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At least 865 records · Page 48Linked to original sources

PubMed1983

L-asparaginase induced antithrombin III deficiency: evidence against the production of a hypercoagulable state.

L-asparaginase, a chemotherapeutic agent employed in the treatment of acute lymphocytic leukemia (ALL), is known to depress the synthesis of numerous plasma proteins. The plasma concentration of the major protease inhibitor of the coagulation mechanism, antithrombin III, is substantially decreased in patients receiving this drug. This observation has generated speculation that L-asparaginase may induce a hypercoagulable state in humans. To examine this hypothesis, we studied ten patients with ALL in remission who were being treated with the above chemotherapeutic agent. Our data revealed that infusion of this enzyme leads to a marked decrease in the plasma concentrations of prothrombin as well as antithrombin III. However, we have also observed a constant level of thrombin generation during the same period of time as monitored by plasma levels of prothrombin activation fragment (F1 + 2) and thrombin-antithrombin complex (TAT). Based upon these findings we suggest that administration of L-asparaginase does not usually lead to the induction of a hypercoagulable state.

Adolescent↗

PubMed1986

Pentosan polysulphate: activation of heparin cofactor II or antithrombin III according to molecular weight fractionation.

The relative potency of pentosan polysulphate in activation of heparin cofactor II/thrombin interaction has been compared to heparin and dermatan sulphate and found to be within the same order. A skewed distribution of molecular weight forms was observed upon gel filtration of pentosan polysulphate with an average molecular weight of 4500 daltons. Two peaks of activity were observed in activation of heparin cofactor II. The greatest activity was observed in high molecular weight fractions (5-fold greater than that of average molecular weight) and a concentration-dependent profile indicated a template mechanism of action. A lower peak of activity was observed at average molecular weight and the effect of increasing concentrations of this material on activity indicated a mechanism involving binding to proteinase inhibitor or proteinase alone. Potentiation of antithrombin III/thrombin interaction was observed only in fractions greater than the average molecular weight. Concentration-dependent profiles indicated binding to antithrombin III and thrombin was a requisite of activation. A fraction of low molecular weight showed no property of activation of antithrombin III or heparin cofactor II/thrombin interaction. Three fractions of high, average and low molecular weights tested in clotting assays showed relative potencies corresponding to those observed in the purified systems.

Antithrombin III↗

PubMed2004

Antithrombin: in control of coagulation.

Antithrombin is a serine proteinase inhibitor (serpin) which controls the process of coagulation. It has a well defined structure, consisting of three beta-sheets, nine alpha-helices and a reactive centre loop (RCL). The RCL contains the reactive centre which harbours a bait sequence for target proteases; cleavage results in inhibition by a unique mechanism. The inhibitory activity of antithrombin is controlled by its interaction with the co-factor, heparin, which accelerates its interaction with target proteases. This ensures that heparin and its newer derivatives, such as heparin pentasaccharide, are the mainstay therapeutics for control of thrombosis or inappropriate clotting. The clinical importance of antithrombin is manifested by its clear association with thrombosis when deficiency states occur.

Animals↗

PubMed2003

Inherited thrombotic tendency in a pedigree with antithrombin La Rochelle (N405K) and factor V Leiden.

An Irish pedigree with a strong thrombotic tendency, due to the novel association of antithrombin La Rochelle (N405K) and factor V Leiden is described. Thromboses occurred at a median age of 16 years in four family members, carrying both mutant alleles. Molecular diagnosis was facilitated by the creation of an additional restriction enzyme site (Mnl1) in exon 6 of the antithrombin gene. Both the genes for antithrombin and factor V are located at chromosome 1q23. The molecular data and phenotypic behaviour in this family are strongly suggestive of allelic co-segregation of the mutant alleles.

Adolescent↗

PubMedDate not supplied

[Treatment of disseminated intravascular coagulation with antithrombin III concentrate in children with verified infection].

Consumption coagulopathy in childhood is still a serious problem. Besides treatment of the underlying diseases therapy of consumption coagulopathy was performed with heparin and nowadays with substitution of coagulation factors, especially antithrombin III concentrate, alone or in combination with heparin. We performed administration of AT III concentrates only, without additional heparin treatment in children with proven septicaemia (preterm infants n = 21, children beyond the newborn period n = 18). Antithrombin III, platelet count, fibrinogen, PT, aPTT and TT were assayed. These coagulation parameters turned to be normal 48 hours after normalisation of the antithrombin III plasma level-AT III increased to normal values within 24 hours after the initial substitution in all children. Lethal outcome was not observed after sole administration of AT III as well as no other side effects have been seen. In summary, these data indicate that consumption coagulopathy in childhood can be managed successfully with early substitution of AT III concentrate.

Adolescent↗

PubMed1981

Hereditary antithrombin III deficiency in an English family.

A family including four members with decreased antithrombin III (ATIII) measured by a biological and an immunological method is described. Immunologically measured levels of other coagulation inhibitors were normal. In the antithrombin III deficient family members there was a history of thrombotic disease. Turnover of 125I-antithrombin III in a deficient individual showed the lower plasma levels probably to be due to a deficiency in the rate of synthesis rather than to an increased catabolic rate.

Adult↗

PubMed1984

Prophylactic antithrombotic therapy with stanozolol in patients with familial antithrombin III deficiency.

Three patients with familial antithrombin III deficiency underwent a trial of prophylactic antithrombotic therapy with stanozolol. An increase in plasma fibrinolytic activity and antithrombin III was seen. Acute venous thrombosis occurred in two patients; in the first patient thrombosis was precipitated by venography but in the second no precipitating factor was found. Our experience suggests that stanozolol is not a suitable prophylactic agent in patients with familial antithrombin III deficiency.

Antithrombin III↗

PubMed1985

Effect of danazol on the biochemical abnormality of inherited antithrombin III deficiency.

Seven members of a family affected by hereditary antithrombin III deficiency were identified. The disorder was associated with recurrent spontaneous episodes of phlebitis, deep venous thrombosis, and pulmonary embolism in middle age. Danazol, a 17-alkyl derivative of ethinyl testosterone, which has been used to treat other antiprotease deficiency states, was assessed in the management of two men with antithrombin deficiency. In a dose of 600 mg a day danazol appeared to correct the antithrombin deficiency. This drug may provide a useful adjunct to anticoagulant treatment, particularly before surgery.

Adult↗

PubMed1995

Developing guidelines for biotechnology drug use: experience with antithrombin III.

Development of institutional guidelines for use of high-cost biotechnology drugs, such as antithrombin III, is a valuable tool in formulary management. This article describes the process by which the University of California Davis Medical Center used an ad hoc committee to the P & T Committee to develop guidelines for antithrombin III use. Performing an objective analysis of available literature to address the appropriate role of a biotechnology agent is necessary to develop consensus guidelines. Approval of use guidelines by the P & T Committee provides the necessary structure for optimal use of biotechnology agents, such as antithrombin III.

Antithrombin III↗

PubMed1990

[Antithrombin III in the Senegalese diabetic].

The chronometric method was applied to 141 diabetics and 151 reference subjects from both sexes aged between 19 and 60 years, all of Black race and Senegalese nationality, to study the effects of Antithrombin III (AT III). A significant reduction in the physiological activity of antithrombin III (AT III) was observed for ages 36-45 and 56-60 and correlated with obesity and other complications. With our patients, insulin dependence does not seem provoke any reduction in antithrombin III's effectiveness.

Adult↗

PubMed1988

Antithrombin III, protein C, and protein S. Naturally occurring anticoagulant proteins.

Protein C, protein S, and antithrombin III are naturally occurring anticoagulant proteins. Activated protein C and protein S act by inhibiting the action of the cofactors factor Va and factor VIIIa. Antithrombin III inhibits the serine proteases (factors II, IX, X, XI, and XII); its anticoagulant action is dramatically enhanced by heparin. Deficiencies of these proteins are associated with thromboembolic disease. Antigen and activity assays practical for the clinical laboratory are available for protein C and antithrombin III. Protein S antigen assays are also available. Diagnosis of an anticoagulant protein deficiency has serious implications for a patient and his kindred, and should therefore only be made on the basis of repeated abnormal determinations of a single protein in an individual patient, or documentation of the same protein deficiency in other family members.

Antithrombin III↗

PubMed1987

Molecular genetic survey of 16 kindreds with hereditary antithrombin III deficiency.

Molecular genetic techniques were utilized to examine antithrombin III (ATIII) gene status in 16 independently ascertained kindreds with hereditary ATIII deficiency. In one of these families antithrombin III deficiency is caused by hemizygosity of the ATIII locus. In the remaining 15 kindreds, two copies of the ATIII gene are present and appear to be grossly normal at the level of whole genome Southern blotting, suggesting that small deletions, insertions or limited nucleotide substitution(s) in the antithrombin III gene, or "trans-acting" defects at other loci involved in the processing, modification, and secretion of biologically active ATIII are responsible for the observed anticoagulant disorders.

Antithrombin III↗

PubMed1987

Extensive thrombus formation with heparin resistance during extracorporeal circulation. A new presentation of familial antithrombin III deficiency.

Extensive thrombus formation during extracorporeal circulation despite the administration of heparin sodium prompted investigation of a 15-year-old boy with a calcified right ventricular thrombus and a history of subacute bacterial endocarditis. In vitro studies confirmed the failure of heparin in standard doses to have an anticoagulant effect. Antithrombin III concentrations were low. The patient's mother, who had no history of thromboembolic disease, was also antithrombin III deficient. Resistance to heparin is a theoretical, but inconsistently documented, feature of antithrombin III deficiency. This deficiency state should be considered whenever heparin resistance is encountered, even in the absence of a personal and family history of thromboses.

Adolescent↗

PubMed1984

[Substitution of antithrombin III by synthetic thrombin inhibitors].

Synthetic, low-molecular weight thrombin inhibitors may substitute for antithrombin III in inactivating thrombin in vitro and in vivo. They are superior to heparin as antithrombotic agents in antithrombin deficiency or consumption. Studies in experimental animals show the effectiveness of synthetic thrombin inhibitors in immunologic antithrombin depletion, thrombin-induced consumption and CCl4-induced liver failure.

Animals↗

PubMed1981

Comparison of progressive antithrombin activity and the concentration of three thrombin inhibitors in nephrotic syndrome.

In order to compare the plasmatic progressive antithrombin activity to the concentration of three thrombin inhibitors, antithrombin III (AT III), alpha 2 macroglobulin (alpha 2 M), alpha 1 anti-trypsin (alpha 1, AT) in nephrotic syndrome, a prospective study was carried out on a group of 28 children affected with the disease. A dramatic reduction of the level of AT III and of alpha 1 AT, two inhibitors of molecular weight close to that of albumin, was observed. The decreased level of AT III was counterbalanced by an increase in alpha 2 M. This phenomenon accounts for the increased progressive antithrombin activity observed in all the affected children. It is suggested that the above compensatory mechanism explains the absence of thrombotic accidents in this series and that the benefit of heparin therapy is doubtful in these conditions.

Adolescent↗

PubMed1981

Acute aortic thrombosis in antithrombin III deficiency.

Two cases of acute aortic thrombosis, a previously unreported complication of antithrombin III deficiency, are reported. Both patients had abnormally low antithrombin III levels, which improved to normal levels with warfarin ;sodium therapy. The possibility of antithrombin III deficiency should be considered in young patients with acute arterial thrombosis.

Acute Disease↗

PubMed1980

Inherited antithrombin III deficiency and cerebral thrombosis in a child.

Identification of a family affected by antithrombin III-heparin cofactor (AT-III) deficiency was made after diagnosis of the index case, a 15-year-old boy who suffered cerebral thrombosis. The proband had a two-year history of recurrent thrombosis involving the lower extremities. His mother and sister were also affected. Studies showed a decreased biological activity (AT-IIIc) and antigen (AT-IIIag) by the Laurell technique in the proband (AT-IIIc = 0.32, AT-IIIag = 46%), his sister (AT-IIIc = 0.29, AT-IIIag = 47%), and his mother (AT-IIIc = 0.41, AT-IIIag = 56%). Crossed immunoelectrophoresis (CIE) of the affected individuals' plasma in agarose-containing heparin demonstrated a normal pattern of migration. Treatment with warfarin sodium (Coumadin) resulted in an increase in activity in two of three affected family members, and in antigen in all three. Anticoagulant therapy did not affect the pattern of AT-III on CIE. This family represents a quantitative deficiency in antithrombin III. A review of the reported cases of antithrombin III deficiency indicates that individuals with this disorder may have thromboembolic disease in childhood.

Adolescent↗

PubMed1980

A South African family with antithrombin III deficiency.

Antithrombin III is the most important natural inhibitor of coagulation. Reduced levels of antithrombin III are a well-documented cause of hypercoagulability. Several families have been described with hereditary antithrombin III deficiency, including one from South Africa. We report a second South African family with this defect.

Antithrombin III↗