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Biomedical subjects

I Pabinger

Publications and source records attributed to I Pabinger.

At least 73 records · Page 4Linked to original sources
PubMed1996

FLAG (fludarabine, cytosine arabinoside, G-CSF) for refractory and relapsed acute myeloid leukemia.

Twenty-two patients with refractory or relapsed AML were treated with FLAG [25 mg/m2 fludarabine daily (days 1-5), 2 g/m2 daily Ara-C (days 1-5) and 400 micrograms/m2 daily G-CSF (day -1 till the absolute neutrophil count was > 500/microliter)]. Median age was 46 years (range 24-63). Eight patients had leukemia which was primarily refractory to conventional regimens, six were in first, seven were in second, and one was in third relapse. Overall, 11 of 22 (50%) patients achieved complete remission (CR), three had a partial response (PR), and seven did not respond (NR). One patient died of an early cerebral hemorrhage. The median remission duration from achievement of CR after FLAG was 9.9 months and median survival was 13.0 months. One patient is alive in CR at 31.9 months. Hematological toxicity of the regimen was severe. The median time to neutrophil recovery (ANC > 500/microliter) was 21 days (range 18-33). A median of seven red cell units (range 0-22) and of six platelet concentrate units (range 3-28) had to be given. Median duration of febrile neutropenia was 2 days (range 0-20 days) and patients were on i.v. antibiotics for a median of 16 days (range 0-51). There was no death from infection. Nonhematological toxicity was remarkably low, with almost no neurotoxicity and no major hepatotoxicity. In conclusion, FLAG seems to be an efficient and well tolerated regimen. It may be particularly useful for patients who have a sibling or unrelated donor for subsequent allogeneic bone marrow transplantation.

Acute Disease↗
PubMed1996

Oral contraceptives enhance the risk of clinical manifestation of venous thrombosis at a young age in females homozygous for factor V Leiden.

In 29 patients (17 females) homozygous Arg 506 Gln mutation (FV Leiden) was identified. 25 had been investigated because of venous thromboembolism (VTE); four asymptomatic patients were found during family studies. The first VTE had occurred significantly earlier in females (median age [m] 26 years, range 17-49) than in males (m=38 years, range 21-82) (P=0.01). 12 females (80%) had taken oral contraceptives (OC, estrogen content 0.02-0.1 mg) for 6-150 months prior to thrombosis. Further triggering conditions in females were hormone replacement (n=1) and pregnancy (n=2). In 8/10 males the first VTE had occurred spontaneously--in two after surgery. The sites of VTE were deep vein thrombosis, pulmonary embolism, caval vein thrombosis and superficial thrombophlebitis. From our data we conclude that OC medication is the most important precipitating factor for VTE in females with homozygous FV Leiden.

Adolescent↗
PubMed1996

Resistance to activated protein C (APC): mutation at Arg506 of coagulation factor V and vascular access thrombosis in haemodialysis patients.

BACKGROUND: Vascular access thrombosis represents a serious problem in haemodialysis patients. Therefore identification of relevant thrombotic risk factors is clinically valuable. Resistance to activated protein C (APC) was recently identified as a new thrombophilic defect which is caused by a single point mutation in the factor V gene. Whether this mutation predisposes to vascular access thrombosis is unknown. METHODS: The presence of factor V Leiden (mutation at nucleotide position 1691 of the factor V gene) was determined by polymerase chain reaction (PCR) analysis in 152 haemodialysis patients from all three haemodialysis units of the University Hospital of Vienna. In 61 patients (54 without mutation, 7 with heterozygous mutation) resistance to APC was evaluated. One hundred-seven individuals without renal failure (57 negative for factor V Leiden, 50 heterozygous subjects) served as controls. Haemodialysis patients with heterozygous factor V Leiden mutation were carefully investigated for thrombotic complications of vascular access, other thromboembolic events and additional putative thromboembolic risk factors. RESULTS: Seven of 152 (4.6%) patients were heterozygous carriers of factor V Leiden. The mean APC resistance ration in heterozygous dialysis patients was 2.31; in the 50 heterozygous controls the ratio was 2.02. The mean APC ratio in haemodialysis patients without mutation was 3.53 in contrast to 2.95 in the control group. Not one of the seven heterozygous haemodialysis patients suffered from vascular access thrombosis of inexplicable origin. Three patients remained totally free of access thrombosis from onset of haemodialysis treatment. In four of seven patients nine events of thrombosis of the vascular access occurred, but were due to anatomical stenosis in each case. In six permanent central venous catheters no episode of occlusion or reduced blood flow requiring thrombolytic therapy was observed. Family history with regard to thrombotic events was negative in all seven patients. No thromboembolic complication occurred during 13 periods of immobilization, in the course of six pregnancies and during oral contraception. CONCLUSIONS: The heterozygous carrier status for factor V Leiden does not appear to represent a risk factor for vascular access thrombosis in haemodialysis patients. This is possibly due to the fact that the functional APC activity is high and in heterozygous haemodialysis patients APC resistance ratios are very close to the normal range. However, it cannot be excluded that a homozygous factor V mutation represents an increased risk for shunt thrombosis. Therefore patients suffering from repeated and/or inexplicable shunt thrombosis should be tested for the factor V mutation to evaluate the effect of a homozygous mutation.

Adult↗
PubMed1996

Thrombotic risk in hereditary antithrombin III, protein C, or protein S deficiency. A cooperative, retrospective study. Gesellschaft fur Thrombose- und Hamostaseforschung (GTH) Study Group on Natural Inhibitors.

A cooperative, retrospective study was performed on data from 8 coagulation laboratories and thrombosis units in Austria, Germany, and Switzerland to assess the risk for thrombosis in patients with hereditary antithrombin III (AT-III), protein C (PC), and protein S (PS) deficiencies; to compare the clinical manifestations of these 3 deficiency states; and to estimate the risk for development of thrombosis in high-risk situations. Two hundred thirty patients from 71 families with a documented hereditary deficiency of a natural coagulation inhibitor were included in the study. The patient group comprised 69 patients from 25 families with AT-III deficiency, 86 patients from 27 families with PC deficiency, and 75 patients from 19 families with PS deficiency. Diagnosis of the deficiency state was made at each participating center. Clinical data were documented in a questionnaire that was completed during each patient's visit to the participating center. The questionnaires were sent to the coordinating center (Vienna) and analyzed centrally. The probability of developing thrombosis was 80% to 90% for all deficiency states by 50 to 60 years of age, and this figure did not change considerably after data from the propositi were excluded. AT-III-deficient females developed thrombosis earlier in life compared with PC- and PS-deficient females due to a high thrombotic risk during pregnancy (40% in patients with AT-III deficiency) and oral contraceptive use. The clinical features of thromboembolism were similar in the three deficiency states except for a higher frequency of superficial thrombophlebitis in patients with PC and PS deficiencies. Mesenteric vein thromboses occurred in 4% to 10% of patients and in 2 of 8 patients as a recurrent event. The recurrence rate was 63% (60% of recurrent events occurred spontaneously) and did not differ significantly among the three deficiency states. Before 14 years of age only 1 of 80 surgical procedures and 0 of 21 leg injuries were followed by thrombosis. After 14 years of age thromboembolic events occurred after abdominal surgery or leg injury in one third of patients. Between 40% and 50% of symptomatic patients reported that they felt handicapped by a postthrombotic syndrome. We conclude that diagnosis of a coagulation inhibitor deficiency state should be made before 14 years of age. During childhood thrombosis prophylaxis cannot be regularly recommended but should be instituted after 13 years of age during/after abdominal surgery, including appendectomy, and after leg injury in AT-III-, PC-, and PS-deficient patients. The high recurrence rate (60% spontaneous recurrence) and the relatively high frequency of mesenteric vein thrombosis as a recurrent event favor introduction of long-term oral anticoagulant treatment after the first thrombotic event in patients with a documented hereditary deficiency of AT-III, PC, or PS.

Adolescent↗
PubMed1996

Lupus anticoagulant and thromboembolism: evaluation of fibrinogen, natural inhibitors and molecular markers of thrombosis.

It has been speculated that an impairment in anticoagulant pathways (protein C (PC), protein S (PS), resistance to activated protein C (APC)), may contribute to the thrombotic tendency in lupus anticoagulant (LA) patients. Increased plasma levels of fibrinogen are predictive for arterial thrombosis and increased molecular markers of thrombosis are indicative for activation of the clotting cascade. We investigated 25 patients (20 women) with LA. All patients were stratified according to their thromboembolic history and women according to their history of fetal loss. Eighteen patients had a history of venous or arterial thrombosis, or both. Seven of 16 women with at least one pregnancy had a history of fetal loss. The interrelation among the levels of fibrinogen, PC and PS, and resistance to APC, thrombin-antithrombin III complexes (TAT), prothrombin fragment F1 + 2, D-dimer and the history of thrombotic events and obstetric complications in patients with LA were evaluated. LA patients with a history of venous or arterial thrombosis had a significantly higher fibrinogen level than LA patients without (mean 366 versus 304 mg/dl; P = 0.018). Among 16 women a slightly lower mean TAT level in women with fetal loss was found (2.4 versus 4.3 ng/ml; P = 0.02). No other statistically significant difference in the remaining parameters was yielded in both analyzed subgroups. The results of the study suggest an association between increased fibrinogen levels and the history of venous or arterial thrombosis, or both, in patients with LA. In the other investigated parameters, no relationship to the thrombotic or obstetric history was found.

Adult↗
PubMed1996

Probability of recurrence of thrombosis in patients with and without factor V Leiden.

Activated protein C (APC) resistance is a common risk factor for venous thromboembolism and is associated with the replacement of Arg 506 by Gln in the factor V gene (factor V Leiden). We investigated the risk of recurrence of venous thromboembolism in APC resistant patients heterozygous for FV Leiden and compared these patient groups with a group of patients, who had a history of venous thromboembolism, but had neither APC resistance nor the FV Leiden mutation. APC resistance was determined in frozen blood samples from patients with a history of venous thromboembolism, who were not receiving oral anticoagulant (OAC) treatment. The plasma samples were collected between 1984 and 1991. Twenty-one patients in whom APC resistance was found in the stored plasma samples were reinvestigated in 1994 (5 males, 16 females, median [m] age 49 years, range 21-71 years). Twenty-one sex and age matched patients with venous thromboembolism (5 males, 16 females, age m = 50 years, range 25-73 years) investigated during the same time period who had a normal APC resistance test served as a control group. Patients with APC resistance as well as controls were reinvestigated for the presence of FV Leiden by genetic analysis in 1994. Of the 21 APC resistant patients, 5 were homozygous and 16 heterozygous for FV Leiden. Before the study entry homozygous patients had a significantly higher recurrence rate (5/5 patients) compared to the control group in heterozygous patients (9/16) and controls (9/21) the recurrence rate was not significantly different. The total observation time was 21 years in patients with homozygous FV Leiden, 83 years in patients with heterozygous FV Leiden and 108 years in controls, excluding the time when patients were on OAC treatment. During the observation time the recurrence rate was highest in patients with homozygous FV Leiden (9.5% per patient per year), but was similar in patients with heterozygous FV Leiden (4.8% per patient per year) and controls (5% per patient per year). Two of five (40%) homozygous patients, 4/16 (25%) heterozygous and 5/21 (24%) controls had a least one recurrent event during the observation period. The probability for development of thrombosis in the Kaplan-Meyer-Plot analysis was not different between the three groups. Bearing limitations of our study in mind (retrospective design, relatively small patient number) we conclude that the risk of recurrence after a thromboembolic event is not higher in patients with heterozygous FV Leiden than in patients without this mutation. Thus, it appears that the identification of heterozygous FV Leiden mutation is not an indication for long-term OAC treatment. Also, long-term OAC treatment cannot generally be recommended for homozygous patients with a single thromboembolic event. More definitive conclusions will require larger prospective studies.

Adult↗
PubMed1996

Factor V enhances the cofactor function of protein S in the APC-mediated inactivation of factor VIII: influence of the factor VR506Q mutation.

Factor V and protein S are cofactors of activated protein C (APC) which accelerate APC-mediated factor VIII inactivation. The effects of factor V and protein S were quantitated in a reaction system in which plasma factor VIII was inactivated by APC and the loss of factor VIII activity was monitored in a factor X-activating system in which a chromogenic substrate was used to probe factor Xa formation. Factor V increased the rate of APC-mediated factor VIII inactivation in a dose-dependent manner in representative plasma samples with protein S or factor V deficiency, abnormal factor V (heterozygous or homozygous for factor VR506Q), or a combination of heterozygous protein S deficiency and heterozygous factor VR506Q. This effect was much less pronounced in the plasma samples with a decreased protein S level, but the impaired response in these plasmas was corrected by addition of protein S, indicating that both factor V and protein S are required for optimal inactivation of factor VIII by APC. The effects of factor V and protein S were also studied in a reaction system with purified proteins. APC-catalysed factor VIII inactivation was enhanced 3.7-fold in the presence of 1.1 nM factor V and 1.5-fold in the presence of 2.4 nM protein S. When both 1.1 nM factor V and 2.4 nM protein were present the rate enhancement was 11-fold. Factor V is a more potent cofactor than protein S, as can be concluded from the fact that 0.04 nM factor V gave the same stimulation as 2.4 nM protein S. Protein S lost its cofactor function after complexation with C4b binding protein, which indicates that it is free protein S that acts as a cofactor. To investigate the effect of the R506Q mutation in factor V on APC-mediated factor VIII inactivation, factor V was purified from the plasma of patients homozygous for factor VR506Q. In the absence of protein S, factor VR506Q did not enhance factor VIII inactivation by APC, but in the presence of 2.4 nM protein S a slight enhancement was observed. The APC cofactor activity of factor V was lost when factor V was activated with thrombin or with the factor V activator from Russell's viper venom. These data indicate that optimal inactivation of factor VIII by APC requires the presence of an intact factor V molecule and free protein S.

Arginine↗
PubMed1996

Two new frequent dimorphisms in the protein S (PROS1) gene.

Two new polymorphisms were identified in the protein S gene (PROS1): an intronic T/A-dimorphism (PIPS1) in intron K, and an exonic C/A-dimorphism (PEPS2), located in the 3'untranslated trailer of exon 15. Allelic frequencies of 24% (PIPS1-A) and 17% (PEPS2-A) respectively, were determined in the normal population. The identification of an intronic and an exonic PROS1 dimorphism, in addition to the known BstXI dimorphism, enlarges the molecular tool box for gene analysis and transcript quantification in hereditary protein S deficiency. Haplotype analysis showed that variability of both new polymorphisms occurred almost exclusively in the A-allele of the known intragenic BstXI dimorphism. Therefore, PEPS2 and PIPS1 are especially valuable in individuals homozygous for the BstXI A-variant.

Alleles↗
PubMed1996

Thrombotic tendency in 75 symptomatic, unrelated patients with APC resistance.

Resistance to activated protein C (APC resistance) was measured in 284 individuals (169 females, 115 males) with a history of objectively confirmed venous thrombosis and/or pulmonary embolism. A decreased APC resistance ratio was found in 75 patients (26%), 47 were females, 28 males. Factor V Leiden was investigated in 60 of 75 patients with APC resistance, of whom 46 were heterozygous, 4 homozygous. In 10 APC resistant patients the Arg 506 Glu mutation was not identified. The median age of the first thromboembolic event in patients with APC resistance was 42 years (range 15-82 years). Most patients had a history of deep vein thrombosis (83%), 28% had experienced pulmonary embolism. More unusual sites of thrombosis were the deep arm veins (7%) and mesenteric veins (one patient, 1.3%). 53% of patients developed the first thromboembolic event spontaneously. Precipitating conditions for thromboembolism were surgery in 9.3% and trauma in 8%. In one third of female patients the first thromboembolic event occurred in conjunction with pregnancy and delivery (14.8%) or oral contraceptives (19%). At the time of investigation 40% of patients with APC resistance had experienced recurrent thromboembolic events. The family history was positive in 60% of patients. We conclude that the clinical feature of APC resistance is similar to the feature of a deficiency of antithrombin, protein C and protein S. Pregnancy, delivery and oral contraceptives seem to be a relevant additional risk factors for thrombosis in females with APC resistance.

Adolescent↗
PubMed1995

Protein S deficiency type I: identification of point mutations in 9 of 10 families.

We identified potentially causative mutations in the active protein S gene (PROS 1) by direct sequencing of PROS 1-specific polymerase chain reaction (PRC) products of all 15 exons, including exon-intron boundaries in 10 families with hereditary protein S deficiency type I. Seven different mutations were found in 9 of 10 families, including one frame shift mutation, a previously published splice site mutation (both occurring in two unrelated families), four missense mutations, and a stop codon at the beginning of exon 12. In family studies, cosegregation of the mutation with the disease could be demonstrated for five mutations; for two missense mutations, this was not possible due to limited family data. All seven mutations were the only abnormalities identified in the respective index patients and were absent in 44 to 62 normal individuals. Therefore, they most likely represent the causal gene defects. For five mutations, analysis of ectopic RNA could be performed. Mutant transcripts were present in the case of the frame shift and three of the missense mutations, while no mutant RNA could be detected in the case of the stop codon.

Adolescent↗
PubMed1995

Peptide bond cleavages and loss of functional activity during inactivation of factor Va and factor VaR506Q by activated protein C.

Factor V was purified from the plasma of an activated protein C (APC)-resistant patient who is homozygous for the mutation Arg506-->Gln (factor VR506Q). Factor VR506Q was converted by thrombin into factor Va which was further purified yielding a factor Va preparation that had the same cofactor activity in prothrombin activation as normal factor Va. Inactivation of low concentrations of normal factor Va (< 5 nM) by 0.15 nM APC in the presence of phospholipid vesicles proceeded via a biphasic reaction that consisted of a rapid phase (k = 4.3 x 10(7) M-1s-1), yielding a reaction intermediate with reduced cofactor activity that was fully inactivated during the subsequent slow phase (k = 2.3 x 10(6) M-1s-1). Inactivation of factor VaR506Q proceeded via a monophasic reaction (k = 1.7 x 10(6) M-1s-1). Immunoblot analysis showed that APC-catalyzed inactivation of factor Va occurred via peptide bond cleavages in the heavy chain. The rapid phase of inactivation of normal factor Va was associated with cleavage at Arg506 and full inactivation of factor Va required subsequent cleavage at Arg306. The slow monophasic inactivation of factor VaR506Q correlated with cleavage at Arg306. Cleavage at Arg506 in normal factor Va resulted in accumulation of a reaction intermediate that exhibited 40% cofactor activity in prothrombin activation mixtures that contained a high factor Xa concentration (5 nM). Compared with native factor Va, the reaction intermediate retained virtually no cofactor activity at low factor Xa concentrations (0.3 nM). This demonstrates that factor Va that is cleaved at Arg506 is impaired in its ability to interact with factor Xa. Michaelis-Menten kinetic analysis showed that cleavage at Arg506 in membrane-bound factor Va was characterized by a low Km for factor Va (20 nM) and kcat = 0.96 s-1. For cleavage at Arg306 in factor VaR506Q the kinetic parameters were Km = 196 nM and kcat = 0.37 s-1. This means that differences between APC-catalyzed inactivation of factors Va and VaR506Q become much less pronounced at high factor Va concentrations. When factor VaR506Q was inactivated by APC in the absence of phospholipids, cleavage at Arg679 of the heavy chain also contributed to factor Va inactivation. Comparison of rate constants for APC-catalyzed cleavage at Arg306, Arg506, and Arg679 in the absence and presence of phospholipids indicated that phospholipids accelerated these cleavages to a different extent.(ABSTRACT TRUNCATED AT 400 WORDS)

Arginine↗
PubMed1995

Antithrombins Southport (Leu 99 to Val) and Vienna (Gln 118 to Pro): two novel antithrombin variants with abnormal heparin binding.

We report the characterization of three variant antithrombins with reduced heparin binding as the primary abnormality. Two of these variants, antithrombin Southport (Leu 99 to Val, 2759 C to G) and antithrombin Vienna (Gln 118 to Pro, 5349 A to C) were novel, whereas the third, Pro 41 to Leu, has been previously described as antithrombin Basel. All three variants exhibited reduced binding for heparin on crossed immunoelectrophoresis and in a quantitative monoclonal antibody-based assay. The mutations were characterized by direct sequence analysis of enzymatically amplified genomic DNA and all affected individuals were heterozygous for the mutations. These three mutations do not occur at the sites of the basic amino acids directly involved in heparin binding nor do they result in a change in charge of the affected residue. It seems probable that they reduce heparin affinity either by perturbing the initial contact site involved in the heparin-binding domain (Arg 47, Arg 129 and possibly Arg 24), or by preventing the subsequent heparin-induced conformational change.

Adult↗
PubMed1995

Elimination of acquired factor VIII antibodies by extracorporal antibody-based immunoadsorption (Ig-Therasorb).

Treatment of potent factor VIII antibodies is a difficult problem. In some cases a reduction of the antibody titer is necessary for effective treatment with human factor VIII concentrates. We describe a new method for extracorporal elimination of factor VIII antibodies (antibody-based immunoadsorption). Blood is drawn from an antecubital vein, citrated, and plasma is separated with a rotating membrane. Plasma passes alternately through one of two columns filled with sepharose-coupled polyclonal sheep antibodies to human immunoglobulins (Ig-Therasorb), whereas the other column is regenerated. Each cycle has a duration of 15 min. Three patients with high titer factor VIII antibodies (one hemophiliac and 2 with spontaneous antibodies; titers 29, 132, and 313 BU/ml, respectively) were treated. The average reduction of the antibody titer was 76.1 +/- 17.2% per session. In each patient 4 sessions were necessary to reduce the antibody titer to < 1 BU/ml. The mean processed plasma volume was 6731 +/- 640 ml and the mean duration of each session 3.9 +/- 0.7 h. Serum IgG, IgA and IgM levels decreased by 75.3 +/- 11.9%, 62.9 +/- 19.1%, and 54.8 +/- 23.8% respectively. The procedure was tolerated without any side effects. Thus, rapid elimination of factor VIII inhibitors can be achieved with antibody-based immunoadsorption, which can be life-saving in some cases. This promising method should be evaluated in a larger number of patients.

Adult↗
PubMed1994

(ATT) trinucleotide repeats in the antithrombin gene and their use in determining the origin of repeated mutations.

Two (ATT) trinucleotide repeat polymorphisms have been identified in the tails of Alu repeat elements in intron 5 of the antithrombin gene. The frequency and distribution of allele sizes for the Alu 5 and Alu 8 tail polymorphisms have been defined in a sample Caucasian population. The Alu 5 polymorphism has two alleles while that of Alu 8 has 10 alleles with a heterozygosity of 0.83. These polymorphisms have been used in combination with four previously described polymorphisms within the antithrombin gene to construct antithrombin gene haplotypes in the sample Caucasian population. Twenty-two different haplotypes were observed, with the Alu 8 polymorphism being particularly useful in subdividing the core haplotype based on the previously identified polymorphisms. The haplotype data were used to investigate the origin of repeat mutations within the antithrombin locus. We compared the haplotypes associated the mutant antithrombin genes in five families with the mutation 2759C-->T (L99F) and five families with the mutation 5381C-->T (R129Stop). The mutation 2759C-->T (L99F), which occurs within a non-CpG dinucleotide, was carried on a gene associated with an identical haplotype in each of the five families. The mutation 5381C-->T (R129Stop), a single base substitution within a CpG dinucleotide, was associated with at least two different haplotypes. The findings suggest a founder effect in the five families sharing the 2759C-->T (L99F) and at least two independent origins for the CpG dinucleotide mutation 5381C-->T (R129Stop).

Antithrombins↗
PubMed1994

HLA class-I and -II antigens in chronic idiopathic autoimmune thrombocytopenia.

We studied MHC class-I and -II phenotypes in adult Caucasian patients with chronic idiopathic autoimmune thrombocytopenia (cAITP). Forty-five patients (median age 51 years, range 21-78 years) with a median disease duration of 7 years (range 2-26 years) were phenotyped for HLA-A, -B, -C by the standard lymphocytotoxicity test, HLA-DR and -DQ by restriction fragment-length polymorphism (RFLP), and -DP by oligonucleotide typing. Antiplatelet antibodies directed against glycoproteins Ib/IX and IIb/IIIa were determined by monoclonal antibody-specific immobilization of platelet antigens (MAIPA). The comparison of antigen frequencies of the whole group of patients with healthy controls revealed no significant difference for any of the MHC class-I or class-II specificities (p > 0.05). Patients were then divided into groups based on (a) their response to therapy, and (b) on whether they did or did not have detectable anti-platelet antibodies (n = 16 versus n = 29). All patients with a poor response to splenectomy carried the HLA-DPB1*0402 phenotype. The HLA-DPB1*1501 allele was found only among patients with detectable antiplatelet antibodies. These differences were not significant after correction for the number of tested antigens, however. Our data suggest that there is no association between MHC class-I/II alleles and adult cAITP or subgroups thereof.

Adult↗
PubMed1994

Homozygous antithrombin deficiency: report of two new cases (99 Leu to Phe) associated with arterial and venous thrombosis.

Inherited antithrombin deficiency is associated with an increased risk of thrombosis, primarily venous rather than arterial. Most affected individuals have inherited only a single copy of an abnormal antithrombin (AT) gene. Homozygously affected individuals, although rare, have a severe thrombotic history of early onset and often affecting the arteries. We report two new cases of type II HBS (heparin binding site) deficiency in which the propositi are homozygous for the previously reported mutation 99 Leu to Phe, and who have a severe thrombotic history. These cases are considered alongside existing homozygote and compound heterozygote cases.

Antithrombins↗