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Results for “Factor XIII Deficiency”

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At least 487 records · Page 27Linked to original sources
PubMed1980

[Behavior of the fibrin-stabilizing blood coagulation factor XIII in hemorrhages after tooth extractions].

The influence of the fibrin-stabilizing coagulation factor XIII is necessary for the formation of a stable blood clot. The factor is not included in the usual global coagulation tests. The presence of lowered concentrations of this factor can be congenital or acquired as a result of various diseases. A lowered concentration of factor XIII was demonstrated in six patients with otherwise normal coagulation tests during a secondary hemorrhage a few days after an extraction. The hemorrhage was attributed to the lowered resistance of the instable blood clot over against the fibrinolytic characteristics of the buccal cavity milieu.

Factor XIII↗
PubMedDate not supplied

[Chronic continuous bleeding in a girl with lack of F. XIII (author's transl)].

A case with chronic continuous bleeding on an eleven year old girl with lack of F. XIII with positive family antecedents and without declarate consanguinity is presented. Analytic data are widely clear as well as parent's research which shows the heterocygosity but with doubts exposed.

Blood Coagulation Tests↗
PubMed1981

Subunit A of factor XIII regulates subunit B plasma concentration.

Subunit a of Factor XIII is found absent in homozygotes and reduced in heterozygotes. Since a concomitant reduction of subunit b occurs in these cases, an interaction between the loci controlling the synthesis of the two subunits was suggested. However in the present study we have shown that the administration of subunit a in two totally devoid homozygotes produced an increase of subunit b, reaching the maximum concentration five days after infusion. This strongly suggests that subunit b plasma level is regulated on the subunit a plasma amount.

Biological Availability↗
PubMed1980

[The prognostic value of factor XIII in Schönlein-Henoch purpura in childhood (author's transl)].

In a prospective study of 19 cases of Schönlein-Henoch purpura, the factor XIII level was compared with 32 normal controls. The study demonstrates that factor XIII levels are of value both in making the diagnosis of Schönlein-Henoch purpura and predicting the outcome. If the factor XIII level is greater than 80% the diagnosis of Schönlein-Henoch purpura is unlikely and if factor XIII level is less than 60% of normal, the risk of complications is high.

Child↗
PubMed1980

[Lessening the impairment of wound healing by pre-or postoperative quantitative factor-XIII substitution (author's transl)].

In the light of listed references, a report is given on the influence of the clotting factor XIII in experiments with animals as well as with patients. Through own examinations in 95 patients with severe abdominal and vessel surgery, a clear lessening of impairment of wound healing could be achieved by the quantitative pre- and postoperative substitution of the fibrin stabilizing factor.

Abdomen↗
PubMed1999

Autoimmune antibody in a hemorrhagic patient interacts with thrombin-activated factor XIII in a unique manner.

Without a prior history of hemorrhagic disease, a 62-year-old man suffered recurrent episodes of bleeding. Solubility of the patient's clot in 5 mol/L urea indicated a problem with fibrin stabilization. The transamidase activity potential of factor XIII, measured by the incorporation of radioactive putrescine into N,N-dimethylcasein as test substrate, was 62% of control, close to the normal range of values. Examination of the patient's clot from recalcified plasma by sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed that essentially none of the alpha chains and only about two thirds of the gamma chains of fibrin became cross-linked under conditions where both were fully cross-linked in the controls. An antibody to factor XIII was isolated which, although recognizing the recombinant rA2 subunits, as well as the virgin A2B2 plasma ensemble, showed a 100-fold greater affinity for the thrombin-activated rA2' and A2'B2 forms of the zymogen, suggesting that the latter would be its main target during coagulation. Furthermore, the patient's IgG has an ability, never seen before, for inducing an enzymatically active configuration in the thrombin-activated zymogen in the absence of Ca2+.

Antigen-Antibody Reactions↗
PubMed1999

Factor XIII modulates intestinal epithelial wound healing in vitro.

BACKGROUND: An acquired deficiency of blood coagulation factor XIII has been proposed to cause an impairment of intestinal wound healing and hemostasis in patients with inflammatory bowel diseases. Substitution of factor XIII seems to result in a rapid improvement of intestinal wound healing. Our aim was therefore to characterize the role of factor XIII in the modulation of intestinal wound healing in vitro. METHODS: Factor XIII was added to subconfluent cultures of two non-transformed small-intestinal epithelial cell lines (IEC-6, IEC-18) and three human colon cancer-derived epithelial cell lines (T84, CaCo-2, HT-29) with subsequent assessment of cell proliferation with a colorimetric 3-(4,5-dimethylthiazole-2-yl)-2,5-diphenylformazan (MTT) assay. The effects on epithelial cell migration in vitro were assessed with an in vitro wounding model of confluent IEC-6 cell monolayers. RESULTS: Factor XIII caused a modest inhibition of proliferation of IEC-6 and IEC-18 cells. However, factor XIII significantly stimulated proliferation of T84, CaCo-2. and HT-29 cell lines. In addition, thrombin-activated factor Xill promoted intestinal epithelial cell restitution in vitro on average 2.5-fold. The modulatory effects of factor XIII could not be significantly blocked by anti-transforming growth factor beta (TGFbeta). CONCLUSIONS: Factor XIII may promote intestinal epithelial wound healing by enhancement of epithelial cell restitution through a TGFbeta-independent pathway. This may explain previously described beneficial effects of factor XIII in the treatment of active ulcerative colitis.

Animals↗
PubMed1992

Rare inherited bleeding disorders secondary to coagulation factors in Jordan: a nine-year study.

This work reports on rare inherited coagulation factors defects which were seen in a developing country over a 9-year period. There were a total of 30 cases which fulfilled this diagnosis. Fibrinogen abnormalities were the most frequently encountered. There were 10 patients with afibrinogenemia, 2 with hypofibrinogenemia and 1 case with dysfibrinogenemia. Factor XI deficiency was found in 7 patients, factor V and VII deficiencies accounted for 3 cases each. Factor X and XIII deficiencies were found in 2 patients each. All these rare deficiencies accounted for 10% of all inherited bleeding disorders in the population studied over 9 years.

Blood Coagulation Disorders↗
PubMed1997

Structural analysis of a missense mutation (Val414Phe) in the catalytic core domain of the factor XIII(A) subunit.

Molecular analysis has been performed on a Malaysian patient with a severe bleeding disorder due to factor XIII(A) subunit deficiency. Total mRNA was isolated from the patient's leucocytes and four overlapping segments corresponding to the entire coding region of the A subunit cDNA were amplified by RT-PCR. The cDNA segments amplified efficiently and were of expected size. Direct sequencing of the complete reading frame revealed a single homozygous base change (nt 1327G-T) in exon 10 corresponding to a missense mutation, Val414Phe, in the catalytic core domain of the A subunit monomer. The mutation eliminates a BsaJ1 restriction site and family screening showed that both parents were heterozygous for the defect. The base substitution was absent in 55 normal individuals. Val414 is a highly conserved residue in the calcium-dependent transglutaminase enzyme family. Computer modelling based on 3D crystallographic data predicts that the bulky aromatic side chain of the substituted phenylalanine residue distorts protein folding and destabilizes the molecule. In addition, conformation changes in the adjacent catalytic and calcium binding regions of the A subunit are likely to impair the enzymatic activity of any protein synthesized.

Adult↗
PubMed1985

Acceleration of fibrinolysis by the N-terminal peptide of alpha 2-plasmin inhibitor.

When blood plasma containing the NH2-terminal 12-residue peptide (N-peptide) of alpha 2-plasmin inhibitor (alpha 2PI; alpha 2-antiplasmin) was clotted in the presence of calcium ions, the N-peptide and alpha 2PI were cross-linked to fibrin by activated coagulation factor XIII. The amount of N-peptide cross-linked to fibrin was proportional to the concentration of N-peptide present in plasma. On the other hand, the amount of alpha 2PI cross-linked to fibrin was decreased by the presence of N-peptide, and the decrease was in reverse relationship to the increase of cross-linking of N-peptide. Spontaneous fibrinolysis or fibrinolysis induced by tissue plasminogen activator was accelerated by the presence of N-peptide, and the acceleration was dependent on the concentrations of N-peptide and directly proportional to inhibition of alpha 2PI cross-linking exerted by N-peptide. The acceleration was more pronounced when the clot was compacted by platelet-mediated clot retraction or by a squeeze. Fibrinolysis of an alpha 2PI-deficient or a factor XIII-deficient plasma clot was not accelerated by N-peptide. These findings were substantiated in a purified system and support the previous proposal that alpha 2PI is cross-linked to fibrin at the glutamine residue that is next to the NH2-terminus of alpha 2PI, and this factor XIII-mediated cross-linking of alpha 2PI is significant in inhibition of physiologically occurring endogenous fibrinolysis.

Fibrin↗
PubMedDate not supplied

[Structure, function and the role of factor XIII in human pathology].

Modern views on the functioning of coagulation system are constantly replenished with the facts obtained using the newest methods of molecular biology and medicine. The purpose of many components of this system is non-uniform and covers the whole spectrum of biochemical reactions responsible for homeostasis. Current data on one of such components--the factor XIII (fibrin stabilizing factor) are stated. Except for the description of the enzyme structure and functions, information is presented about the methods of its detection, which development has resulted in accumulation of knowledge on the role of fibrin stabilizing factor in bleedings and thrombosis genesis. Data are given on hereditary and acquired deficiency of the factor XIII, as well as on conditions accompanied with the increase of its activity.

Blood Coagulation↗
PubMed1998

A novel insertion mutation (1286insC) in exon 9 of the factor XIII-A subunit gene.

Molecular studies have been performed on a Greek family with factor XIII-A subunit deficiency. The 15 exons of the A subunit gene were amplified by polymerase chain reaction and analysed by direct nucleotide sequencing. A homozygous single base insertion (1286insC) in exon 9 of the gene was identified in three affected family members. The insertion results in a frameshift and a premature stop signal a short distance downstream at codon 403. Any A subunit protein expressed is likely to be unstable and lack part of the catalytic core domain together with both beta barrel domains towards the C-terminal of the molecule. This study contributes to our knowledge of the mutational spectrum in patients with factor XIII-A deficiency.

DNA Transposable Elements↗