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PubMed1988

Factor XIII: enzymatic and clinical aspects.

The present knowledge about clotting F XIII is roughly displayed. It is explained why F XIII is not a clotting factor in the strict sense of the word and that its biological function more general is the crosslinking of proteins via a transamidase reaction, the reduction of the permeability of the microvasculature, the stimulation of connective tissue cells, and finally the steering of connective tissue processes involved in wound healing. These effects are demonstrated as well in cell culture studies, animal experiments as by clinical results. Concerning the clinical results with F XIII, its effects on sclerodermia, subarachnoidal hemorrhage, inflammatory bowel diseases, Purpura Schönlein Henoch, and the wound healing are described in more detail.

Animals↗
PubMed2004

[Molecular biology of haemostasis: fibrinogen, factor XIII].

Genetic defects of fibrinogen are caused by a broad spectrum of mutations in one of the three structural genes FGA, FGB and FGG. They result in complete or partial lack of plasma fibrinogen (a- or hypofibrinogenaemia) or in structural abnormalities affecting protein function (dysfibrinogenaemia). In contrast to afibrinogenaemia mainly caused by nonsense, frameshift, and splice site mutations resulting in substantially truncated polypeptide chains (mainly Aalpha), in hypo- and dysfibrinogenaemias missense mutations lead to the exchange of single amino acids as dominating underlying defect. In the cases with quantitative disorders, bleeding with various degrees of severity is generally observed. Dysfibrinogenaemia is associated with both bleeding or thrombosis or even a combination of haemorrhagic and thromboembolic symptoms. About one half of the dysfibrinogenaemic cases is clinically asymptomatic. The plasmatic factor XIII (FXIII) is a heterotetramer composed of two A and two B subunits encoded by two different genes. FXIII deficiency is associated with bleeding, wound dehiscence and recurrent spontaneous abortions. The most frequent form is caused by defects in the A subunit with a broad spectrum of underlying mutations. Defects of the B subunit are very rare and were molecularly elucidated in only a few cases.

Amino Acid Substitution↗
PubMed2006

Fibrinogen plasma levels modify the association between the factor XIII Val34Leu variant and risk of coronary artery disease: the EPIC-Norfolk prospective population study.

BACKGROUND: The factor (F) XIII Val34Leu variant has been implicated in coronary artery disease (CAD). In vitro evidence suggests an interaction between this variant and fibrinogen concentrations in determining thrombus structure. OBJECTIVES: To test whether this interaction is relevant in influencing coronary risk in apparently healthy individuals. METHODS: In an 8-year prospective population study of 25 663 men and women, we compared 898 apparently healthy men and women developing incident CAD with 1580 matched controls. RESULTS: Overall, the FXIII Val34Leu variant was not associated with the risk of future CAD. However, a significant interaction existed between the Val34Leu variant and fibrinogen levels for the risk of future CAD (P = 0.004). Among people in the lowest tertile of fibrinogen concentrations, LeuLeu carriers had an odds ratio (OR) of 2.88 (95% confidence interval; CI 1.24-6.74) compared to wild-type individuals (P for linearity = 0.003). By contrast, among those in the highest fibrinogen tertile, LeuLeu carriers were had a lower risk than wild-type individuals (OR 0.47, 95% CI 0.18-1.17, P for linearity = 0.1). CONCLUSIONS: Our results suggest that a significant gene-covariate interaction exists between the FXIII Val34Leu variant and fibrinogen levels. Relationships between genotype and disease risk may be altered by biological covariates. Simplistic paradigms of gene or biomarker associations are unlikely to fully characterize disease risk in populations.

Adult↗
PubMed1986

Biosynthesis of factor XIII B subunit by human hepatoma cell lines.

The plasma transglutaminase, factor XIIIa (FXIIIa), circulates as a zymogen containing two proteins, A and B, arranged in a noncovalent tetrameric complex, A2B2. Biosynthesis of plasma FXIII has not previously been demonstrated. In the present study, direct evidence has been obtained that two human hepatoma cell lines, Hep G2 and PLC/PRF/5, synthesize and secrete FXIII B protein. Secretion of the B subunit of FXIII by Hep G2 was demonstrated by immunoblotting. De novo synthesis by Hep G2 was confirmed in 35S-methionine-labeled cultures. Radiolabeled conditioned medium was concentrated, mixed (1:1) with purified B protein, and examined by crossed immunoelectrophoresis with antiserum to the B subunit. The single protein precipitin arc of purified B protein comigrated with the radiolabeled FXIII from Hep G2 visualized by autoradiography, indicating both electrophoretic and antigenic identity. The data presented here represent the first demonstrations of biosynthesis of FXIII B protein by any cell type and suggest that the liver is the site of synthesis of FXIII B protein. Further analysis of concentrated Hep G2 serum-free conditioned medium (SFCM) and cell lysate by immunoblotting following nondenaturing agarose gel electrophoresis demonstrated the FXIII A protein as well as the B protein and also revealed synthesis and secretion of the A and B proteins by PLC/PRF/5. Crossed immunoelectrophoresis studies of Hep G2 SFCM and cell lysate suggest that Hep G2 cells also synthesize and secrete the plasma FXIII zymogen. With a specific radioimmunoassay for B protein, FXIII was found in Hep G2 SFCM at approximately 4 ng/mL; with an amplified rocket immunoelectrophoresis technique the level was approximately 5 ng/mL.

Carcinoma, Hepatocellular↗
PubMed1993

[Congenital deficiency of fibrin stabilizing factor [factor XIII)].

The authors report a new case of congenital deficiency of fibrin stabilizing factor. The defect is transmitted as an autosomal recessive trait. The earliest symptom is umbilical bleeding when the cord separates. The diagnosis is confirmed by the rapid dispersion of the clot in urea 5 M or monochloroacetic acid.

Factor XIII Deficiency↗