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PubMed2004

Scleredema of Buschke: remission with factor XIII treatment.

We describe the case of a 55-year-old man with scleredema of Buschke of the torso complicated by insulin-dependent diabetes mellitus. Due to (i) the patient's poor general health status, (ii) the similarity between scleroderma and scleredema of Buschke, and (iii) the well known efficacy of factor XIII infusions in scleroderma, we attempted an intravenous treatment with factor XIII. This therapy resulted in marked increase of movements and in softening of the skin, together with ultrasonographic and histopathological improvements. In conclusion, to the best of our knowledge, this is the first case in which factor XIII has been successfully used for the treatment of scleredema of Buschke.

Diabetes Mellitus, Type 1↗
PubMed1993

Association of the A subunits of recombinant placental factor XIII with the native carrier B subunits from human plasma.

Interactions of a recombinant human placental protein (rA2) expressed in yeast and considered to be identical to the catalytic A2 subunits of factor XIII, the fibrin stabilizing factor zymogen, were examined with the native carrier subunits (B2) of the factor isolated from human plasma. Nondenaturing electrophoresis and HPLC gel-filtration experiments showed a tight binding of rA2 to B2 for forming an ensemble similar to that of plasma factor XIII (A2B2). In the presence of excess B2, however, some higher ordered oligomers (rA2Bn, where n > 2) were also seen in electrophoresis. The same technique revealed a microheterogeneity in the rA2 preparation; nevertheless, all isoforms could bind to B2. By employing an ELISA procedure for measuring free B2 in mixtures with rA2, an apparent binding constant of 4 x 10(7) M-1 was derived for the association of rA2 with B2. Fluorescence depolarization was used to monitor the heterologous association of rA2 with fluorescein-labeled B2F as well as the dissociation of the rA2B2F structure. The former was characterized by an increase, and the latter by a decrease, in the fluorescence anisotropy of the system. Binding of rA2 to B2F (pH 7.5, mu = 0.315, 37 degrees C) was not influenced by low concentrations of Ca2+ (< or = 30 mM), and rA2B2F proved to be quite stable under these conditions. Much higher concentrations of Ca2+, as well as higher ionic strengths, were required to dissociate this assembly. By contrast, release of B2F from the thrombin-modified rA2'B2F occurred rapidly in the presence of low concentrations of Ca2+ at low ionic strength.(ABSTRACT TRUNCATED AT 250 WORDS)

Calcium↗
PubMed1987

[Bronchiolo-alveolar carcinoma complicating systemic scleroderma under long-term treatment with factor XIII].

A 52-year old woman with systemic scleroderma had been treated since 1978 with factor XIII. The skin lesions had improved, and respiratory lesions had become stabilized. In 1984, she developed a bronchiolo-alveolar carcinoma which was treated by surgery. The authors emphasize that factor XIII is well tolerated and has beneficial effects on the skin and probably also on the lungs, without tachyphylaxis; however, the possibility of a bronchioloalveolar carcinoma occurring cannot be ruled out.

Adenocarcinoma, Bronchiolo-Alveolar↗
PubMed1992

[Factor XIII deficiency: blood coagulation defect in pregnancy].

Rare haemorrhagic disorders cause a lot of diagnostic and therapeutic problems to the obstetrician. By means of a pregnancy course and a birth process a report is given on the physiological drop of the factor XIII serum concentration and its difficult clinical interpretation. This paper presents pathophysiology, symptoms, complications and treatment of factor XIII deficiency in pregnancy.

Adult↗
PubMed1991

Congenital factor XIII deficiency. A family report.

Four sisters born to consanguineous muslim parents with a bleeding disorder since birth are presented. They also had prolonged umbilical cord bleeding and history of delayed wound healing. Since childhood, they have been developing spontaneous ecchymotic spots. Three out of four sisters had Factor XIII deficiency. Their mother's sisters, who have been developing ecchymotic spots were found to have normal clot stability and Factor XIII levels. Family study indicates autosomal recessive mode of inheritance of the congenital Factor XIII deficiency.

Adolescent↗
PubMed1984

Fibronectin and coagulation factor XIII increases blood platelet adhesion to fibrin.

Fibronectin is covalently linked to fibrin during clot formation by coagulation factor XIII and has been suggested as a possible mediator of platelet adhesion to collagen. Fixed human platelets were found to adhere to fibrin. This adhesion was significantly increased when fibronectin was incorporated into the fibrin network, and was supported by factor XIII.

Factor XIII↗
PubMed1982

[Studies on the physiological changes of blood coagulation factor XIII during pregnancy and their significance (author's transl)].

We measured the blood coagulability in pregnancy. Factor XIII, that showed unusual variations in these experiment, was investigated for its biological significance. The results are summarized as follows: 1) Blood coagulation factors XII, IX, VIII, VII and X, prothrombin and plasminogen showed a increasing tendency as the course of pregnancy. These was not very much change in factor V and plasmin activity during pregnancy. Factor XI showed a decreasing tendency. The further dramatic variation appeared in each coagulation factor at the onset of labor. 2) With regards to the factor XIII, XIII-S a carrier protein was inclined to increase from the value of 94.0 +/- 16.0% before pregnancy and reached the value of 109 + 16.3% at the last stage of pregnancy, while XIII-A an active site showed a decreasing tendency from 97.5 + 17.5% before pregnancy to 67.0 + 12.0%. 3) In placenta homogenate XIII-A was observed, but XIII-S absent. In retro-placental blood XIII-S was observed, but no XIII-A was seen. No significant difference between uterine venous blood and maternal peripheral blood was recognized. 4) The placental localization of XIII-A was investigated by the methods of fluorescent antibody technique and enzyme labeled antibody technique. XIII-A appeared in syncitiotrophoblast, but was not found in stroma, vessel wall and fetal side. In regards to decidua region its presence was not confirmed.

Factor IX↗
PubMed1997

Crosslinking kinetics of the human transglutaminase, factor XIII[A2], acting on fibrin gels and gamma-chain peptides.

Factor XIII is the terminal enzyme of the coagulation cascade which serves to rapidly crosslink the adjacent gamma-chain C-termini of fibrin clots. In vivo, this process is initiated by the proteolytic action of thrombin which simultaneously converts both soluble fibrinogen to fibrin and activates zymogen FXIII; fibrin then spontaneously polymerizes to form a gel which activated FXIII stabilizes through crosslinking. Due to the kinetic complexity and the difficulty of investigating gel phase reactions, methods employing pre-activation of recombinant human Factor XIII (rFXIII[A'2]) were developed to effectively decouple these reactions. By utilizing these methods, the kinetic parameters of gamma-chain crosslinking in fibrin gels could be determined by both initial rate and integrated rate techniques under physiologically relevant conditions. The crosslinking of the gamma-chain of fibrin gels could be described by apparent Michaelis kinetics with K(m)(app) = 6.2 microM, kcat = 1872 min-1, and Ksp = 302 min-1 microM-1 for a fibrin gamma-chain monomer of M(r) = 170000 Da. In contrast, both the crosslinking rates of alpha-chains within fibrin gels (Ksp = 0.38 min-1 microM-1: Bishop et al. (1993)) and the crosslinking of a soluble synthetic peptide containing the unique gamma-chain fibrin crosslinking site (Ksp = 0.030 min-1 microM-1) could not be shown to saturate and gave apparent first-order rates with respect to rFXIII[A'2]. These observations coupled with the large differences in the turnover rates (approximately 10(4)) suggest two likely mechanisms for FXIII[A'2]-substrate interactions: (1) random (or independent) binding of non- or weakly interacting substrate pairs imposes a high entropic barrier (i. e., delta Gbinding) to the formation of a productive catalytic complex, e.g., for soluble gamma-chain peptides and the flexible alpha-chains within fibrin, and (2) binding to an oriented substrate pair effectively lowers the entropic barrier to formation of a Michaelis complex and thus greatly enhances the rate of catalysis, e.g., for gamma-chain pairs within the fibrin fibrils.

Amino Acid Sequence↗
PubMed1976

gamma-dimerization, alpha-polymerization, and plasmin degradation of human fibrin. Effect of various inhibitors of factor XIII on the patterns in SDS-electrophoresis and crossed immunoelectrophoresis.

The effect of different factor XIII inhibitors (competetive inhibition, interference with active center SH-groups in different ways, Ca2+ depletion) on the sequence of the gamma-dimerization and alpha-polymerization of fibrin is examined by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAE) (reduced material). They all inhibit either gamma-dimerization and alpha-polymerization or alpha-polymerization alone irrespective of the factor XIII inhibitory mechanism. Non-crosslinked fibrin and fibrin clots of different degrees of crosslinking are digested with plasmin and the lysate tested in SDS-PAE (non-reduced material) and crossed agarose gel immunoelectrophoresis (CAIE). The digests contain Fragment D and Fragment D-D respectively and Fragment E. An additional Fragment E with less anodic mobility in CAIE, and not demonstrable in SDS-PAE, is seen in increasing amounts with increasing gamma-dimerization, alpha-polymerization does not further change the CAIE patterns.

Animals↗
PubMedDate not supplied

Concentrations of factor VIII-related antigen and factor XIII during open heart surgery.

Plasma levels of factor VIII-related antigen (fVIIIRA) and factor XIII S and A subunits (fXIIIS, fXIIIA) were assayed by counterimmunoelectrophoresis before, during, and after cardiopulmonary bypass (CPB) in patients with coronary artery and valvular heart disease to define the basis for clinical and laboratory abnormalities of hemostasis occurring in this form of surgery. During CPB, concentrations of fXIIIA dropped in both patient groups but returned to preoperative levels promptly after pump removal. In contrast, fVIIIRA and fXIIIS, which are not incorporated into the clot, remained unchanged even during fluid administration. These data provide evidence of a transient consumption coagulopathy as a feature of CPB. Hemodilution probably plays a secondary role in these changes.

Antigens↗
PubMed1992

Immunocytochemical detection of factor XIII A--subunit in acute leukemia.

Factor XIII (FXIII) is a plasma pro-transglutaminase consisting of A and B subunits in a tetrameric structure. A cellular form of FXIII consisting exclusively of A subunits exists in platelets and monocytes: monocyte FXIII may be involved in connective tissue organization. To evaluate the expression and diagnostic significance of FXIII A subunit (FXIIIA) in acute leukemia, we performed an immunocytochemical study (PAP technique) with rabbit antiserum against FXIIIA on leukemic blasts of 48 cases. FXIIIA was detected only in myelomonocytic (M4), monocytic (M5) and megakaryocytic (M7) cases: in M4 and M5 samples the amount of blast cytoplasmic FXIIIA was closely correlated with the expression of monocyte-specific antigenic and cytochemical markers. Our data show immunocytochemical detection of FXIIIA to be useful for acute leukemia characterization.

Acute Disease↗
PubMed2002

Factor XIII mediates adhesion of platelets to endothelial cells through alpha(v)beta(3) and glycoprotein IIb/IIIa integrins.

Coagulation factor XIII (FXIII) is a transglutaminase that catalyzes crosslink formation in fibrin clots. Endothelial cells (EC) were demonstrated to bind FXIII via their alpha(v)beta3 integrin receptor. FXIII was also shown to bind platelet glycoprotein IIb/IIIa receptor. In the present study, we analyzed if FXIII can mediate platelet-EC interaction. Both FXIII and activated FXIII (FXIIIa) bound to EC monolayers; this binding was enhanced by the addition of Mn2+ and was inhibited by the monoclonal antibody L609 against alpha(v)beta3 integrin. Normal washed platelets also bound surface-immobilized or soluble FXIII and FXIIIa, and the binding was GPIIb/IIIa dependent. The effect of FXIII concentrate (Fibrogammin-P) treatment on the interaction of ECs with platelets from six FXIII-deficient patients was studied. Patients' platelets were radiolabeled with 3H-Adenine, washed, resuspended in autologous plasma and allowed to adhere to immortalized EC line EAhy926. Adhesion of platelets from FXIII-deficient patients to ECs increased 1.7+/-0.4-fold (P=.01) following intravenous infusion of FXIII concentrate. Similarly, addition of 1 U/ml of FXIII concentrate to the patients' PRP in vitro increased the adhesion 1.8+/-0.5-fold (P=.008). Preincubation of the EC monolayers with increasing concentrations of either FXIII or FXIIIa augmented the adhesion of normal washed platelets to ECs in a dose-dependent manner. At 10 U/ml of EC-bound FXIII or FXIIIa, platelet adhesion enhanced 1.7+/-0.25-fold (P=.03) and 2.5+/-0.5-fold (P=.02), respectively. The increase in platelet adhesion was completely abolished by pretreatment of ECs with the anti-alpha(v)beta3 antibody L609 or by preincubation of the platelets with the GPIIb/IIIa inhibitor Abciximab. Taken together, our data indicate that FXIII mediates the interaction of platelets with ECs by bridging between endothelial alpha(v)beta3 and platelet GPIIb/IIIa integrins. This interaction may be relevant for tissue remodeling and wound repair after vascular injury in FXIII-deficient patients.

Cell Line↗
PubMed1999

[Congenital factor XIII deficiency in pregnancy. A case report].

Congenital factor XIII deficiency is a rare hemorrhagic syndrome with an altered fibrin stability, hemorrhagic diathesis and habitual abortions. After a short introduction, a case report is described and the clinical differences between plasmatic and platelet deficiency pointed out.

Adult↗
PubMed1984

A new rapid and simple assay for factor XIII activity using dansylcadaverine incorporation and gel filtration.

A new sensitive, reproducible and simple assay for factor XIII activity was developed, in which fluorescent dansylcadaverine (DC) is incorporated into casein and DC-casein is separated from free DC by gel filtration. A good correlation was found between our method and Lorand's. The main advantages of our method are: (1) our assay technique is simple with good reproducibility and takes only a couple of hours; (2) the detectable limit of factor XIII activity is about 1% of normal pool plasma, but, if necessary, can be lowered by increasing the sample amount and lengthening the reaction time.

Cadaverine↗
PubMed1989

On the location in the thrombin B chain of substrate recognition sites for fibrinopeptide release and factor XIII activation.

Thrombin, a serine proteinase comprised of two disulfide-linked subunits (A chain and B chain), induces clotting by releasing fibrinopeptide A from fibrinogen and then influences the character of the resulting fibrin by releasing fibrinopeptide B and by activating factor XIII. While the active center of thrombin is known to reside in its B chain, the subunit location of the structural determinants that govern the specific release of fibrinopeptides A and B and the activation of factor XIII have not been established. We have investigated the subunit location within the thrombin molecule of the determinants of substrate specificity for these actions using an isolated, immobilized B-chain preparation. Isolated B chain was prepared by covalently linking the intact thrombin molecule to Sepharose beads via the carbohydrate chain attached to asparagine 53 of its B chain, then reducing the single interchain disulfide bond to release the A chain, and finally reoxidizing the intrachain disulfide bonds of the immobilized B chain, allowing it to refold. The isolated, immobilized B chain of thrombin induced clotting of purified fibrinogen, releasing both fibrinopeptides A and B as demonstrated by HPLC and by electrophoresis of reduced fibrin chains. In addition, the B-chain preparation activated added factor XIII, yielding electrophoretically characteristic cross-linked fibrin chains.

Animals↗
PubMed1991

Congenital factor XIII deficiency: two case reports.

Two patients with factor XIII deficiency, presenting with bleeding disorder since birth, are reported. The condition is rare and is likely to be missed unless clot solubility in 5 M urea is performed as a screening test in all patients with bleeding disorders. A correct diagnosis is essential as prophylactic management is practicable in this disorder.

Adult↗
PubMed1993

Molecular cloning of the b subunit of mouse coagulation factor XIII and assignment of the gene to chromosome 1: close evolutionary relationship to complement factor H.

The b subunit of human coagulation factor XIII (FXIII-b) is composed of 10 short consensus repeats (SCRs) characteristic of the regulatory proteins of complement activation system. A full-length cDNA clone of mouse FXIII-b was isolated and the entire sequence was determined. The predicted amino acid sequence showed 77.5% homology with human FXIII-b, although mouse FXIII-b contained seven extra amino acid residues at the carboxyl terminal. The strong reactivity of the translation product of this clone with rabbit anti-human FXIII-b antiserum confirmed that it encodes a mouse counterpart of the human FXIII-b. By in situ hybridization and mapping studies using 66 interspecific backcross mice, the mouse FXIII-b gene (designated F13b) was shown to be located on distal chromosome 1 closely linked to Cfh, extending a conserved linkage group between human and mouse chromosome 1. In addition, a significant structural similarity between FXIII-b and complement factor H is described.

Amino Acid Sequence↗