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At least 379 records · Page 21Linked to original sources
PubMed1978

[Twin pregnancy in a patient with Glanzmann disease (congenital thrombasthenia) (author's transl)].

Report on a 30-year old primigravida with a family history of bleeding and a personal history of nasopharyngeal bleeding since age four. Severe menorrhagia since her menarche. First seen at 20 weeks gestation with naso-pharyngeal bleeding and a twin pregnancy. The patient was found to have Glanzmann's disease (congenital thrombasthenia) with an excessive lack of factor XIII. Ambulatory treatment with packed cell transfusions until 35 weeks gestation. The thrombelastogram did not improve with transfusions of platelet concentrates. In-patient treatment from 35 to 37 weeks gestation, no vaginal bleeding throughout the pregnancy. Elective Caesarean hysterectomy at 37 weeks gestation with lo units fresh blood, 3 units platelet concentrate and 10 ampules factor XIII concentrate in readiness. Delivery of twin girls 3180 and 3050 g without signs of Glanzmann's disease. Treatment of the maternal bleeding by replacement. Factor XIII 80% of normal 8 weeks postpartum. This appears to be the first case of twin pregnancy in the presence of Glanzmann's disease and the fourth case in the world literature.

Adult↗
PubMedDate not supplied

Failure to measure plasma activated factor XIII during disseminated intravascular coagulation.

The search for activated products of coagulation factors in blood is of considerable clinical interest because its detection would indicate activation of the clotting system. Factor XIII circulates as inactive zymogen and becomes enzymatically active after thrombin or factor Xa activation. Employing an amine-incorporating system, activated factor XIII was measured in normal and pathological plasma from leukemic patients with overt laboratory signs of disseminated intravascular coagulation (DIC). Only traces of the activated factor were detected in both normal and DIC plasma. The method, sensitive and specific, as shown by the results of measurements on the plasma of 8 patients with congenital deficiency and on normal serum, did not prove to be useful for detecting pathological in vivo thrombin generation.

Acute Disease↗
PubMed2002

[Factor XIII in man: a review].

Activated by calcium and thrombin, factor XIII (FXIIIa) cross-links fibrin, thus increasing the stability of the fibrin clot. Furthermore, the hemostatic and reparative function of factor XIIIa is mediated by cross-linking other proteins like alpha(2)-plasmin-inhibitor, fibronectin, and collagen. The FXIII Val34Leu polymorphism plays a role in athero- and thrombogenesis. FXIII deficiency is an autosomal recessive disorder. The most common symptom is the bleeding tendency of the umbilical cord some days after birth. The diagnosis is confirmed by a solubility clot test in urea (5 mol/l) and then differentiated with an incorporation assay and immuno-electrophoresis. The bleeding tendency typically becomes obvious when FXIIIa activity is <1-2%. Severe bleeding episodes, however, may even occur with FXIIIa activities of 30-50%, especially in heterozygous persons. The sometimes life-threatening bleeding tendency of the inherited FXIII deficiency can be treated with FXIII concentrates. Acquired FXIII deficiency occurs in several internal diseases and after major surgery. The clinical significance is not completely clear. Moreover, FXIII is applied locally as a component of fibrin glues.

Factor XIII↗
PubMed1999

Factor VIII/von Willebrand factor complex in methylene blue-treated fresh plasma.

BACKGROUND: The effect of virus inactivation of fresh plasma with methylene blue has been studied on the factor VIII/von Willebrand factor molecular complex (FVIII/vWF), factor XIII, and fibrinogen. STUDY DESIGN AND METHODS: FVIII function or activity, vWF activity, vWF antigen, vWF:Ag, vWF multimeric structure, fibrinogen, and factor XIII were analyzed in paired samples of control fresh plasma (untreated) and the same fresh plasma treated with methylene blue. Treated plasma was filtered (0.8-1.2 microm), mixed with a methylene blue solution (300 microg/L), and illuminated at 50,000 lux for 30 minutes on both sides. RESULTS: Average loss of biologic activity of coagulation factors studied was 25 percent (FVIII function, 29%; fibrinogen, 39%; factor XIII, 16%; and vWF activity, 18%). Reduction in vWF activity was significantly lower than that in FVIII function (p<0.05), and the vWF multimeric structure did not show alterations. CONCLUSION: Methylene blue-treated plasma and the cryoprecipitates obtained from it may be effective for replacement therapy in cases of von Willebrand disease and deficiencies of factor XIII and fibrinogen, but the clinical studies are needed to verify that possibility.

Dimerization↗
PubMed2006

Does FXIII deficiency impair wound healing after myocardial infarction?

Inadequate healing of myocardial infarction may contribute to local expansion of the infarct, frequently leading to chamber dilation, heart failure, or myocardial rupture. Experimental evidence in mouse models suggests that Factor XIII might play a key role in wound healing, and low persistent values lead to increased incidence of cardiac rupture following myocardial infarction. Here we would like to share our initial clinical experiences with strikingly similar observations in patients with this grave disease, and compare these observations to experimental findings.

Animals↗
PubMed1995

An acquired hemorrhagic disorder of fibrin crosslinking due to IgG antibodies to FXIII, successfully treated with FXIII replacement and cyclophosphamide.

We report a new case of severe bleeding diathesis due to an acquired inhibitor of fibrin crosslinking. The patient, an 80-year-old woman, was admitted to the hospital for a massive subcutaneous hematoma, with severe anemia requiring red cell transfusion; a subsequent retroperitoneal hematoma developed 2 weeks later. Coagulation studies were normal except for a thromboelastographic pattern suggestive of FXIII deficiency. Clot solubility test was abnormal even after 1:1 mix with normal plasma. Immunochemical studies confirmed the presence of a monoclonal IgG lambda inhibitor directed against FXIII activity (type II FXIII inhibitor). The patient IgG fraction selectively inhibited FXIII transamidating activity but did not inhibit the thrombin-mediated activation of FXIII. The patient was treated with high doses of FXIII concentrate to overcome the inhibitor and immunosuppressive therapy with cyclophosphamide and discharged in good conditions. High doses of commercially available FXIII appear to be a safe and effective method of controlling acute episodes of bleeding in patients with acquired FXIII deficiency.

Aged↗
PubMed1984

The molecular form of alpha 2-antiplasmin with affinity for plasminogen is selectively bound to fibrin by factor XIII.

Two molecular forms of alpha 2-antiplasmin (PB = plasminogen-binding; NPB = non-PB) exist. We have studied the extent of binding of these two forms to fibrin by factor XIII. A modified crossed immunoelectrophoresis technique which separately determines both forms showed that, compared with plasma, the PB-form is reduced by 31 +/- 11% (SD) in serum of twelve individuals and the NPB form by only 6%. Laurell assay showed a reduction of 18 +/- 9% (n = 12) in total alpha 2-antiplasmin antigen (PB + NPB) in serum; the immediate plasmin inhibition test (mainly recording the PB-form) revealed 35 +/- 6% (n = 12) reduction in inhibition. Coagulation of blood, platelet-rich and platelet-poor plasma yielded comparable results. No decrease in alpha 2-antiplasmin or change in its composition was observed when factor XIII-deficient plasma was clotted. Fibrin binding was not significantly different from normal in either plasminogen-depleted or plasminogen-enriched plasma. It is concluded that the PB-form of alpha 2-antiplasmin becomes selectively bound to fibrin.

Binding Sites↗
PubMed2003

Calibrated automated thrombin generation measurement in clotting plasma.

Calibrated automated thrombography displays the concentration of thrombin in clotting plasma with or without platelets (platelet-rich plasma/platelet-poor plasma, PRP/PPP) in up to 48 samples by monitoring the splitting of a fluorogenic substrate and comparing it to a constant known thrombin activity in a parallel, non-clotting sample. Thus, the non-linearity of the reaction rate with thrombin concentration is compensated for, and adding an excess of substrate can be avoided. Standard conditions were established at which acceptable experimental variation accompanies sensitivity to pathological changes. The coefficients of variation of the surface under the curve (endogenous thrombin potential) are: within experiment approximately 3%; intra-individual: <5% in PPP, <8% in PRP; interindividual 15% in PPP and 19% in PRP. In PPP, calibrated automated thrombography shows all clotting factor deficiencies (except factor XIII) and the effect of all anticoagulants [AVK, heparin(-likes), direct inhibitors]. In PRP, it is diminished in von Willebrand's disease, but it also shows the effect of platelet inhibitors (e.g. aspirin and abciximab). Addition of activated protein C (APC) or thrombomodulin inhibits thrombin generation and reflects disorders of the APC system (congenital and acquired resistance, deficiencies and lupus antibodies) independent of concomitant inhibition of the procoagulant pathway as for example by anticoagulants.

Anticoagulants↗
PubMed1974

Electroimmunoassay of plasma subunits-a and -s in a case of congenital fibrin stabilizing factor deficiency.

Antigenic material related to the fibrin stabilizing factor (Factor XIII-FSF) has been found in all the examined patients with congenital deficiency, albeit in reduced amount. Recently, Bohn et al. (1973) showed that plasma Factor-XIII is composed by two subunits, A (or a) and S (or b); the former active protein, the latter probably FSF-vinding protein. Using specific anti-S and anti-A antisera the Authors found, in a case of congenital deficiency of factor XIII, absence of subunit A. Subunit S presented abnormal behaviour as demonstrated by means of quantitative immunoelectrophoresis according to Laurell.

Blood Coagulation Tests↗
PubMedDate not supplied

Late hemorrhagic disease of the newborn as a cause of intracerebral bleeding.

We report a case of a 4-week-old female who presented with late hemorrhagic disease of the newborn (HDN). The newborn was previously healthy, and she received 1 mg of intramuscular vitamin K at birth. She was exclusively breast-fed. At 4 weeks she began bleeding at the umbilicus and 4 days after she suffered an intracranial hemorrhage. Coagulation studies showed a deficiency of vitamin K-dependent coagulation factors, and the normalization of all clotting studies after administration of vitamin K confirmed the diagnosis of HDN. Our conclusions are that physicians must be alert to mild bleeding in newborns and that prophylaxis with 1 mg of intramuscular vitamin K at birth may be insufficient to prevent late HDN.

Age of Onset↗
PubMed2000

A modified, optimized kinetic photometric assay for the determination of blood coagulation factor XIII activity in plasma.

BACKGROUND: Blood coagulation factor XIII (FXIII) is a zymogen that is transformed into an active transglutaminase by thrombin and Ca(2+). FXIII plays an essential role in fibrin stabilization and in the protection of fibrin from proteolytic degradation. No convenient method has been available for the measurement of FXIII activity in plasma. The aim of the present study was to improve and optimize a kinetic photometric FXIII assay originally developed in our laboratory. METHODS: In the assay, FXIII was activated by thrombin and Ca(2+). Fibrin polymerization was prevented by an inhibitory tetrapeptide. Glycine-ethyl ester and a glutamine residue of a synthetic dodecapeptide served as acyl acceptor and acyl donor transglutaminase substrates, respectively. The amount of ammonia released during the reaction was monitored using glutamate dehydrogenase and NADPH. RESULTS: The use of a new glutamine substrate and optimization of activator and substrate concentrations increased sensitivity. Substitution of NADPH for NADH and introduction of an appropriate blank eliminated systemic overestimation of FXIII activity. The recovery of FXIII was 96%, the assay was linear up to 470 U/L, the detection limit was 1 U/L, and the imprecision (CV) was <8% even at very low FXIII activities. A reference interval of 108-224 U/L (69-143%) was established. The results correlated well with results obtained by an immunoassay specific for plasma FXIII. CONCLUSIONS: The optimized FXIII assay is a simple, rapid method for the diagnosis of inherited or acquired FXIII deficiencies and increased FXIII concentrations. It can be easily adapted to clinical chemistry analyzers.

Adult↗