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Results for “Factor XIII Deficiency”

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PubMed2002

Effect of fibrin sealant composition on human neutrophil chemotaxis.

The use of fibrin sealants offers one of the most physiologically compatible approaches to preventing postoperative adhesions. Although a number of fibrin sealant formulations have been developed, little is known about how the various components of these preparations affect the wound-healing process. Because one of the key steps in wound healing is the migration of phagocytic leukocytes, such as neutrophils, into the site of injury, we performed studies to characterize systematically the effects of various fibrin sealant components on neutrophil chemotaxis. Using a transwell chemotaxis assay, we found that increasing fibrin concentration resulted in an inhibition of the ability of the cells to migrate through the clots in a dose-dependent manner, and at fibrin clot concentrations >2.0 mg/mL chemotaxis was completely blocked. Factor XIII crosslinking of the clots also had a significant impact on neutrophil chemotaxis, and sealant preparations deficient in Factor XIII allowed neutrophil migration at much higher fibrin concentrations. The presence of various other fibrin sealant components such as plasminogen and fibrinolysis inhibitors (aprotinin and tranexamic acid) did not have any significant effects on the ability of neutrophils to migrate through fibrin clots as compared to control clots without these components. Overall, these studies show that the composition of fibrin sealant preparations can significantly affect neutrophil migration into the site of injury, which could possibly influence the wound healing process.

Chemotaxis, Leukocyte↗
PubMed1989

Immunohistochemical detection of factor XIII subunit a in histiocytes of human uterus.

As spontaneous abortion is a frequent finding in females with Factor XIII (FXIII) deficiency it has been presumed that this clotting factor is essential to normal pregnancy. FXIII subunit a (FXIII A) has been demonstrated in the homogenate of human uterus, but no information on its cellular distribution has been published, so far. In the present study first FXIII A was detected in paraformaldehyde-fixed, paraffin-embedded sections of human uterus by immunoperoxidase technique. Cells containing FXIII A were localized between collagen fibrils stained by Picrosirius Red F3B in the connective tissue. To characterize them the immunofluorescent detection of FXIII A was combined by the visualization of different marker antigens of monocytes and macrophages recognized by Leu-M3, RFD7, anti-HLA-DR and DAKO-anti-macrophage monoclonal antibodies on frozen sections. The coexpression of FXIII A with monocyte and macrophage differentiation marker antigens clearly proves that cells containing FXIII A in the uterus are monocyte-derived tissue macrophages. The results well agree with our previous findings demonstrating FXIII A in human monocytes and different types of macrophages. On the basis of these results, the presence of FXIII A does not seem to be a specificity of the uterus but a characteristic of monocyte/macrophage cell line including tissue macrophages, in general.

Adult↗
PubMed2006

Genetic diagnosis of haemophilia and other inherited bleeding disorders.

Inherited deficiencies of plasma proteins involved in blood coagulation generally lead to lifelong bleeding disorders, whose severity is inversely proportional to the degree of factor deficiency. Haemophilia A and B, inherited as X-linked recessive traits, are the most common hereditary hemorrhagic disorders caused by a deficiency or dysfunction of blood coagulation factor VIII (FVIII) and factor IX (FIX). Together with von Willebrand's disease, a defect of primary haemostasis, these X-linked disorders include 95% to 97% of all the inherited deficiencies of coagulation factors. The remaining defects, generally transmitted as autosomal recessive traits, are rare with prevalence of the presumably homozygous forms in the general population of 1:500,000 for FVII deficiency and 1 in 2 million for prothrombin (FII) and factor XIII (FXIII) deficiency. Molecular characterization, carrier detection and prenatal diagnosis remain the key steps for the prevention of the birth of children affected by coagulation disorders in developing countries, where patients with these deficiencies rarely live beyond childhood and where management is still largely inadequate. These characterizations are possible by direct or indirect genetic analysis of genes involved in these diseases, and the choice of the strategy depends on the effective available budget and facilities to achieve a large benefit. In countries with more advanced molecular facilities and higher budget resources, the most appropriate choice in general is a direct strategy for mutation detection. However, in countries with limited facilities and low budget resources, carrier detection and prenatal diagnosis are usually performed by linkage analysis with genetic markers. This article reviews the genetic diagnosis of haemophilia, genetics and inhibitor development, genetics of von Willebrand's disease and of rare bleeding disorders.

Blood Coagulation Disorders, Inherited↗
PubMed1995

Molecular and cellular basis of deficiency of the b subunit for factor XIII secondary to a Cys430-Phe mutation in the seventh Sushi domain.

We studied the defect responsible for deficiency of the b subunit for factor XIII in the first known case of this condition. The patient is a compound heterozygote of two genetic defects: deletion of A-4161 at the acceptor splice junction of intron A, resulting in a loss of the obligatory AG splicing sequence; and, replacement of G-11499 by T in exon VIII, resulting in an amino acid substitution of Cys430 by Phe. To determine how the latter mutation impaired b subunit synthesis, recombinant b subunit bearing the mutation was expressed in BHK cells. The mutant as well as wild-type b subunit was synthesized by the cells. However, the apparent molecular weight of the mutant was slightly higher than those of the wild-type and plasma b subunits under nonreducing conditions, probably because of destruction of a disulfide bond. The mutant b subunit was secreted from the cells much less effectively than the wild type and remained susceptible to endoglycosidase H, indicating that it was not transported from the endoplasmic reticulum to the Golgi apparatus where the processing of oligosaccharides occurs. Immunofluorescence study suggested that the mutant protein was retained in the endoplasmic reticulum. These studies demonstrate that a Cys430-Phe mutation does not prevent the de novo synthesis of the b subunit, but alters the conformation of the mutant protein sufficiently to impair its intracellular transport, resulting in its deficiency in this patient.

Animals↗
PubMed1996

Factor XIII in chronic inflammatory bowel diseases.

Severe acute inflammation in chronic inflammatory bowel disease is associated with large wound areas and ulcerations that show spontaneous hemorrhage or marked friability. Therefore, an enormous potential of hemostasis and wound healing is required. Coagulation studies demonstrate a deficiency of factor XIII that is important for both clot formation and wound healing. Consequently, the substitution of factor XIII may be beneficial; the first case reports present favorable clinical results. In a prospective pilot study, we treated 12 patients with therapy-resistant ulcerative colitis. The colitis activity index (CAI) and the endoscopic score (ES) according to Rachmilewitz were elevated; all patients suffered from hematochezia. After substitution therapy with factor XIII concentrate (1,250 U/d) the stool frequency dropped and no further hematochezia was detected. The CAI and the ES declined highly significantly. Because of these encouraging results two placebo-controlled multicenter trials have been initiated. In the first study, patients with acute stage of ulcerative colitis associated with severe intestinal blood loss are treated with two different dosages of factor XIII concentrate (1,250 and 500 U/d, respectively) or placebo for 10 days. In the second trial, patients with therapy-resistant ulcerative colitis with a lack of remission in spite of a consequent therapy for 2 weeks are included; factor XIII concentrate or placebo is administered for 10 days. The aim of both trials is an end of intestinal bleeding and the fostering of a more effective wound-healing process.

Adult↗
PubMed1993

Two genetic defects in a patient with complete deficiency of the b-subunit for coagulation factor XIII.

A genomic DNA obtained from a female patient with complete b-subunit deficiency was examined by Southern blotting analysis and in vitro amplification. Nucleotide sequence analysis showed that adenosine-4161 at the acceptor splice junction of intron A/exon II was deleted in half of the amplified DNAs, resulting in a loss of the obligatory AG splicing sequence. The absence of adenosine-4161 was confirmed by cleavage with TaqI endonuclease of the amplified DNAs. Moreover, sequence analysis showed that guanosine-11499 coding for Cys 430 (TGC) in exon VIII was replaced by thymidine in half of the amplified DNAs, resulting in an amino acid change to Phe (TTC) and the destruction of a disulfide bond in the seventh Sushi domain. This mutation was also confirmed by cleavage with MboII endonuclease. Thus, the proband turned out to be a compound heterozygote of two separate defective alleles. Although half of the amplified DNAs for exon VIII of her daughter or son were cleaved by MboII, those for intron A were not cleaved by TaqI. The replacement of guanosine-11499 by thymidine in their exon VIII has also been confirmed by sequence analysis, indicating that they are heterozygous for one normal and one defective allele.

Alleles↗