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Results for “Antithrombin III Deficiency”

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PubMed1995

Modulation of hemostatic balance with antithrombin III replacement therapy in a case of liver cirrhosis associated with recurrent venous thrombosis.

Patients with liver failure can present both thrombotic and hemorrhagic complications because of the deficiency in coagulation factors and inhibitors (protein C and S, antithrombin III) and impairment of fibrinolytic balance. Here we report the case of a 63-year-old man with liver cirrhosis, recurrent thrombosis, and features of low-grade consumption coagulopathy, showing severe antithrombin III deficiency (about 30% of normal values). Treatment with antithrombin III (2000 U/day) and low doses of heparin (5000 U b.i.d.) was successful in modulating the coagulation system toward an antithrombotic effect. After discharge from hospital the ambulatory treatment with antithrombin III concentrates (2000 U twice a week) allowed the attainment of antithrombin III activity of about 60% and prevented the patient from recurrence of venous thrombosis.

Antithrombin III↗
PubMed1981

Antithrombin deficiency--a cause of unexplained thrombosis in vascular surgery.

Antithrombin deficiencies may be the reason for seemingly unexplained thrombosis and graft failure. We treated seven patients who developed clotting difficulties as a result of antithrombin II and/or III deficiencies. In four, arterial thrombosis occurred after arterial reconstruction--three with occluded femoral grafts and one with runoff and digital vessel thrombosis that developed during profundoplasty. Two patients has spontaneous thrombosis of the arterial system of the vessels of the lower leg, and one developed ileofemoral phlebitis. Three patients had abnormally low levels of both antithrombin II and III, whereas two had low levels of antithrombin II only and two had low levels of antithrombin III. Of the four patients in whom this disorder occurred during vascular reconstruction, three experienced graft occlusion that resulted in below-knee amputation in two. There were no common predisposing factors. Antithrombin deficiency should be suspected when there is an unusual propensity to develop thrombus, when heparin cannot prolong coagulation time, and when measurements show reduced levels of antithrombin. Fresh frozen plasma should be given initially and long-term Coumadin therapy started. Early recognition and treatment is necessary to avoid limb loss or death.

Adult↗
PubMed1997

Potentially prothrombotic abnormalities of coagulation in benign intracranial hypertension.

OBJECTIVE: Benign intracranial hypertension (BIH) may be caused by intracranial venous sinus thrombosis. Cerebral angiograms may, however, be normal in patients with BIH that are associated with conditions with an increased risk of venous thrombosis. This raises the possibility that unrecognised non-occlusive venous thrombus might impede CSF drainage. This study therefore examined the strength of the association between risk factors for thrombosis and BIH. METHODS: The incidence of prothrombotic abnormalities among a mixed prospectively and retrospectively investigated cohort of 38 patients with BIH, was compared with healthy obese subjects, and patients with other neurological diseases. Prothrombotic abnormalities investigated included anticardiolipin antibodies, lupus anticoagulant, antithrombin III, proteins C and S, plasma fibrinogen, kaolin cephalin clotting time, prothrombin time, and full blood counts. RESULTS: Evidence for the presence of an antiphospholipid antibody was found in 32% of cases. Cases of familial deficiency of antithrombin III, thrombocytosis, and polycythaemia were also noted. Additionally, an increased concentration of plasma fibrinogen was found in 26%. A coagulation abnormality was more often detectable in those subjects with normal or low body mass index and in those tested within six months of onset. CONCLUSION: There is a thrombotic pathogenesis in some cases of BIH.

Adolescent↗
PubMed1987

The role of heparin cofactor II in the modulation of hemostasis.

Human plasma contains two distinct heparin dependent thrombin inhibitors; antithrombin III (ATIII) and Heparin cofactor II (HCII). The latter is also known as antithrombin BM, because of its moderate binding affinity to heparin. The protein is distinct from ATIII by immunological and functional criteria as well as by its amino acid sequence. HCII selectively inhibits thrombin by forming a 1:1 molar complex with the protease and has no activity towards other coagulation serine proteases. Dermatan sulphate, a glycosaminoglycan, specifically activates HCII and increases its thrombin neutralizing activity by over a thousand fold. Dermatan sulphate does not catalyze the activity of ATIII. Human fibroblasts have been shown to accelerate the neutralization of thrombin by HCII. These cells can synthesize proteoglycans containing dermatan sulphate. Current evidence would thus suggest that extravascular tissues are the major sites of action of HCII. The specificity of dermatan sulphate for HCII has allowed the development of functional assays for this protein. Reduced levels have been observed in patients with significant hepatocellular dysfunction and in association with disseminated intravascular coagulation. Two families have been reported with hereditary HCII deficiency and recurrent thrombosis (both venous and arterial). Although these observations suggest a role for HCII in the modulation of hemostatic system, further studies are required to define the importance of HCII deficiency as a marker of thrombosis.

Antithrombin III↗
PubMed1985

A pasteurized antithrombin III concentrate for clinical use.

A method for large-scale production of a pasteurized antithrombin III (AT III) concentrate for therapeutic use has been adapted from published methods. It includes the following steps: (1) batchwise adsorption onto heparin-Sepharose from plasma depleted of cryoprecipitate and prothrombin complex; (2) chromatographic elution at high salt concentration; (3) pasteurization for 10 h at 60 degrees C in the presence of added citrate ion; (4) desalting on Sephadex G-25, and (5) sterile filtration and freeze-drying. Seven batches prepared in this manner gave a mean yield of 269 U AT III/kg plasma. The product passed all the usual animal safety and pyrogenicity tests and has been used successfully in several courses of treatment of congenital deficiencies.

Adsorption↗
PubMed1990

Laboratory identification of conditions predisposing to thrombosis.

The 5-year experience with a panel of laboratory tests designed to identify patients with high risk of thromboembolism was reviewed. This panel included an activated partial thromboplastin time and reptilase time as well as specific assays for antithrombin III, protein C, protein S, and plasminogen. One hundred and nine patients were evaluated by this panel. Conditions predisposing to thrombosis were identified in 24 of these patients and these conditions included: dysfibrinogenemia, lupus anticoagulant, and deficiencies of antithrombin III, protein C and protein S. The limitations of this panel are also discussed.

Adolescent↗
PubMed1996

The plasma turnover of transfused antithrombin concentrate in patients with acquired antithrombin deficiency.

Antithrombin concentrate, prepared from human plasma, has been used as replacement therapy in 35 patients with acquired antithrombin deficiency. The inhibitory activity of the concentrate, measured by chromogenic assay, correlates well with the manufacturer's quoted activity. The mean in vivo recovery of the product was 0.0124 iu mL-1 per iu of antithrombin (AT) concentrate administered by kilogram body weight. The recovery was similar in all diagnostic groups studied and did not vary during the course of treatment. Consumption of the antithrombin concentrate was monitored by measuring the production of thrombin-antithrombin complexes and the loss of plasma antithrombin activity. The mean concentration of thrombin-antithrombin complexes was elevated (23 ng mL-1) at the time of admission to the intensive care unit and fell progressively over the next 4 days. The mean time for the decay of half the antithrombin activity was 23 h during the first 24 h of therapy and rose to 42.1 h after day 1. The recovery and half-life measurements are necessary to plan an appropriate dosage regimen for the administration of this antithrombin concentrate in acquired deficiency states.

Antithrombin III↗
PubMed1997

Antithrombin and its inherited deficiency states.

Antithrombin is the primary inhibitor of thrombin that also inhibits many of the other activated serine proteinases involved in blood coagulation. A hypercoagulable state occurs when a deficiency of antithrombin exists in plasma; the deficiency may be either inherited or acquired. This failure to regulate adequately the activity of coagulation proteinases can, with additional provocation, result in clot formation and in the clinical presentation of thromboembolic disease. The structure and function of antithrombin, nature and heterogeneity of the molecular defects in the antithrombin gene associated with inherited antithrombin deficiency, prevalence and the natural history of inherited antithrombin deficiency are all reviewed here.

Antithrombin III↗
PubMed1999

[New screening method for coagulation abnormality including AT III deficiency during CABG].

In our institute, 1 ml of heparin is administered to the patients undergoing CABG before dissection and mobilization of the internal thoracic arteries (ITAs) and/or right gastroepiploic artery (GEA) to prevent possible thrombosis or coagulation tendency. Two patients with AT III deficiency underwent CABG and one of them died. The aim of this study is to know whether ACT check before and after administration of 1 ml of heparin is useful as a screening test of coagulation abnormalities including AT III deficiency. One hundred patients (84 males and 16 females) undergoing CABG were studied. Age ranged from 41 to 79 years (mean 64.8 +/- 8.0 years). One ml of heparin was administered to all the patients before ITAs and/or GEA were dissected and mobilized. ACT was doubly checked before (control ACT: c-ACT) and after (heparinized ACT: h-ACT) administration of heparin. ACT extension was defined as follows: ACT extension = (c-ACT)-(h-ACT). Mean c-ACT was 124 +/- 12 sec., h-ACT 188 +/- 26 sec. and ACT extension 64 +/- 24 sec. There were only 3 cases which ACT extension were less than 30 sec.: two of them were combined with AT III deficiency and the other was due to insufficient administration of heparin. In conclusion, examination of ACT after 1 ml administration of heparin is new, simple and convenient screening method for coagulation abnormalities including AT III deficiency during CABG.

Adult↗
PubMed1986

[Congenital abnormalities related to coagulation and the fibrinolytic system in patients with vein thrombosis of the lower extremities].

Plasma concentrations of antithrombin III (AT III), plasminogen (Plg), and protein C (PC) were assayed in 28 patients with venous thrombosis of lower extremities without distinct underlying disorders. Three abnormalities were found in 5 cases (17.8%) in relation to coagulation and fibrinolytic system (3 with congenital AT III deficiency, one each with dysplasminogenemia and congenital PC deficiency). In the patients with either one of these abnormalities, characteristic features of thrombosis are summarized as follows; 1. early onset of clinical symptoms. 2. high frequency of superficial vein thrombosis. 3. high recurrence rate. 4. high frequency of pulmonary embolism.

Adolescent↗
PubMed1988

The frequency of type I heterozygous protein S and protein C deficiency in 141 unrelated young patients with venous thrombosis.

The frequency of heterozygous protein C and protein S deficiency, detected by measuring total plasma antigen, in a group (n = 141) of young unrelated patients (less than 45 years old) with venous thrombotic disease was studied and compared to that of antithrombin III, fibrinogen, and plasminogen deficiencies. Among 91 patients not receiving oral anticoagulants, six had low protein S antigen levels and one had a low protein C antigen level. Among 50 patients receiving oral anticoagulant therapy, abnormally low ratios of protein S or C to other vitamin K-dependent factors were presented by one patient for protein S and five for protein C. Thus, heterozygous Type I protein S deficiency appeared in seven of 141 patients (5%) and heterozygous Type I protein C deficiency in six of 141 patients (4%). Eleven of thirteen deficient patients had recurrent venous thrombosis. In this group of 141 patients, 1% had an identifiable fibrinogen abnormality, 2% a plasminogen abnormality, and 3% an antithrombin III deficiency. Thus, among the known plasma protein deficiencies associated with venous thrombosis, protein S and protein C deficiencies (9%) emerge as the leading identifiable associated abnormalities.

Adult↗