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PubMed1976

Purification and immunochemical characterization of human plasma factor XIII.

A detailed study of the conditions for purification of plasma factor XIII was undertaken and an optimal procedure developed. This procedure involves adsorption with aluminum hydroxide, repeated fractionation with ammonium sulfate, heat denaturation of fibrinogen, precipitation with polyethylene glycol, cryoprecipitation, and chromatography on DEAE-cellulose with gradient elution. The specific activity of the final product, as measured by the fluorescent amine incorporation assay for factor XIII, averages about 3,000-4,000 mumol dansylcadaverine incorporation/mg protein. The yield is about 20%. In SDS electrophoresis the final product has two bands under nonreducing conditions, characteristic of the a and b subunits.

Ammonium Sulfate↗
PubMed1997

Fibrinolytic and factor XIII activity in subarachnoid hemorrhage.

The balance between fibrinolytic activity and coagulation mechanisms seems to play an important role in the rebleeding of a subarachnoid hemorrhage (SAH) due to aneurysmatic rupture. In the present paper we describe our findings in a group of patients (n 10) with SAH. The plasmatic levels of fibrinogen and their degradation products (FDP), APTT, prothrombin activity and factor XIII were determined within 72 hours of initial bleeding or of eventual rebleeding. Factor XIII activity in the first bleeding was 82.1 +/- 4%, while the levels of FDP were 3.8 +/- 1 micrograms/ml. In patients presenting rebleeding (n 4), Factor XIII activity was 67.3 +/- 4.5% the day it manifested, which is significantly less than the values previously observed (p < 0.01), while the FDP level was 4.1 +/- 2 micrograms/ml. The decrease of factor XIII activity suggests an important role as regards clot stability in rupture location. It is also possible to attribute a rebleeding predictive value to its activity reduction.

Adult↗
PubMed1995

Mutations causing coagulation factor XIII subunit A deficiency: characterization of the mutant proteins after expression in yeast.

We identified the mutations causing factor XIII A subunit deficiency in two families. Two distinct mutations were identified in the S family: the nonsense mutation Tyr 441-->stop in exon 11, inherited through the paternal line, and the missense mutation Asn 60-->Lys in exon 3, inherited through the maternal line. Two members of the J family were heterozygous for the previously described type 3 A subunit. The substitution giving rise to the type 3 variant was found to be Gly 501-->Arg in exon 12. The Asn 60-->Lys and Gly 501-->Arg mutations were constructed in cDNA clones and expressed in yeast (Saccharomyces cerevisiae AH22). Although mRNA could be detected, protein containing the Asn 60-->Lys substitution could not be detected, suggesting extreme instability or susceptibility to proteolysis. A subunits containing the Gly 501-->Arg substitution were expressed and found to be enzymatically active in fresh yeast lysates. This variant has thermal instability and lost activity during storage or purification. Gel filtration studies suggested that the type 3 variant assembled as a dimer, as do normal A subunits. The data suggest that the Gly 501-->Arg (Type 3 variant) would cause severe factor XIII deficiency if inherited in the homozygous form or as a compound heterozygote with another deleterious mutation.

Adult↗
PubMed2004

Morphologic changes in neo-intimal proliferation in an experimental aneurysm after coil embolization: effect of factor XIII administration.

We investigated histological changes in aneurysmal orifices after embolization with Guglielmi detachable coils (GDCs) and determined the effects of the wound-healing factor, factor XIII, on promoting intimal proliferation by scanning electron microscopy (SEM). GDC embolization was performed in an experimental model of aneurysm in swine. In the control group (17 aneurysms), the aneurysms were resected immediately after surgery, at 1 and 3 weeks after the procedure. In the factor XIII-administered group (13 aneurysms), the swine received factor XIII postoperatively, and the aneurysms were excised at 1 and 3 weeks. The endothelial cell proliferation changes in the aneurysm orifices in both groups were evaluated by SEM. The histological changes at the orifices began immediately after the procedure, and endothelialization was observed at 1 week. One week after the procedure, the rate of endothelial cell proliferation was significantly higher in the factor XIII group (P<0.05). But no difference was observed at 3 weeks, when endothelialization of the orifices was essentially completed. The process of intimal proliferation after coil embolization was similar to the wound-healing process after vascular intimal injury. Administration of the wound-healing factor, factor XIII, would contribute rapid intimal proliferation and may be effective to facilitate complete obliteration of aneurysms after coil embolization.

Animals↗
PubMedDate not supplied

[Binding of alpha-2-antiplasmin with fibrinogen/fibrin and their fragments independent of factor XIII].

Possible interaction of alpha-2-antiplasmin with fibrinogen, fibrin and their fragments independent of factor XIII as well as the inhibitor effect on the Glu-plasminogen activation by tissue activator were studied. It was shown that alpha-2-antiplasmin is adsorbed on desAA- and desAABBfibrin films (Kd 69.0 +/- 1.0 nM 68.6 +/- 5.3 nM, respectively). Glu-Plasminogen has no effect on the inhibitor binding with desAABBfibrin. Alpha-2-antiplasmin shows strong affinity for fibrin D-dimer (Kd 65.0 +/- 4.0 nM) and D-fragment of fibrinogen (Kd 119.0 +/- 21.0 nM), but it does not interact with E-fragment. The inhibitor inside the fibrin clot decreases 10 times the activation rate of Glu-plasminogen by the tissue activator both is the presence and without factor XIII at physiological ratio of Glu-plasminogen, tissue activator, fibrin and alpha-2-antiplasmin. Thus we have shown that fibrinogen/fibrin binds alpha-2-antiplasmin independent of the factor XIII. Binding sites of the inhibitor are localized in D-fragment of fibrinogen and/or fibrin D-dimer. Alpha-2-antiplasmin inhibits the Glu-plasminogen activation by tissue activator on fibrin.

Animals↗
PubMed1988

Hemostasis in Crohn's disease: low factor XIII levels in active disease.

Massive gastrointestinal hemorrhage sometimes occurs in Crohn's disease. To examine the possible role of acquired disorders of hemostasis contributing to such events, several laboratory indicators of hemostasis (APT time, Normotest, platelet count, bleeding time, fibrinogen, factor VIII activity, vWF:Ag, factor X, factor XIII, antithrombin III, fibrinopeptide A, and B beta(15-42] were studied in 10 patients with active Crohn's disease (Crohn's disease activity index (CDAI) greater than 150) and 10 patients with quiescent disease (CDAI less than 150). Marked thrombocytosis was seen in three patients with active disease. Factor VIII activity and fibrinogen levels were significantly elevated in patients with Crohn's disease (p less than 0.001), and the factor VIII activity levels were significantly higher (p less than 0.05) in the patients with active disease than in those with quiescent disease. Factor XIII levels were significantly lower (p less than 0.02) in patients with active disease. Three of the patients with active disease had factor XIII levels below the lower reference limit. The two patients with the lowest levels had hemorrhagic diarrhea and spontaneous bleeding from the rectal mucosa. Fibrinopeptide A and B beta(15-42) levels were significantly elevated in both groups. The other coagulation analyses were essentially normal in both patient groups. The results suggest that factor XIII deficiency acquired through gastrointestinal leakage may contribute to gastrointestinal hemorrhage in some patients with active Crohn's disease.

Adolescent↗
PubMed2003

Surgery in severe factor XIII deficiency: report of a case of epilepsy neurosurgery and review.

Factor XIII (FXIII) deficiency is a rare autosomal recessive congenital disorder of haemostasis, associated with a high risk of intracranial haemorrhage. Intracranial haemorrhage can result in neurological sequelae including seizure disorders. In some cases, medically intractable epilepsy led to epilepsy surgery. Little has been reported on the management of FXIII deficiency during surgery, and there is only a few data on the management, safety and efficacy of epilepsy surgery in the patients with haemostatic disorder. We report here an epilepsy neurosurgery in a case of severe FXIII deficiency.

Child, Preschool↗
PubMed2001

Polymorphisms of coagulation factor XIII subunit A and risk of nonfatal hemorrhagic stroke in young white women.

BACKGROUND AND PURPOSE: Although family studies have suggested a genetic influence on hemorrhagic stroke, the underlying genetic risk factors remain poorly defined. Coagulation factor XIII, which is involved in hemostasis, fibrinolysis, vascular remodeling, and tissue repair, represents a candidate gene for hemorrhagic stroke. We assessed the potential role of 3 factor XIII subunit A coding-sequence polymorphisms, along with a promoter polymorphism of plasminogen activator inhibitor-1 (PAI-1, which is also involved in fibrin stabilization and vascular remodeling), in young white women with hemorrhagic stroke. METHODS: Genotype analysis for factor XIII subunit A Val34Leu, Tyr204Phe, and Pro564Leu and for PAI-1 -675 4G/5G was performed in a population-based case-control study of 42 white women aged <45 years with nonfatal hemorrhagic stroke and 345 demographically similar control subjects. RESULTS: Compared with the respective homozygous wild-type genotypes, the Tyr204/Phe204 genotypes (age-adjusted odds ratio [OR] 2.9, 95% 95% CI 1.1 to 7.5) and the Leu564/Leu564 genotype (OR 4.3, 95% CI 1.4 to 13.7) were each associated with an increased risk of nonfatal hemorrhagic stroke. The risk estimate associated with the Phe204 variant was highest in women with subarachnoid hemorrhage and in nonsmokers, whereas the risk estimate of the Leu564/Leu564 genotype was highest in women with intracerebral hemorrhage and in smokers. Women who carried either the Phe204 allele or the Leu564/Leu564 genotype in combination with the PAI-1 5G/5G genotype had a nearly 20-fold increased risk of hemorrhagic stroke (OR 18.9, 95% CI 3.8 to 95.1). CONCLUSIONS: Our findings suggest that the Phe204 and Leu564 variants of coagulation factor XIII may be markers for genetic susceptibility to hemorrhagic stroke in women aged <45 years.

Adolescent↗
PubMed2002

Factor XIII and tissue transglutaminase antibodies in coeliac and inflammatory bowel disease.

Tissue transglutaminase (tTg) has been identified as an autoantigen in coeliac disease (CD). There is a marked homology between different forms of transglutaminase, such as tTg and coagulation factor XIII. We compared titres of both IgA- and IgG-antibodies against these two antigens in 20 CD patients, 20 endomysial antibody (EMA)-negative controls and a group with inflammatory bowel disease (34 with Crohn's disease and 23 with ulcerative colitis). IgA-antibodies against tTg correlated with EMA titres and had high sensitivity and specificity in screening for CD. Only in two CD patients were high titres found of IgA-antibodies against factor XIII, non-reactive with tTg. Both lacked bleeding tendency. The presence of IgG-antibodies against tTg, in contrast, had low sensitivity and specificity in screening for CD and were frequently seen in inflammatory bowel disease. Similarly, factor XIII IgG-antibodies displayed a non-specific pattern with modestly elevated titres in patients with Crohn's disease and in both EMA-negative and positive patients. Despite a marked homology with tTg, the occurrence of high titre IgA-antibodies against factor XIII is infrequent in CD, but may-when present-be the result of epitope spreading. The presence of IgG-antibodies in CD and inflammatory bowel disease illustrates the complexity of autoantibody reactions in gastrointestinal disease.

Adult↗
PubMed1988

Characterisation of connective tissue cells containing factor XIII subunit a.

Paraffin embedded sections of human liver, lymph node, and placenta showed that certain connective tissue cells were positive for factor XIII subunit a. These cells were further characterised by double immunofluorescence labelling and by combined immunofluorescence and enzyme cytochemical staining on frozen sections. They were labelled by the monoclonal antibodies RFD7 and anti-Leu M3 (markers of the macrophage cell line) but gave a negative reaction for the fibroblast marker IIG10 and showed no alkaline phosphatase activity. Immunoblotting detected factor XIII subunit a in macrophages isolated from placenta but not in human fibroblasts. At lower dilutions, the commercially available antibody against the b subunit of factor XIII also positively reacted with the same cell population. The facts that immunoblotting showed that the antiserum crossreacted with the a subunit and that placental macrophages did not stain strongly for the b subunit also indicate that this antigen is not present in adult connective tissue cells.

Connective Tissue↗
PubMed1998

A founder effect is proposed for factor XIII B subunit deficiency caused by the insertion of triplet AAC in exon III encoding the second Sushi domain.

We previously concluded that genetic defects in the B subunit of factor XIII were the basis for former Type I deficiency (i.e. factor XIII B subunit deficiency). When we examined an Italian patient with the disease at the DNA level, restriction digestion and sequencing analyses of amplified DNAs revealed that the proband and her family members possessed an AAC insertion within the codon for Tyr-80 in exon III in the gene for the B subunit. a nucleotide polymorphism (A-G) in its 3'-noncoding region in exon XII, and a short tandem repeat polymorphism of (TTTA9, in the 3'-flanking region. These mutations and 3'-polymorphisms were also identified in another Italian family reported in a previous study (10). suggesting that a founder effect is responsible for factor XIII B subunit deficiency in Italians.

DNA Transposable Elements↗
PubMed2002

Factor XIII a-positive dermal dendrocytes and shear wave propagation in human skin.

BACKGROUND: The in vivo interdependence between the phenotypic characteristics of dermal cells and the strain imposed on the tissue has not been studied thoroughly in humans. In particular the mechanical force modulation of Factor XIII a expression in dermal dendrocytes (DD) remains unknown. MATERIALS AND METHODS: The present study compares the numerical density of Factor XIII a-positive DD and the in vivo shear wave velocity in the skin. The investigation was performed in 20 men of normal weight and 20 obese men before and after entering a slimming process. RESULTS: Excess cutaneous fat places the skin under increased intrinsic tension. The resonance running time measurement (RRTM) and the DD density were significantly reduced in overweight individuals. After a short-term but intense slimming process, the same individuals showed a trend to normalization of these two parameters without, however, reaching significance. Pooling all data yielded a significant logarithmic correlation between RRTM values and densities in Factor XIII a-positive DD. CONCLUSION: Factor XIII a expression in human DD may be partially regulated by the intrinsic resting tensions in the skin.

Adult↗
PubMed2006

Evaluation of the pro-angiogenic effect of factor XIII in heterotopic mouse heart allografts and FXIII-deficient mice.

Thrombin-activated Factor XIII (FXIIIa), a plasma transglutaminase, stabilizes fibrin clots by crosslinking fibrin chains. FXIIIa was previously shown by us to exhibit proangiogenic activity associated with downregulation of thrombospondin-1, phosphorylation of vascular endothelial growth factor receptor 2 (VEGFR-2), and upregulation of c-Jun. In the current study, we evaluated the proangiogenic effect of FXIIIa in two murine models: a neonatal heterotopic cardiac allograft model in normal mice, and a Matrigel plug model in FXIII-deficient mice. In the neonatal cardiac allograft model, the number of new vessels as well as graft viability (contractile performance) was significantly higher in FXIIIa-injected animals than in controls. A significant increase in the level of c-Jun mRNA and a significant decrease in the level of TSP-1 mRNA were observed in heart allografts treated with FXIIIa. A marked decrease in TSP-1 protein expression was observed within the endothelial cells of hearts treated with FXIIIa. In the Matrigel plug model, FXIII-deficient mice showed a significantly decreased number of new vessels compared to that of the control mice, and the number of vessels almost reached normal levels following addition of FXIIIa. The results of this study provide substantial in vivo evidence for the proangiogenic activity of FXIIIa.

Angiogenesis Inducing Agents↗
PubMed2006

Contact activation prolongs clot lysis time in human plasma: role of thrombin-activatable fibrinolysis inhibitor and Factor XIII.

BACKGROUND: Contact activation system proteins (e.g., Factor XII, kallikrein) have been implicated as direct or indirect activators of plasminogen. However, contact activation and Factor XI have enhanced thrombin-activatable fibrinolysis inhibitor (TAFI) activation and decreased fibrinolysis, and Factor XIII (FXIII) also delays fibrinolysis via alpha(2)-anti-plasmin deposition on fibrin polymers. Thus, the goals of this study were to define how fibrinolysis is modulated in human plasma by contact or tissue factor (TF) activation, and what role TAFI and FXIII plays in this system. METHODS: Normal, TAFI-deficient and TAFI-deficient/FXIII-supplemented plasma was exposed to tissue-type plasminogen activator and activated with either celite or TF. Clot growth/disintegration kinetics were documented with thrombelastography. RESULTS: Normal plasma activated with celite had significantly prolonged onset and duration of clot lysis compared with samples activated with TF. TAFI-deficient plasma activated with celite was noted to have a duration of clot lysis not different from samples activated with TF, but a significant difference in time to onset of lysis persisted. Celite activation of TAFI-deficient/FXIII-supplemented plasma showed significantly prolonged onset and duration of clot lysis compared with samples activated with TF. CONCLUSIONS: Primarily TAFI, and to a lesser extent FXIII, contributed to contact system protein-mediated attenuation of fibrinolysis. Clinical investigation of these phenomena is warranted in clinical settings involving contact activation (e.g., intra-aortic balloon pumps and ventricular assist devices) to determine whether these devices modulate fibrinolysis and perhaps contribute to thromboembolic morbidity.

Carboxypeptidase B2↗
PubMed2001

Factor XIII replacement in stem cell transplant (SCT) recipients with severe graft-versus-host disease of the bowel: report of an initial experience.

BACKGROUND: Severe acute graft-versus-host disease (aGVHD) of the gut is a serious and frequent posttransplantation event associated with a high mortality rate. We report on our experience with factor XIII replacement in patients with severe aGVHD of the bowel after allogeneic hematopoietic stem cell transplantation. METHODS: Twenty-seven patients after allogeneic stem cell transplantation and severe aGVHD of the gut were enrolled. All patients suffered from bloody diarrhea that required packed red blood cell infusions. All patients received high-dose immunosuppression in combination with coagulation factor XIII (5,000 units initially, followed by 20 IU/kg body weight three times a day) for up to 3 weeks. RESULTS: After 8 days of factor XIII replacement and unchanged high-dose immunosuppression, we observed a significant reduction in the red blood cell requirement of 21 patients. CONCLUSION: We conclude that factor XIII replacement might be a useful supplementation in the treatment of aGVHD of the bowel.

Acute Disease↗
PubMed1977

Congenital deficiency of factor XIII with normal subunit S and lack of subunit A. Report of a new family.

Two sisters born from a nonconsanguineous marriage were found to have congenital factor XIII deficiency. In the electroimmunoassay system, using an anti-subunit S antiserum, two distinct peaks or rockets were seen in normal plasma and serum whereas only one peak was present in the propositae plasma or serum. In the bidimensional immunoelectrophoresis system, using the anti-subunit S antiserum, two major peaks were seen in normal plasma whereas only one peak was seen in the propositae plasma. Using an anti-subunit A antiserum no peak or precipitate was seen in our propositae in the electroimmunoassay or in the bidimensional immunoelectrophoresis systems. Both the parents and the children of our two propositae showed a normal coagulation pattern. Therefore, the heredity appears to be autosomal recessive. These data indicate that the defect is characterized by a normal factor XIII subunit S (support) and a lack of factor XIII subunit A (activity).

Adult↗
PubMed1987

Selective visualization of human dendritic reticulum cells in reactive lymphoid follicles by the immunohistochemical demonstration of the subunit A of factor XIII (F-XIIIa).

Immunohistochemical techniques have been used to localize clotting factor XIII subunit A in human reactive lymphoid follicles. The follicular dendritic reticulum cells (DRCs) were identified by the monoclonal antibodies R4/23 and OKB-7 as well as by their 5'-nucleotidase positivity. Follicular histiocytic reticulum cells (HRCs) were demonstrated by their acid phosphatase and non-specific esterase reactions. Capillaries were selectively visualized by adenosine triphosphatase. The immunohistochemical demonstration of F-XIIIa was preferably carried out in combination with one or two of the above marker techniques, on the same cryostat section. The subunit A of factor XIII is present in follicular DRCs. Their selective immunohistochemical demonstration with antibody against F-XIIIa requires formaldehyde fixation of cryostat sections. Similar fixation, however, is inappropriate for the demonstration of F-XIIIa reactivity of DRCs in paraffin sections. For this purpose, acetic acid-formalin fixation is useful. Follicular HRCs are consistently negative for F-XIIIa, contrary to the F-XIIIa positivity of sinusoidal and interfollicular HRCs. Developmental and functional implications of F-XIIIa reactivity in DRCs and HRCs are suggested.

Antigens↗