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PubMed2003

The G-to-T point mutation in codon 34 of the factor XIII gene and the risk of pre-eclampsia.

A G-to-T point mutation in exon 2 of the FXIII A-subunit gene results in a leucine rather than valine at amino acid position 34 of the factor XIII molecule. The presence of leucine has been associated with a reduced risk of both arterial and venous thrombosis. We examined the prevalence of this point mutation in 102 cases of pre-eclampsia and 208 matched control subjects, as inherited and acquired risk factors for arterial and venous thrombosis are associated with an increased risk of pre-eclampsia. The GT genotype was observed in 38% of controls and 29.4% of cases and the TT genotype was observed in 6.7% of controls and 5.9% of cases. In subjects heterozygous for the T genotype (GT) the relative risk of pre-eclampsia was 0.7 [95% confidence interval (CI95 ) 0.4-1.1] when compared with the GG genotype. For subjects homozygous for the T allele the relative risk for pre-eclampsia was 0.8 (CI95 0.3-2.1) when compared with the GG genotype. The risk associated with the T allele in the heterozygous and homozygous forms compared with the GG genotype was 0.7 (CI95 0.4-1.1). We conclude that the presence of leucine at this site is not associated with a protection against pre-eclampsia to the magnitude of that reported in other thrombotic disease.

Adult↗
PubMed1989

Localization of the coagulation factor XIII B subunit gene (F13B) to chromosome bands 1q31-32.1 and restriction fragment length polymorphism at the locus.

In situ hybridization of tritiated cDNA probes for the gene for the B subunit of coagulation factor XIII localized the F13B locus to bands q31-q32.1 on human chromosome 1 and perhaps more precisely to sub-bands 1q31.2 or 1q31.3. Restriction fragment length polymorphisms (RFLPs) were detected with BglII, EcoRI and XbaI. Because the RFLPs detected with each of the three enzymes were concordant in every individual studied and since each showed a similar size difference, it was concluded that the RFLPs probably result from an insertion or deletion of length approximately 0.37-0.4 kb.

Blotting, Southern↗
PubMed1989

Glanzmann's thrombasthenia associated with a transient deficiency of factor XIII.

A three-year-old girl suffering from ecchymoses developed severe epistaxis. The diagnosis of thrombasthenia was made on the basis of platelet aggregation studies, flow cytometric analysis with monoclonal antibodies and gel electrophoretic analysis. In addition, coagulation studies at the time of epistaxis repeatedly showed a transient deficiency of factor XIII activity and antigen.

Blood Platelet Disorders↗
PubMed1986

Identification of histiocytic reticulum cells by the immunohistochemical demonstration of factor XIII (F-XIIIa) in human lymph nodes.

Morphologically and enzyme histochemically distinguishable tissue macrophages and stromal cells of human reactive lymph nodes were characterized by the cytoplasmic presence of the subunit A of factor XIII and by the expression of surface antigenic determinants reacting with monoclonal antibodies directed against monocyte/macrophage populations (Mo 1, Leu M3) and HLA-DR antigens. The distribution of F-XIIIa positive cells was studied on formaldehyde-fixed paraffin-embedded sections with immunoperoxidase techniques. established on cryostat section with double immunofluorescence. Alpha-Naphthyl acetate esterase (ANAE) reaction was The immunophenotype was established on cryostat sections with double immunofluorescence. Alpha-Naphthyl acetate esterase (ANAE) reaction was carried out on these cryostat sections to identify tissue macrophages. The antibody against F-XIIIa detected histiocytes in both intra- and extra-sinusoidal locations which were ANAE+, Mo 1+, Leu M3+ and HLA-DR-. F-XIIIa was also present in fibroblast-like mesenchymal cells with the following phenotypic characteristics: ANAE-, Mo 1+, Leu M3+ and HLA-DR+. The anti F-XIIIa antibody did not stain lymphoid cells, granulocytes, epithelial cells, endothelial cells and mast cells. The immunohistochemical detection of F-XIIIa works on formaldehyde-fixed paraffin-embedded sections. The most promising application seems to be the identification of histiocytes in lymphoid and histiocytic proliferations.

Antigens, Surface↗
PubMed1997

Degradation of human factor XIII by lonomin V, a purified fraction of Lonomia achelous caterpillar venom.

Lonomia achelous caterpillar venom (LACV) causes a severe bleeding diathesis in humans. A constant finding in these cases is a profound depression of blood clotting Factor XIII (FXIII) activity. The molecular mechanisms by which LONOMIN V (a chromatographically purified fraction from LACV) alters the FXIII complex is the subject of the present study. Incubation of human purified FXIII with Lonomin V shows that both the zymogen and the activated forms of FXIII were proteolytically degraded, with the generation of peptidic fragments of low molecular weight. Both the A and B subunits of FXIII were degraded in a progressive, dose dependent manner. The B subunit was more resistant to the action of Lonomin V, requiring higher concentrations in order to achieve complete degradation. On the basis of these findings we postulate that the proteolysis of FXIII in vivo is one of the pathophysiological factors behind this bleeding syndrome.

Animals↗
PubMed1989

The B subunit of coagulation factor XIII is linked to renin and the Duffy blood group to alpha-spectrin on human chromosome 1.

Family linkage studies were used to detect two linkage relationships on human chromosome 1. The B subunit of coagulation factor XIII showed significant linkage to renin with a maximum lod score of 5.071 at a distance of 10 cM. Significant linkage was also shown between the Duffy blood group and alpha-spectrin with linkage results giving a combined lod score of 3.194 at 5 cM.

Blood Group Antigens↗
PubMed1986

Genetic polymorphism of coagulation factor XIII B subunit in the Japanese population: description of three new rare alleles.

Polyacrylamide gel isoelectric focusing (PAGIEF) of neuraminidase-treated EDTA plasma samples followed by electroblotting with enzyme immunoassay was performed to further investigate coagulation factor XIII B subunit (FXIII B) polymorphism. In 435 Japanese subjects PAGIEF patterns of FXIII B were classified into five common and three rare allotypes. This suggested that the FXIII B*2 allele existed in the Japanese population in the same manner as in Caucasians. Three new rare allotypes were considered to be controlled by three rare alleles which were designated FXIII B*13, FXIII B*14, and FXIII B*15, respectively. The gene frequencies calculated from 435 Japanese subjects were FXIII B*1 = 0.2977, FXIII B*2 = 0.0184, FXIII B*3 = 0.6805, FXIII B*13 = 0.0011, FXIII B*14 = 0.0011, and FXIII B*15 = 0.0011, respectively.

Alleles↗
PubMed1976

[Tissue adhesion and local haemostasis using fibrinogen, thrombin and clotting factor xiii. (experimental investigations--clinical experience) (author's transl)].

A report is given on experimental investigations and clinical experience in the use of a biological adhesive system. This system consists of highly-concentrated native fibrinogen, thrombin and clotting factor XIII. Experimental tissue adhesion was successfully performed in numerous experiments and with various organs. Local haemostasis was obtained even in cases when other methods failed by sealing off bleeding surfaces with a fibrin layer. The satisfactory results obtained in these experimental investigations were confirmed by the excellent outcome of a clinical trial. Fibrin represents a biological system which is completely absorbable, contrary to the commonly-used synthetic adhesives. Further advantages are its highly adhesive properties, elasticity of consistency and good tissue compatibility.

Animals↗
PubMed2004

Factor XIII Val34Leu polymorphism does not contribute to the prevention of thrombotic complications in patients with antiphospholipid syndrome.

The effect of thrombophilic mutations in the development of thrombosis in patients with antiphospholipid syndrome (APS) has been extensively investigated. Factor XIII (FXIII) Val34Leu polymorphism is a newly described polymorphism which is located in the three amino acids away from the thrombin activation site of the FXIII-A subunit. It has been reported that the Leu allele decreases the risk of both arterial and venous thrombosis. In the present study, we examined the association between the FXIII Val34Leu polymorphism and the development of thrombosis in patients with APS. Sixty APS patients with arterial and venous thrombosis, 22 antiphospholipid antibody (aPLA) positive patients with first trimester abortus and/or thrombocytopenia, 126 healthy controls, and 60 healthy subjects who were age- and sex-matched with thrombotic APS group were included into the study. FXIII Leu allele frequencies in the APS patients with thrombosis, aPLA-positive patients without thrombosis, healthy controls, and matched controls were 13.3, 16, 19.5, and 18.3%, respectively. When we compared Leu allele frequencies between APS patients with thrombosis and aPLA-positive patients without thrombosis, healthy controls or matched controls, we could not find any difference (chi2, p = 0.43, and P = 0.09, P = 0.67, respectively). Our results showed that the FXIII Leu allele has no protective effect in the development of thrombosis in APS.

Adolescent↗