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At least 19 recordsLinked to original sources
PubMed1978

Quantitative estimation of coagulation factors in liver disease. The diagnostic and prognostic value of factor XIII, factor V and plasminogen.

20 coagulation parameters were investigated in 144 patients with different liver diseases. The groups of acute hepatitis, chronic active hepatitis and liver cirrhosis were compared and the prognostic value of the coagulation analyses investigated. It is clear that the determination of the factor V activity is a good and easy test for detection of actual liver function. Repeated controls over several weeks revealed with a statistical significance (p less than 0.0005) that all patients with a factor XIII below 35% and a plasminogen below 19% will die in liver coma, if they have not died beforehand from acute gastrointestinal haemorrhage, acute infection or cardiac arrest. Plasminogen is also lower in the group of non-survivors but the values of the two groups are overlapping and of no prognostic help in a single case. The possible causes of the diminution of factor XIII activity are discussed.

Adolescent↗
PubMed1975

Alternative pathways for the activation of factor XIII.

Factor XIII is present in plasma as a proenzyme, which when activated catalyses the formation of epsilon(gamma-glutamyl)lysyl bonds in fibrin. In this study the activation of purified plasma factor XIII was examined quantitatively with the fluorescent amine incorporation assay. Activation products were examined by polyacrylamide gel electrophoresis. The serin proteases, thrombin, trypsin, chymotrypsin, and factor Xa, and also Reptilase were tested for their ability to activate factor XIII. Highly purified thrombins activated purified factor XIII; this reaction was not calcium dependent. Trypsin was also a potent activator, but no transglutaminase activity was found with chymotrypsin. The most highly purified preparations of Reptilase had no effect on factor XIII activity. Less purified Reptilase preparations activated factor XIII, which suggests the presence of another enzyme in these Reptilase preparations. Highly purified factor Xa was found to be an effective activator of purified factor XIII. In contrast to thrombin activation, this reaction required calcium. It may be that under certain circumstances factor XIIIa could be formed in vivo directly by the alternative pathway of factor Xa. Factor XIIIa could then crosslink fibrinogen, which would also provide an alternative pathway for thrombus formation. Also, the activation of factor XIII by both factor Xa and thrombin provides a further point of control in the blood coagulation process.

Batroxobin↗
PubMed1976

[Longtime therapy of congenital factor XIII deficiency using factor XIII concentrate].

Factor XIII was determined by enzymatic and immunochemical methods in 3 patients with congenital factor XIII deficiency. Factor XIII activity measured by trans-glutaminase assay was below 1% of normal value in each of these cases. Immunelectrophoresis determination revealed the absence of the functionally active subunit A, whereas subunit S was only slightly diminished (30 to 50% of the normal value). Substitution with factor XIII concentrate caused a parallel increase of factor XIII activity and subunit A concentration. No uptake of factor XIII activity or of subunit. A by platelets could be demonstrated. Despite discontinuous substitution over a period of six years no antibody against factor XIII activity could be demonstrated in one patient with congenital factor XIII deficiency.

Antibodies↗
PubMed1976

Plasma factor XIII and platelet factor XIII in hyperlipaemia.

Plasma factor XIII activity measured by a quantitative assay was found to be significantly higher in hypertriglyceridaemic patients (type IV and combined hyperlipoproteinaemia), as compared to normolipaemic controls. No such elevation in plasma factor XIII activity was found in patients with type Ha hyperlipaemia. Plasma pseudocholinesterase was found to parallel the elevated factor XIII activity in hypertriglyceridaemic subjects. In contrast, platelet factor XIII activity was not raised in hyperlipaemic subjects, and plasma factor XIII was found to be normal in a normolipaemic subjects with thrombocythaemia. It was concluded that there is no significant contribution from platelets to plasma factor XIII activity, and that the observed increase in plasma factor XIII in hypertriglyceridaemia results from enhanced hepatic synthesis of the enzyme.

Adult↗
PubMed1977

Comparison of the cross-linking patterns of lamprey fibrinogen and fibrin by the action of the intrinsic lamprey factor XIII and human factor XIII during the process of blood coagulation.

Intrinsic lamprey factor XIII cross-links the gamma chain of lamprey fibrin (50,000 daltons) to the gamma-dimer (100,000 daltons). The alpha-chain (110,000 daltons) is cross-linked very slowly to alpha-dimer (210,000 daltons) and alpha-trimer (330,000 daltons). In contrast, human factor XIII, when added in combination with intrinsic lamprey factor XIII, cross-links the alpha-chain of lamprey fibrin to a high molecular weight polymer, and any remaining gamma-chain is also cross-linked to a polymer. However, the gamma-chain that has previously cross-linked to the gamma-dimer by the intrinsic lamprey factor XIII remains as a gamma-dimer. Factor XIII-free lamprey fibrin cross-links all its subunits (alpha, beta, gamma) to high molecular weight polymers when human factor XIII is added. In contrast to human and bovine fibrin where alpha-chain cross-linking in the process of blood coagulation commences when all of the gamma-chain has cross-linked, the lamprey alpha-chain will begin to cross-link when approximately half of the gamma-chain has cross-linked to the gamma-dimer.

Animals↗
PubMed1975

Rheological properties of fibrin clots. Effects of fibrinogen concentration, Factor XIII deficiency, and Factor XIII inhibition.

The effect of fibrinogen concentration, Factor XIII deficiency, and Factor XIII inhibition, utilizing hydroxylamine, on the formation of clot structure in vitro was studied in human platelet-free plasma systems. Rheological and biochemical techniques were employed to relate changes in clot elasticity and viscosity to clot structure formation following recalcification of citrate anticoagulated samples. Classical theories of linear viscoelasticity for swollen crosslinked materials were shown to give an excellent estimate of the number of covalent crosslinks per fibrin monomer, which is directly attainable from rheological data. SDS gel electrophoresis was utilized to show qualitatively that decreases in maximum clot elasticity, at constant fibrinogen concentration, are directly related to a decrease in Factor XIII-mediated intermolecular crosslinking. The use of the technique to investigate both kinetic and equilibrium crosslinking (or structure formation) abnormalities in plasma systems is discussed.

Blood Coagulation↗
PubMed1978

Studies on factor XIII antigen in congenital factor XIII deficiency. A tentative classification of the disease in two groups.

Immunological and immunofluorescent studies carried out on plasma and platelets of three cases of congenital factor XIII deficiency are reported. Two of these patients were originally thought to have normal factor XIII subunit S and no subunit A. However, repeated assays carried out using different lots of antiserum showed that in reality the patients lacked both subunit S and subunit A. The false positive finding was due to the presence of a anti-factor VIII contaminant in the antiserum originally used. The third patient had a normal subunit S and no subunit A. No factor XIII antigen was found by the indirect immunofluorescent technique in normal, factor XIII deficiency and von Willebrand's disease platelets. On the contrary, by using the non-monospecific antiserum a fluorescent pattern similar to that observed by using an anti-factor VIII antiserum, had been noted. On the basis of the data presented in this paper a tentative classification of factor XIII deficiency in two groups is proposed: Type I is characterized by the lack of both factor XIII subunit S and A. Type II is characterized by a normal subunit S and no subunit A. The need for a re-evaluation of published case of factor XIII deficiency by means of monospecific antisera is indicated.

Antigens↗
PubMed1992

A reversed activity staining procedure for detection of an acquired antibody against factor XIII in a girl with factor XIII deficiency.

A new method for detection of inhibitors against factor XIII is described. Agarose gel electrophoresis with normal platelet poor plasma as a factor XIII source included in the gel was combined with reversed activity staining. The procedure was applied to a 10-year-old girl with factor XIII deficiency where substitution therapy had failed. Plasma samples from the patient inhibited the factor XIII catalysed incorporation of the fluorescent monodansylthiacadaverine into casein at a position corresponding to the migration of gamma-globulins. Treatment with Sepharose-bound protein A effectively adsorbed the factor XIII antibody in the patient's plasma.

Antibodies↗
PubMed1991

Intracerebral haemorrhage due to acquired factor XIII inhibitor--successful response to factor XIII concentrate.

A 63-year-old woman presented with extensive bruising. An inhibitor to factor XIII was detected. Subsequent subcutaneous bruising and soft tissue haemorrhage into the left foot were treated with infusions of pasteurized factor XIII concentrate with good effect. Immunosuppression with cyclophosphamide was attempted but in spite of this she suffered a right cerebral haemorrhage necessitating further intensive therapy with factor XIII concentrate. This overcame the inhibitor, adequate post-infusion factor XIII levels were achieved and she made an excellent recovery. Factor XIII concentrate was well tolerated with no evidence of transmission of hepatitis or HIV infection. The inhibitor appeared to interfere with haemostasis by hindering the fibrin binding site of factor XIII, resulting in interference in clot-solubility tests. Subsequently the inhibitor resolved.

Blood Coagulation Tests↗
PubMedDate not supplied

[Factor XIII activity in the presence of suppression of the function of the anticoagulant system and its restoration in animals on an atherogenic ration].

With depressed function of the anticoagulation system in rats produced by their long-term maintenance on an atherogenic ration a rising fibrin-stabilizing activity of the XIII factor, by comparison with that in healthy animals and pertinent controls, is observed. A protracted administration to the animals with depressed function of the anticoagulation system of the compound "Linetol", that contains ethers of unsaturated fatty acids, given together with vitamin "A" results in a drastic fall of the factor XIII activity in the blood plasma with continued maintenance on the atherogenic diet.

Animals↗
PubMed1979

Factor XIII deficiency. A family study by measurement of factor XIII subunits A and S.

A girl with congenital factor XIII deficiency and her large family have been studied by electroimmunoassay of factor XIII subunits A and S. The homozygote has absence of subunit A and a decreased level of subunit S. The heterozygotes have decreased levels of both subunits, and were more readily identified by measurement of subunit A than by the ratio subunit S/subunit A. The mother of the propositus appears to be a new heterozygote, but heterozygosity on the paternal side is traced through three generations.

Adult↗
PubMed1977

Factor XIII (fibrin stabilising factor) in Henoch-Schönlein's purpura.

In 13 out of 17 consecutive children with Henoch-Schönlein's purpura the factor XIII determined with the dansyl cadaverine method was found to be decreased during the acute phase. The decrease is assumed to be due to a specific degradation by proteolytic enzymes liberated from inflammatory cells, with defective local haemostasis as a result. This assumption is strengthened by the observation that treatment with factor XIII combined with an antifibrinolytic drug controlled life-threatening gastro-intestinal bleeding in one of the patients. It would therefore appear that such treatment might offer a new possibility of controlling severe haemorrhages in Henoch-Schönlein's purpura.

Adolescent↗
PubMed1977

[Factor XIII deficiency in adults with acute leukemia: results of a substitution therapy with factor XIII (author's transl)].

A decrease in fibrin stabilizing factor (Factor XIII) is the most frequent coagulation disorder seen in adults with acute leukemia. Patients with prominent reduction of factor XIII (FSF) (less than 50%) were substituted with a factor XIII concentrate from human placenta, and factor XIII plasma concentration and bleeding tendency were followed up during the course of the disease. After substitution plasma, factor XIII activity went up to normal levels in most of the patients. As compared to the course of 12 patients with distinct factor XIII reduction without factor XIII therapy, there were less bleeding complications in 13 courses of patients with prominent reduction of factor XIII substituted with factor XIII concentrate and in 11 with normal or only slightly reduced factor XIII levels.

Acute Disease↗
PubMed1979

Factor XIII.

1. Activated factor XIII is the enzyme that covalently cross-links fibrin monomers into fibrin polymers and results in increased clot strength and resistance of the clot to fibrinolysis. 2. Small amounts (greater than 1% of normal) of factor XIII are necessary for normal in vitro and in vivo activity. 3. Factor XIII deficiency is a rare autosomal recessive illness in which a hemorrhagic diathesis is caused by the virtual absence of the active a subunit of factor XIII. Approximately 100 cases have been described. 4. The disease in homozygotes is characterized by umbilical stump bleeding, a high incidence of fetal wastage, delayed soft tissue hemorrhage, and a high incidence of intracranial bleeding. The heterozygote is asymptomatic. 5. This paper calls attention to the apparent high incidence of oligospermia and small testes seen in homozygote males. Otherwise secondary sex characterics are normal. 6. Because there is no abnormality in thrombin generation and conversion of fibrinogen to fibrin, route coagulation tests (prothrombin time, partial thromboplastin time, thrombin time, etc.) are normal. Platelet function tests are normal. 7. Clots made from recalcified plasma severely deficient in factor XIII are soluble in 5 M urea or 1% monochloroacetic acid. These screening tests are simple and nearly pathognomonic of the illness. 8. More sophisticated and quantitative tests (e.g., dansylcadaverine incorporation) are available for definitive diagnosis and heterozygote detection. 9. Replacement treatment of the illness is simple, effective, and relatively inexpensive. Due to the long half-life of infused factor XIII and the small amounts necessary for normal hemostasis, prophylaxis is feasible and encouraged.

Adult↗
PubMed1992

[Analysis of coagulation factor XIII in Crohn's disease--establishment of a novel monoclonal anti-coagulation factor XIII antibody].

A novel monoclonal anti-human coagulation factor XIII (F. XIII) antibody (2C3 antibody) raised in BALB/c mice was established by Kohler and Milstein methods. The monoclonal antibody recognized F. XIII of 85 KD demonstrated by western blotting analysis. Plasma F. XIII-IR levels measured by ELISA with 2C3 antibody were significantly lower in active disease than in quiescent disease in a total of 21 Crohn's disease (CD) patients. Plasma F. XIII levels were significantly lower on admission in CD with fistulas than in CD without fistulas. Relationships between activities of CD and plasma F. XIII levels were shown. No significant relationships, however, were observed between F. XIII-IR levels and nutritional states assessed by TP, ALB, TF, PA, RBP, %IBW. Low levels of F. XIII in active CD patients with fistulas may occur regardless of hyponutrition. By using 2C3 antibody, global functions of F. XIII will become clarified as well as pathologic and diagnostic roles of plasma F. XIII in CD.

Adolescent↗