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PubMed2002

Factor XIII Val34Leu polymorphism, factor XIII antigen levels and activity and the risk of deep venous thrombosis.

Varying results on the effect of factor XIII (FXIII) Val34Leu on venous thrombotic risk have been reported. The probability of a true association between this polymorphism and venous thrombotic risk would be enhanced by a laboratory phenotype associated with this polymorphism and with the thrombotic risk. The aim of this study was to assess the effect of FXIII Val34Leu, FXIII activity and subunit levels on venous thrombotic risk in a large case-control study, The Leiden Thrombophilia study (LETS). We found higher FXIII activity for 34Leu carriers (Leu/Leu: 158.0, Val/Val: 95.0). FXIII subunit levels were not associated with genotype. Higher FXIII activity was associated with a slightly decreased thrombotic risk [Odds ratio (OR): 0.8, 95% confidence intervals (CI): 0.5-1.3]. This effect was not present for elevated FXIII subunit levels. Higher FXIII activity was also associated with a higher dissociation index (percentage A2B2 complex dissociated after activation by thrombin for a fixed time interval). This index was higher for FXIII 34Leu carriers. The risk of deep venous thrombosis was slightly decreased for carriers of the 34Leu allele [OR: 0.9 (95%CI: 0.7-1.1)]. For homozygous 34Leu carriers the OR was 0.7 (95%CI: 0.4-1.3). This finding, suggesting a weak protective effect, was completely restricted to men. An overall estimate of thrombotic risk was calculated by using earlier reports on the risk of FXIII Val34Leu. The overall risk estimate for homozygous 34Leu carriers was 0.8 (95%CI: 0.6-1.0). In this study, a weak protective effect against venous thrombosis was found, of FXIII 34Leu as well as of increased FXIII activity.

Adolescent↗
PubMed1978

Studies on factor XIII antigen in congenital factor XIII deficiency. A tentative classification of the disease in two groups.

Immunological and immunofluorescent studies carried out on plasma and platelets of three cases of congenital factor XIII deficiency are reported. Two of these patients were originally thought to have normal factor XIII subunit S and no subunit A. However, repeated assays carried out using different lots of antiserum showed that in reality the patients lacked both subunit S and subunit A. The false positive finding was due to the presence of a anti-factor VIII contaminant in the antiserum originally used. The third patient had a normal subunit S and no subunit A. No factor XIII antigen was found by the indirect immunofluorescent technique in normal, factor XIII deficiency and von Willebrand's disease platelets. On the contrary, by using the non-monospecific antiserum a fluorescent pattern similar to that observed by using an anti-factor VIII antiserum, had been noted. On the basis of the data presented in this paper a tentative classification of factor XIII deficiency in two groups is proposed: Type I is characterized by the lack of both factor XIII subunit S and A. Type II is characterized by a normal subunit S and no subunit A. The need for a re-evaluation of published case of factor XIII deficiency by means of monospecific antisera is indicated.

Antigens↗
PubMed1993

Single step purification of platelet factor XIII using an immobilized factor XIII a-subunit monoclonal antibody.

To facilitate the analysis of the catalytic subunit of factor XIII we have developed a method for the immunoaffinity purification of this protein from platelets. This method employs a monoclonal antibody that binds to the a-subunit of factor XIII. The anti-factor XIII antibody was immobilized on agarose and then incubated with platelet lysate. Subsequently factor XIII was isolated from the platelet lysate in a single step with a 41% yield as measured by enzyme assay. The purified platelet factor XIII appeared nearly homogeneous when analyzed by polyacrylamide electrophoresis and by immunoblotting with another factor XIII monoclonal antibody.

Animals↗
PubMed1996

ETRO Working Party on Factor XIII questionnaire on congenital factor XIII deficiency in Europe: status and perspectives. Study Group.

A questionnaire was sent out in 1993 to more than 350 European institutions caring for patients with hemorrhagic disorders with the request to provide data of patients with congenital factor XIII deficiency, to pursue the following aims: (1) establish a registry of congenital factor XIII deficiency patients, (2) promote exchange between clinicians and basic researchers, (3) improve diagnostic and therapeutic approaches, and (4) stimulate research on gene defects and their impact on factor XIII function. So far, 72 patient questionnaires from 60 families have been collected. Their bleeding pattern is typical, with frequent involvement of the umbilical cord and the central nervous system. Forty-nine patients receive regular factor XIII replacement, but obviously some patients with mild symptoms do not require prophylactic substitution, despite low factor XIII levels. On the other hand, 18 patients had factor XIII activities of > or = 5% of normal, but only 3 of those patients were reported to have no bleeding symptoms. Furthermore, 17 symptomatic, apparently heterozygous relatives in eight families were observed. Seven out of 30 females aged over 18 years had experienced spontaneous abortions; wound healing problems were seen in 26 patients. Currently, a second questionnaire is being distributed to obtain more detailed information on bleeding and other symptoms, diagnostic approaches, and exclusion of concurrent other bleeding diatheses. Future activities will be validation and standardization of assays, and study of gene defects and their impact on the structure of factor XIII and symptoms of patients. We intend to expand the survey to countries outside Europe.

Abortion, Habitual↗
PubMed1983

Determination of factor XIII activity and of factor XIII inhibitors using an ammonium-sensitive electrode.

An assay for rapid factor XIII activity measurement has been developed based on the determination of the ammonium released during fibrin stabilization. Factor XIII was activated by thrombin and calcium. Ammonium was measured by an ammonium-sensitive electrode. It was demonstrated that the assay procedure yields accurate and precise results and that factor XIII-catalyzed fibrin stabilization can be measured kinetically. The amount of ammonium released during the first 90 min of fibrin stabilization was found to be 7.8 +/- 0.5 moles per mole fibrinogen, which is in agreement with the findings of other authors. In 15 normal subjects and in 15 patients suffering from diseases with suspected factor XIII deficiency there was a satisfactory correlation between the results obtained by the "ammonium-release-method', Bohn's method, and the immunological assay (r1 = 0.65; r2 = 0.70; p less than 0.01). In 3 of 5 patients with paraproteinemias the values of factor XIII activity determined by the ammonium-release-method were markedly lower than those estimated by the other methods. It could be shown that inhibitor mechanisms were responsible for these discrepancies.

Ammonium Chloride↗
PubMed1997

[Effect of factor XIII on intractable CSF leakage after a transpetrosal-approach operation: a case report].

The authors reported an experience showing that the XIII factor was effective for intractable cerebrospinal fluid (CSF) leakage after a transpetrosal operation to deal with cerebellopontine angle meningioma. A 63-year-old female noted a slight headache and a floating feeling. She became dependent on a stick for walking alone because of gradual gait disturbance. As the headache became more severe, she consulted the outpatient clinic of the department of neurosurgery of Kobe University Hospital. Magnetic resonance images (MRI) revealed a 4.3 x 3.0cm sized right cerebellopontine angle tumor. She was admitted for the purpose of removal of the tumor and preoperative examinations were performed. Neurological findings on admission showed only slight right cerebellar signs. The operation was performed via the transpetrosal approach and the tumor was totally removed (Simpson Grade II). It took 12 hours 40 minutes for the operation. The amount of blood loss was 1970ml and the blood transfusion volume was 1200ml. Postoperative course was uneventful and her complaints disappeared. There were no postoperative complications at all, but 2 weeks after the operation, CSF leakage under the skin flap appeared. As subcutaneous fluid collection after skull base surgery is usual, spinal drainage and compression of the skin flap was carried out but these measures were not effective. The collection of fluid did not disappear for 2 weeks. Based on our successful experience with the XIII factor therapy in intractable cerebrospinal fluid leakage from the nose after a transsphenoidal approach operation for recurrent pituitary adenoma, the blood level of the XIII factor activity was examined. As the result was far below the normal limit in this case, the XIII factor was infused at a rate of 750 units per day for 5 days. One week after the administration, the level of the XIII factor became normal. Fluid collection disappeared and the drainage tube was removed. Recently, in neurosurgery, skull base surgery has been used widely and the range of craniotomy has been extended because operations can now be performed without compression of cerebral cortexes. However, operation time has increased and the volumes of bleeding and of blood transfusion are increasing. Postoperative complications such as CSF leakage and infection have become new problems. In this case, the XIII factor was still far below the normal level 2 weeks after the operation and it could be considered to have caused delayed CSF leakage. Some papers have reported that the XIII factor was effective in treating intractable fistula after operations in other surgical areas. However, this is the first report of skull base surgery such as an operation using transpetrosal approach taking advantage of the effect of the XIII factor.

Cerebellopontine Angle↗
PubMed1996

Intracellular factor XIII: cellular distribution of factor XIII subunit a in humans.

In addition to the plasma where factor XIII subunit A is present as part of the heterodimers of the tetrameric fibrin-stabilizing factor, homodimers of factor XIII A can also be detected in cellular localization in different human tissues. Experimental findings verified that these cells belong to the megakaryocyte/ platelet and the monocyte/macrophage cell lines. Additionally, factor XIII A is present in hepatocytes localized mainly around central veins in the liver and occasionally expressed in certain malignantly transformed cells. It is reasonable to suppose that factor XIII A acts not only as a member of the clotting cascade, but also as a cellular enzyme that can catalyze molecular interactions intracellularly (during the assembly/reassembly of the cytoskeleton) or extracellularly (in the connective tissue matrix around the cells containing it).

Blood Platelets↗
PubMed1987

Rapid formation of large molecular weight alpha-polymers in cross-linked fibrin induced by high factor XIII concentrations. Role of platelet factor XIII.

After fibrin polymerization, activated Factor XIII catalyzes the formation of intermolecular cross-links between gamma-chain pairs and also among two or more alpha-chains to form polymers. In this report we characterize the size and heterogeneity of alpha-chain polymers, establish the role of high concentrations of Factor XIII in determining the extent and rate of alpha-polymer formation, and also provide evidence that the Factor XIII required can be provided by platelets. Fibrin prepared from purified fibrinogen or platelet-deficient plasma contained a series of cross-linked alpha-chain polymers with Mr from 140,000 to 770,000 with a mean Mr difference of 32,000 consistent with a staggered, overlapping addition of monomers to the growing alpha-polymer chain. In plasma containing no platelets, alpha-polymer formation was incomplete with residual alpha-monomer remaining, but higher platelet counts facilitated more rapid cross-linking into larger polymers. Purified Factor XIII was equally effective as platelets in facilitating cross-linking. We conclude that cross-linked alpha-polymer chains are heterogeneous in size reaching a molecular weight of several million and that high concentrations of Factor XIII as provided by platelets are required for maximum cross-linking.

Blood Platelets↗
PubMed1989

The subunit composition of factor XIII proteins in normal and factor XIII deficient plasma and serum analysed by line immunoelectrophoresis.

Line immunoelectrophoresis was used for the characterization of human coagulation factor XIII in normal and factor XIII-deficient plasma and serum. In normal plasma, two immunoreactive factor XIII proteins termed XIII-p (Mr 330,000 Da) and XIII-s (Mr 170,000 Da) were identified within the beta-globulin fraction. Their reactions with monospecific antisera against known factor XIII subunits, suggests that the factor XIII-p and -s proteins recognized represent the factor XIII a2b2 tetramer and -b2 dimer, respectively. The concentration of the XIII-p protein was, in normal plasma, approximately 6 mg/l, in plasma from a case of congenital factor XIII, approximately 1 mg/l and in normal serum approximately 3 mg/l. The concentration of the XIII-s protein (approximately 18 mg/l) was unaffected by the coagulation process and normal in plasma and serum from the case of congenital factor XIII deficiency. Thus, the present investigation indicates the presence of an excess of the anticatalytic, DNA-binding factor XIII carrier protein in normal as well as in factor XIII-deficient plasma and serum.

Factor XIII↗
PubMed1992

A reversed activity staining procedure for detection of an acquired antibody against factor XIII in a girl with factor XIII deficiency.

A new method for detection of inhibitors against factor XIII is described. Agarose gel electrophoresis with normal platelet poor plasma as a factor XIII source included in the gel was combined with reversed activity staining. The procedure was applied to a 10-year-old girl with factor XIII deficiency where substitution therapy had failed. Plasma samples from the patient inhibited the factor XIII catalysed incorporation of the fluorescent monodansylthiacadaverine into casein at a position corresponding to the migration of gamma-globulins. Treatment with Sepharose-bound protein A effectively adsorbed the factor XIII antibody in the patient's plasma.

Antibodies↗
PubMed1991

Intracerebral haemorrhage due to acquired factor XIII inhibitor--successful response to factor XIII concentrate.

A 63-year-old woman presented with extensive bruising. An inhibitor to factor XIII was detected. Subsequent subcutaneous bruising and soft tissue haemorrhage into the left foot were treated with infusions of pasteurized factor XIII concentrate with good effect. Immunosuppression with cyclophosphamide was attempted but in spite of this she suffered a right cerebral haemorrhage necessitating further intensive therapy with factor XIII concentrate. This overcame the inhibitor, adequate post-infusion factor XIII levels were achieved and she made an excellent recovery. Factor XIII concentrate was well tolerated with no evidence of transmission of hepatitis or HIV infection. The inhibitor appeared to interfere with haemostasis by hindering the fibrin binding site of factor XIII, resulting in interference in clot-solubility tests. Subsequently the inhibitor resolved.

Blood Coagulation Tests↗
PubMed1996

Therapeutic factor XIII preparations and perspectives for recombinant factor XIII.

With the increasing availability of human plasma this source was used to substitute for the production of factor XIII concentrate from placenta. Prior to changing the source material, the virus safety in accordance with the Committee for Proprietary Medicinal Products (CPMP) guidelines and the half-life were investigated. Concerning the virus safety, the following cumulative log 10 clearance factors were obtained: human immunodeficiency virus (HIV) > or = 18.9, herpes simplex virus (HSV-1) > or = 21.5, polio > or = 19.1, bovine viral diarrhea virus (BVDV) > or = 13.3. Half-life studies of factor XIII from plasma in comparison with factor XIII from placenta were done in rabbits by determination of the antigen and in patients with congenital factor XIII deficiency by determination of the activity and antigen. In rabbits, the terminal half-life of the antigen was 78.2 hours for factor XIII from placenta and 87.0 hours for factor XIII from plasma. In patients the half-lives were similar: 9.2 days for activity and antigen of factor XIII from plasma and 8.5 days (activity) versus 9.4 days (antigen) for the placenta-derived factor XIII. Some further clinical studies with factor XIII concentrates are also reviewed. Newer developments concerning recombinant factor XIII, its expression, characterization, and properties are summarized. Concerning the physicochemical data, the behavior in plasma was characterized by the formation of high-molecular-weight complexes, and first in vivo results, the recombinant factor XIII product was comparable to the naturally occurring material.

Amino Acid Sequence↗
PubMed1990

Congenital factor XIII deficiency with treatment of factor XIII concentrate and normal vaginal delivery.

The outcome of all pregnancies complicated by congenital factor XIII (F XIII) deficiency has resulted in abortion without replacement therapy. We experienced a case with this disease and succeeded in normal vaginal delivery after treatment with weekly F XIII concentrate (Fibrogammin P, Behringwerke AG) during pregnancy. This 20-year-old woman, gravida 1, para 0, was found to have an F XIII level of 0% at age 6 and was treated with F XIII concentrate occasionally when she suffered from massive bleeding. In 1986 she became pregnant and was hospitalized at 6 weeks' gestation because of genital bleeding. Subsequent to this episode, F XIII concentrate was administered every week. At 37 weeks' gestation a 2,646-gram girl with a 1-min Apgar score of 9 was delivered. Postpartum blood loss was 260 ml. One year after delivery neither the mother nor the infant were found to have hepatitis B, nonA, nonB hepatitis, ATL or HIV. F XIII concentrate proved effective in such cases without any risk of viral infection.

Adult↗
PubMed1980

Characteristics of the factor VIII protein and Factor XIII in various factor VIII concentrates.

The in vitro properties of 5 factor VIII preparations (AHF-Kabi, Hemofil Hyland, AHF-Profilate Abbott, Kryobulin Immuno and Factorate High Purity Armour) and an ordinary cryoprecipitate were studied with reference to factor VIII clotting activity (VIII:C), factor VIII clotting antigen (VIII:CAg), factor VIII related antigen (VIIIR:Ag) (EI, IRMA, CIE), ristocetin cofactor activity (VIIIR:RCF), fibrinogen and factor XIII. All the preparations with the exception of Factorate had higher levels of VIII:CAg than VIII:C indicating inactivation of the biological activity of VIII:C during the procedure. AHF-Kabi (fraction I-0) and the cryoprecipitate, the only preparations capable of normalising the defect in patients with von Willebrand's disease, showed the same level of VIIIR:Ag determined by EI and by IRMA, while all the other preparations (i.e. cryoprecipitates purified further in different ways) had considerably lower levels of VIIIR:Ag determined by IRMA than by EI. Based on these in vitro techniques it seems to be possible to predict which preparations can be used successfully in patients with von Willebrand's disease, while no such conclusions can be made from VIIIR:RCF determinations. EI yielded similar concentrations of factor XIII a subunit in all the preparations tested. 3 functional assays showed high factor XIII activities in AHF-Kabi but low or no activities in the others. Thus, considerable differences were found on the in vitro properties of the proteins in 5 factor VIII concentrates and a cryoprecipitate. The action of proteases and the techniques used in the purification procedure are probably of crucial importance for the properties of the various factors.

Antigens↗
PubMedDate not supplied

[Factor XIII activity in the presence of suppression of the function of the anticoagulant system and its restoration in animals on an atherogenic ration].

With depressed function of the anticoagulation system in rats produced by their long-term maintenance on an atherogenic ration a rising fibrin-stabilizing activity of the XIII factor, by comparison with that in healthy animals and pertinent controls, is observed. A protracted administration to the animals with depressed function of the anticoagulation system of the compound "Linetol", that contains ethers of unsaturated fatty acids, given together with vitamin "A" results in a drastic fall of the factor XIII activity in the blood plasma with continued maintenance on the atherogenic diet.

Animals↗
PubMed2000

The role of gamma A/gamma ' fibrinogen in plasma factor XIII activation.

Factor XIII zymogen activation is a complex series of events that involve fibrinogen acting in several different roles. This report focuses on the role of fibrinogen as a cofactor in factor XIII activation by thrombin. We demonstrate that fibrinogen has two distinct activities that lead to an increased rate of factor XIII activation. First, the thrombin proteolytic activity is increased by fibrin. The cleavage rates of both a small chromogenic substrate and the factor XIII activation peptide are increased in the presence of either the major fibrin isoform, gammaA/gammaA fibrin, or a minor variant form, gammaA/gamma' fibrin. This enhancement of thrombin activity by fibrin is independent of fibrin polymerization and requires only cleavage of the fibrinopeptides. Subsequently, gammaA/gamma' fibrinogen accelerates plasma factor XIII activation by a non-proteolytic mechanism. This increased rate of activation results in a slightly more rapid cross-linking of fibrin gammaA and gamma' chains and a significantly more rapid cross-linking of fibrin alpha chain multimers. Together, these results show that although both forms of fibrin increase the rate of activation peptide cleavage by thrombin, gammaA/gamma' fibrinogen also increases the rate of factor XIII activation in a non-proteolytic manner. A revised model of factor XIII activation is presented below.

Amino Acid Sequence↗