII in various conditions are reviewed.

Blood Coagulation↗
PubMed2005

[The change and significance of coagulation activity in bleomycin-induced lung fibrosis in rats].

OBJECTIVE: To investigate the role of coagulation activity of bronchoalveolar lavage fluid (BALF) in the pathogenesis of lung fibrosis. METHODS: Fourty-eight Sprague-Dawley rats were randomly divided into 2 groups, 24 rats in each group. In the bleomycin (BLM) group, the lung fibrosis model was made by tracheal instillation of bleomycin A(5) (BLMA(5), 5 mg/kg). At day 7, 14, 28 and 40, the recalcification time of normal pooled plasma, factor VII and X deficiency plasma were measured for procoagulation activity (PCA), and the thrombin activity and the protein level of transforming growth factor beta(1) (TGF-beta(1)) in BALF were also measured. In the control group, normal solution was instillated into the lungs. RESULTS: In the BLM group, the recalcification time of normal pooled plasma in BALF at the four time points were (56 +/- 10), (78 +/- 4), (172 +/- 11) and (180 +/- 6) s respectively, while in the control group, were (190 +/- 10), (186 +/- 8), (184 +/- 6) and (185 +/- 6) s respectively. The thrombin activity at the four time points were (1.26 +/- 0.03), (0.82 +/- 0.05), (0.28 +/- 0.03) and (0.28 +/- 0.02) microg/ml respectively in the BLM group, but were (0.31 +/- 0.02), (0.32 +/- 0.03), (0.31 +/- 0.04) and (0.29 +/- 0.05) microg/ml respectively in the control group. The level of TGF-beta(1) at the four time points were (310 +/- 36), (220 +/- 30), (109 +/- 12) and (96 +/- 11) ng/ml respectively in the BLM group, but were (92 +/- 20), (94 +/- 12), (92 +/- 10) and (90 +/- 9) ng/ml respectively in the control group. The above measurements were significantly different in day 7 and 14 between the BLM group and the control group (P < 0.01), while the differences were not significant at day 28 and 40 (P > 0.01). In the BLM group, at day 7 and 14, the recalcification time of factor VII deficiency plasma was (123 +/- 12) and (162 +/- 4) s respectively; the recalcification time of factor X deficiency plasma was (357 +/- 22) and (387 +/- 12) s respectively; the recalcification time of factor X deficiency plasma was longer than that of factor VII deficiency plasma and that of normal pooled plasma. Within 14 day, the level of TGF-beta(1) was positively correlated with PCA and thrombin activity. CONCLUSIONS: During the period of alveolitis, the PCA and thrombin activity were upregulated in BALF, which was caused by activated factor VII activating factor X and the switching to the exogenous coagulation pathway. But during the period of lung fibrosis, their activities were not upregulated. These results suggest that the coagulation factor and thrombin might contribute to the development of pulmonary fibrosis by promoting production of TGF-beta(1).

Animals↗
PubMed1986

Activation of human factor VII in the initiation of tissue factor-dependent coagulation.

We have used activation peptide release assays to compare factor VII and activated factor VII (VIIa) activation of factor X, normal factor IX (IXN), and a variant factor IX (IXBmLE), which, after activation, is unable to back-activate factor VII. In purified systems, factor VII and VIIa each rapidly activated factor X, but after a one minute lag for factor VII. VIIa also readily activated both IXN and IXBmLE. Factor VII initially failed to activate substantial amounts of either IXN or IXBmLE; on further incubation factor VII activated IXN but not IXBmLE. Activation of IXN began when approximately 10% of factor VII had been converted to VIIa, as measured by 125I-factor VII radioactivity profiles. Adding factor VII to VIIa slowed its activation of IXBmLE. However, in the presence of factor X, factor VII alone rapidly activated IXBmLE. Unlike purified systems, 1 nmol/L VIIa added to factor VII-deficient plasma failed to activate factor IX. Increasing factor VII to 10 nmol/L (plasma concentration) either as native VII or VIIa yielded similar activation curves for factor IX and similar activation curves for factor X. Adding 5% VIIa to factor X-deficient plasma and to factor XII-deficient plasma substantially shortened the dilute tissue factor clotting time of only the former. These data support the hypothesis that factor VII/tissue factor complex initiates tissue factor-dependent clotting through a minimal generation of Xa. This Xa then rapidly back-activates a small amount of factor VII, following which the rates of activation of both factors IX and X increase dramatically.

Blood Coagulation↗