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PubMed1982

Decreased antithrombin III level associated with failure of anticoagulation.

A 67-year-old man with adenocarcinoma of the colon had recurrent pulmonary emboli. The patient's level of serum antithrombin III was found to be below normal. Heparin therapy led to further reduction, resulting in failure of adequate anticoagulation. The patient subsequently died of massive pulmonary emboli despite heparin therapy. We believe the antithrombin III level should be routinely determined for patients receiving heparin therapy.

Adenocarcinoma↗
PubMed1987

An abnormal antithrombin III (AT III) with low heparin affinity: AT III Clichy.

We have identified an inherited qualitative deficiency of antithrombin III (AT III) in a family with apparently no increased incidence of venous thrombosis. Plasma antithrombin and anti-Xa activities were normal, but the interaction with heparin, heparan sulphate and low molecular weight heparin was uniformly decreased. An immunoblotting technique performed in plasma showed normal complex formation with thrombin. By using heparin-Sepharose affinity chromatography and crossed immunoelectrophoresis, the variant could be separated: at least two fractions of low affinity AT III were obtained. A minor one had no antiprotease activity; the other one was further purified to homogeneity and found to have normal specific activity in absence of heparin and a 50% decreased activity in presence of heparin. We propose to call this new variant AT III Clichy.

Adult↗
PubMed1987

Antithrombin III Pescara: a defective AT III variant with no alterations of plasma crossed immunoelectrophoresis, but with an abnormal crossed immunoelectrofocusing pattern.

An abnormal AT III variant was found in five members from a family where a high incidence of thromboembolism occurred. In all the affected subjects AT III antigen concentration was normal, whereas antithrombin and antifactor Xa progressive activities as well as heparin cofactor activities were low. Crossed immunoelectrophoresis performed either in absence or in presence of heparin showed a normal plasma pattern. Further chromatographic investigations showed a normal affinity to heparin. An abnormal plasma pattern was evidentiated by crossed immunoelectrofocusing throughout all the AT III pH range. These data are consistent with the presence of an abnormal AT III variant with a defective binding to serine proteases and clearly identifiable only by crossed immunoelectrofocusing. This variant appeared different from the other qualitative AT III defects so far described and was named 'Antithrombin III Pescara'.

Adolescent↗
PubMed1992

Effect of antithrombin concentrate on haemostatic variables in critically ill patients.

In a controlled pilot study of 32 critically ill patients, we have attempted prospectively to identify laboratory variables which can be used to select and monitor patients on antithrombin (AT) therapy. Patients with plasma AT levels less than 70% of normal were randomized to receive (AT group) or not to receive AT concentrate (non-AT group). The groups did not differ in median age, sex, median APACHE II and TISS scores, number of days spent in the Intensive Care Unit or mortality rate. At the time of inclusion all patients had activated coagulation and fibrinolysis demonstrated as high levels of soluble fibrin, thrombin-antithrombin complexes and fibrin-D-dimers (twice, four and ten times the upper reference range, respectively). In the AT group these levels decreased faster and the prothrombin complex concentration increased more rapidly to normal (i.e. the prothrombin time decreased). The level of C-reactive protein which was high in both groups on inclusion (139 and 98 mg/l, respectively) decreased by 40% in the AT group but did not change in the control group. Our study indicates that laboratory variables normalize faster in seriously ill patients who have activated coagulation and fibrinolysis when they receive AT concentrate and that the variables mentioned above seem to be useful for monitoring the treatment.

Aged↗
PubMed1984

Antithrombin III Trento. A 'new' congenital AT III abnormality with a peculiar crossed-immunoelectrophoretic pattern in the absence of heparin.

A family with a new congenital abnormality of antithrombin III (AT III) is presented. 5 members, all females, were affected. The proposita has had several thrombotic manifestations. The other patients, so far, are asymptomatic. Antithrombin activities were all decreased regardless of the method used (chromogenic or clotting) and regardless of the presence or absence of heparin in the assay system. AT III antigen, on the contrary, was normal in all patients regardless of the method used (electroimmunoassay, radial immunodiffusion or Laser nephelometer). The crossed immunoelectrophoresis without heparin showed in plasma the presence of an abnormal peak which was more anodal than the normal counterpart. The same pattern was seen in serum. In the heparin-modified cross-immunoelectrophoresis a normal pattern was seen in plasma and an abnormal one in serum. In the latter the anodal peak was in fact larger than the normal counterpart. Chromatographic studies using Heparin-Sepharose column failed to show changes in heparin affinity, and indicated that both the normal and the abnormal proposed to describe this abnormality. These studies further emphasize the great heterogeneity of AT III defects. This is the first AT III abnormality to show an abnormal crossed-immunoelectrophoresis in the absence of heparin.

Adult↗
PubMed1983

Fatal pulmonary embolism and antithrombin III deficiency in adult lymphoblastic leukaemia during L-asparaginase therapy.

We describe 2 adult patients with acute lymphoblastic leukaemia (ALL) who died from pulmonary embolism following L-asparaginase treatment. Since this drug is known to cause a decrease in antithrombin III, the most important protein physiologically involved in the neutralization of thrombin, we studied the behaviour of this inhibitor in 14 ALL patients treated with a protocol including a 14-day course of L-asparaginase. A significant but transient fall of biological and immunological antithrombin III and a concomitant reduction of fibrinogen were documented.

Acute Disease↗
PubMed1990

A Scottish Hebridean antithrombin III deficient family--twelve years on.

The members of this family with ATIII deficiency have been followed for at least 12 years (1976-1989). All those with previous venous thrombo-embolism have been free from recurrence when on warfarin. During the half century 1931-1981, all 11 full term pregnancies in four affected patients were associated with venous thromboembolism; one patient was enigmatic having one full term pregnancy, without thrombotic event; between 1982 and 1989 three pregnancies have been actively managed with no clinical thrombosis. Management involved use of monitored, self administered, subcutaneous heparin before or very soon after conception and throughout pregnancy (warfarin having been stopped), planned delivery under cover of intravenous antithrombin III, reduction of heparin dosage at delivery and reintroduction of warfarin in the puerperium. The recognised hazards of heparin therapy in pregnancy did not occur. The involvement of the arterial system is reviewed. Clinical evidence provides tentative suggestions on (a) possible additional risk of cigarette smoking (b) avoidance of venography (c) avoidance of varicose vein surgery. A probe is now available for the defective antithrombin III gene in this family, but there has been no occasion yet to apply this in antenatal diagnosis.

Abortion, Spontaneous↗
PubMed2001

Creation of an additional glycosylation site as a mechanism for type I antithrombin deficiency.

We report the identification of a new mutation resulting in type I antithrombin (AT) deficiency and the mechanism by which the deficiency arose. The single base substitution of G to A at nucleotide 2709 was identified in a proband with a family history of venous thrombosis. The mutation results in a substitution of 82 Ser by Asn, creating a new glycosylation site. Expression studies were then carried out, to confirm Asn-linked glycosylation occurred at this consensus site and that this resulted in the AT deficient phenotype. Cell-free translations using rabbit reticulocyte lysate in the presence of microsomes demonstrated that the 82 Asn variant was post-translationally processed efficiently. The 82 Asn variant protein was of a higher molecular weight than normal AT. consistent with the addition of a fifth glycan chain. Incubation of translation product with endoglycosidase H, confirmed that the higher molecular weight product had resulted from additional carbohydrate. Expression of the 82 Asn variant in COS-7 cells resulted in intracellular accumulation, with a low level of secretion of the protein into culture supernatant, consistent with type I AT deficiency. The addition of an extra carbohydrate side chain to residue 82 of antithrombin may block post-translational folding. trapping the variant intracellulary.

Adolescent↗
PubMedDate not supplied

[Plasma antithrombin III activity in patients with pulmonary thromboembolism].

A decreased plasma antithrombin III activity has been noted in 12 out of 20 patients. In 2 patients it was most probably congenital defect, whereas in the remaining 10 patients--acquired. The observed disorders in the activity of antithrombin III with particular reference to anticoagulant therapy have been discussed.

Adult↗
PubMed1987

Antithrombin III in full-term and pre-term newborn infants: three cases of neonatal diagnosis of AT III congenital defect.

Antithrombin III (AT III) plasma levels were investigated in 18 full term neonates and 14 healthy preterm neonates. A control group of 20 healthy adults was also studied. AT III was measured as antigen concentration (Ag) and antithrombin or anti-factor Xa heparin cofactor (H.C.) activities. Crossed immunoelectrophoresis on heparin-agarose (H-CIE) was carried out on plasma samples; moreover the distribution of isoantithrombins was investigated on whole plasma by a technique of crossed immunoelectrofocusing (CIEF). AT III plasma levels in full term infants were significantly lower as compared to the adult values. The preterm newborns group showed a further significant decrease in AT III levels as compared to the full term neonates. In all infants AT III H-CIE runs displayed a single fast moving anodal peak, so that a normal binding to heparin was demonstrated. The CIEF AT III plasma pattern of the adults as well as of all neonates displayed three major peaks at pH range 5.2-4.9, a small amount of AT III at pH 4.9-4.8 and a minor peak at pH 4.8-4.6, so that it was concluded that the isoantithrombins plasma distribution in neonatal age is identical to that of the adult subjects. Four neonates whose mothers were affected by AT III congenital defect were also investigated: diagnosis of congenital deficiency was established in three cases.

Adult↗
PubMed1986

[Therapeutic management of pregnancy complicated by congenital antithrombin III deficiency associated with pregnancy nephropathy].

Thrombo-embolic complications in pregnant women who have congenital antithrombin III deficiency are usually prevented by giving injections of sub-cutaneous heparin from the beginning to the end of pregnancy and with the administration of concentrated doses of antithrombin III (A.T. III) at delivery and in the following days. When we discovered a severe pre-eclampsia at the 28th week of pregnancy in a patient who had congenital deficiency of A.T. III and who had a past history of very severe thrombo-embolic complications we administered concentrated A.T. III as well as continuing the heparin treatment and anti-hypertensive treatment during the pregnancy. Severe fetal distress made us carry out a caesarean operation after 32 weeks of amenorrhoea. Delivery and the post-partum period were conducted without any complications. The newborn baby, who did not have congenital A.T. III deficiency, is very well.

Adult↗
PubMedDate not supplied

[Antithrombin III deficiency as a risk factor in postoperative thrombosis].

Hypercoagulation caused by decreased antithrombin III level leads to thrombosis inspite of postoperative prophylactic heparin therapy. Induced low level of antithrombin III is recognised in particular diseases which lead to a reduced ATIII synthesis, high breakdown or loss. Induced forms should be substituted with ATIII transfusions. Congenital forms should be treated lifelong with coumarin derivates. One should always suspect an ATIII deficiency when in spite of full heparin dosage a prolonged plasma thrombin time is not attained. A case history of recurrent thrombosis may also point to such deficiency.

Antithrombin III↗
PubMed1979

[Progressive antithrombin activity in blood of pregnant women and neonates in the first four days of life (author's transl)].

Progressive antighrombin activity was assayed in 45 term infants in the first four days of life, in 20 cord blood specimens and in the blood of 20 pregnant women (at term). In the term infants a positive correlation was shown between progressive antithrombin and postnatal age. No correlation could be demonstrated with sex, ethnic group or type of delivery. Maternal antithrombin activity was shown to be moderately decreased, maternal values being closely related to cord blood values.

Antithrombin III↗
PubMed1984

Substitution of antithrombin III.

AT III substitution is indicated in patients with inherited antithrombin III deficiency if these patients suffer acute thrombosis, if they have to be treated surgically and in the case of pregnancy in women with AT III deficiency who have an abortion or thrombosis, as well as during and after delivery. In acquired antithrombin III deficiency such as in patients with liver cirrhosis or the nephrotic syndrome, AT III substitution may be necessary if thrombotic complications occur. AT III substitution has been propagated especially in patients with polytrauma, septicaemia, DIC, acute liver failure and in toxaemia. In AT III substitution initial doses of 1 U/kg body weight are used to reach a 1,5% rise in plasma AT III level. If AT III turnover is normal a rise above 80% of normal should be achieved. If AT III turnover is increased, much higher initial and maintenance doses may be needed to normalize plasma AT III levels and to block DIC.

Antithrombin III↗
PubMed1981

[Antithrombin III and its role in normal and pathological hemostasis].

The paper is a survey on the latest up-to-date data on the character, determination methods, physiology, pathophysiology and clinical significance of one of most important factors of anticoagulation system--antithrombin III. Its normal activity is of essential importance for physiological hemostasis. It could be reduced via diminished production, increased elimination and intensified consumption, particularly in case of concomitant grave states and diseases. The enhanced activity of antithrombin III, found most frequently in the treatment with indirect anticoagulants, renal transplantations, and application of anabolic steroids, has given no data of clinical importance so far. Numerous of the outlined problems remain still not sufficiently elucidated.

Antithrombin III↗
PubMed1995

Ectopic transcript analysis in human antithrombin deficiency.

Reverse transcription and amplification of total cellular RNA isolated from peripheral blood mononuclear cells has been used to identify correctly spliced transcripts for human antithrombin. We have explored the potential of this technique for identifying the underlying mutation in five individuals with a Type I deficiency and one individual with a Type II deficiency. In each case correctly spliced transcripts of the correct size were obtained, direct sequencing of which clearly demonstrated the mutation. This method simplifies the detection of mutations in cases of antithrombin deficiency and further extends the use of ectopic transcript analysis.

Antithrombin III↗