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Thromb Haemost 1993; 70(02): 361-369
DOI: 10.1055/s-0038-1649581
Scientific and Standardization Committee Communications
Schattauer GmbH Stuttgart

Antithrombin III Mutation Database: First Update

For the Thrombin and its Inhibitors Subcommittee of the Scientific and Standardization Committee of the International Society on Thrombosis and Haemostasis
D A Lane
The Charing Cross and Westminster Medical School, London, UK, Institute of Molecular Medicine, Oxford, UK, Thrombosis Research Institute, London, UK, the McMaster University, Hamilton, Canada, University of Cambridge, UK, and Hôpital Broussais, Paris, France
,
R J Olds
The Charing Cross and Westminster Medical School, London, UK, Institute of Molecular Medicine, Oxford, UK, Thrombosis Research Institute, London, UK, the McMaster University, Hamilton, Canada, University of Cambridge, UK, and Hôpital Broussais, Paris, France
,
M Boisclair
The Charing Cross and Westminster Medical School, London, UK, Institute of Molecular Medicine, Oxford, UK, Thrombosis Research Institute, London, UK, the McMaster University, Hamilton, Canada, University of Cambridge, UK, and Hôpital Broussais, Paris, France
,
V Chowdhury
The Charing Cross and Westminster Medical School, London, UK, Institute of Molecular Medicine, Oxford, UK, Thrombosis Research Institute, London, UK, the McMaster University, Hamilton, Canada, University of Cambridge, UK, and Hôpital Broussais, Paris, France
,
S L Thein
The Charing Cross and Westminster Medical School, London, UK, Institute of Molecular Medicine, Oxford, UK, Thrombosis Research Institute, London, UK, the McMaster University, Hamilton, Canada, University of Cambridge, UK, and Hôpital Broussais, Paris, France
,
D N Cooper
The Charing Cross and Westminster Medical School, London, UK, Institute of Molecular Medicine, Oxford, UK, Thrombosis Research Institute, London, UK, the McMaster University, Hamilton, Canada, University of Cambridge, UK, and Hôpital Broussais, Paris, France
,
M Blajchman
The Charing Cross and Westminster Medical School, London, UK, Institute of Molecular Medicine, Oxford, UK, Thrombosis Research Institute, London, UK, the McMaster University, Hamilton, Canada, University of Cambridge, UK, and Hôpital Broussais, Paris, France
,
D Perry
The Charing Cross and Westminster Medical School, London, UK, Institute of Molecular Medicine, Oxford, UK, Thrombosis Research Institute, London, UK, the McMaster University, Hamilton, Canada, University of Cambridge, UK, and Hôpital Broussais, Paris, France
,
J Emmerich
The Charing Cross and Westminster Medical School, London, UK, Institute of Molecular Medicine, Oxford, UK, Thrombosis Research Institute, London, UK, the McMaster University, Hamilton, Canada, University of Cambridge, UK, and Hôpital Broussais, Paris, France
,
M Aiach
The Charing Cross and Westminster Medical School, London, UK, Institute of Molecular Medicine, Oxford, UK, Thrombosis Research Institute, London, UK, the McMaster University, Hamilton, Canada, University of Cambridge, UK, and Hôpital Broussais, Paris, France
› Author Affiliations
Further Information

Publication History

Publication Date:
04 July 2018 (online)

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  • References

  • 1 Lane DA, Ireland H, Olds RJ, Thein SL, Perry DJ, Aiach M. Antithrombin III: a database of mutations. Thromb Haemostas 1991; 66: 657-661
    PubMedGoogle Scholar
  • 2 Bjork I, Olson ST, Shore JD. Molecular mechanisms of the accelerating effect of heparin on the reactions between antithrombin and the clotting proteinases. In: Heparin: Chemical and Biological Properties, Clinical Applications. Lane DA, Lindahl U. (eds) Edward Arnold; London: 1989: 229-255
  • 3 Huber R, Carrell RW. Implications of the three dimensional structure of a1 antitrypsin for structure and function of serpins. Biochemistry 1989; 28: 8951-8966
    CrossrefPubMedGoogle Scholar
  • 4 Lane DA, Caso R. Antithrombin: structure, genomic organization, function and inherited deficiency. Bailliere’s Clin Haematol 1989; 2: 961-968
    CrossrefPubMedGoogle Scholar
  • 5 Lane DA, Olds RJ, Thein SL. Antithrombin and its deficiency states. Blood Coag Fibrinolysis 1992; 3: 315-341
    CrossrefPubMedGoogle Scholar
  • 6 Blajchman MA, Austin RC, Fernandez-Rachubinski F, Sheffield WP. Molecular basis of inherited human antithrombin deficiency. Blood 1992; 80: 2159-2171
    PubMedGoogle Scholar
  • 7 Abildgaard U. Highly purified antithrombin III with heparin cofactor activity prepared by disc gel electrophoresis. Scand J Clin Lab Invest 1968; 21: 89-91
    CrossrefPubMedGoogle Scholar
  • 8 Abildgaard U. Binding of thrombin to antithrombin III. Scand J Clin Lab Invest 1969; 24: 23-27
    CrossrefPubMedGoogle Scholar
  • 9 Rosenberg RD, Damus PS. The purification and mechanism of action of human antithrombin-heparin cofactor. J Biol Chem 1973; 248: 6490-6505
    PubMedGoogle Scholar
  • 10 Bjork I, Danielsson A, Fenton JW, Jornvall H. The site in human antithrombin for functional proteolytic cleavage by human thrombin. FEBS Letts 1981; 126: 257-260
    CrossrefPubMedGoogle Scholar
  • 11 Bjork I, Jackson CM, Jornvall H, Lavine KK, Nording K, Salsgiver WJ. The active site of antithrombin. Release of the same proteolytically cleaved form of the inhibitor from complexes with Factor IXa, Factor Xa and thrombin. J Biol Chem 1982; 257: 2406-2411
    PubMedGoogle Scholar
  • 12 Egeberg O. Inherited antithrombin III deficiency causing thrombophilia. Thromb Diath Haemorrhag 1965; 13: 516-530
    PubMedGoogle Scholar
  • 13 Thaler E, Lechner K. Antithrombin III deficiency and thromboembolism. Clin Hematol 1981; 10: 369-390
    PubMedGoogle Scholar
  • 14 Sas G, Banhegyi D, Blasko G, Domjam G. Heterogeneity of the “classical” antithrombin III deficiency. Thromb Haemostas 1980; 43: 133-136
    PubMedGoogle Scholar
  • 15 Sas G. Hereditary antithrombin III deficiency: biochemical aspects. Haematologia 1984; 7: 81-86
    PubMedGoogle Scholar
  • 16 Hultin MB, McKay J, Abildgaard U. Antithrombin Olso: Type Ib classification of the first reported antithrombin-deficient family with a review of the hereditary antithrombin variants. Thromb Haemostas 1988; 59: 468-473
    PubMedGoogle Scholar
  • 17 Finazzi G, Caccia R, Barbui T. Different prevalence of thromboembolism in the subtypes of congenital antithrombin III deficiency: review of 404 cases. Thromb Haemostas 1987; 58: 1094
    PubMedGoogle Scholar
  • 18 Lane DA, Olds RJ, Conard J, Boisclair M, Bock SC, Hultin M, Abildgaard U, Ireland H, Thompson E, Sas G, Horellou MH, Tamponi G, Thein SL. Pleiotropic effects of antithrombin strand 1C substitution mutations. J Clin Invest 1992; 90: 2422-2433
    CrossrefPubMedGoogle Scholar
  • 19 Olds RJ, Lane DA, Chowdury V, De Stefano V, Leone G, Thein SL. Complete nucleotide sequence of the antithrombin gene. Evidence for homologous recombination causing thrombophilia. Biochemistry 1993; 32: 4216-4224
    CrossrefPubMedGoogle Scholar
  • 20 Bock SC, Harris JF, Schwartz CE, Ward JH, Hershgold EJ, Skolnick MH. Hereditary thrombosis in a Utah kindred is caused by a dysfunctional antithrombin III gene. Am J Hum Genet 1985; 37: 32-41
    PubMedGoogle Scholar
  • 21 Olds RJ, Lane DA, Beresford CH, Abildgaard U, Hughes PM, Thein SL. A recurrent deletion in the antithrombin gene, AT106-108(-6bp), identified by DNA heteroduplex detection. Genomics 1993; 16: 298-299
    CrossrefPubMedGoogle Scholar
  • 22 Daly ME, Perry DJ, Harper PL, Carrell RW. The molecular basis of quantitative antithrombin deficiency in 8 unrelated families. Brit J Haematol 1992; 80: 15
    CrossrefPubMedGoogle Scholar
  • 23 Daly M, Perry DJ, Harper PL, Daly HM, Roques AWW, Carrell RW. Insertions/deletions in the antithrombin gene: 3 mutations associated with non-expression. Thromb Haemostas 1992; 67: 521-525
    PubMedGoogle Scholar
  • 24 Chowdhury V, Olds RJ, Lane DA, Conard J, Pabinger I, Ryan K, Bauer K, Bhavani M, Abildgaard U, Finazzi G, Castaman G, Mannucci PM, Thein SL. Identification of nine novel mutations in type I antithrombin deficiency by heteroduplex screening. Brit J Haematol. 1993 In press
    PubMedGoogle Scholar
  • 25 Olds RJ, Lane DA, Ireland H, Leone G, De Stefano V, Wiesel ML, Cazenave JP, Thein SL. Novel point mutations leading to type I antithrombin deficiency and thrombosis. Brit J Haematol 1991; 78: 408-413
    CrossrefPubMedGoogle Scholar
  • 26 Miller DS, Lopez A, White D, Abraham G, Laursen B, Holding S, Reverter JC, Reynand J, Martinowitz U, Hayes JPLA, Kakkar VV, Cooper DN. Screening for mutations in the antithrombin III (AT3) gene causing recurrent venous thrombosis by single strand conformation polymorphism analysis. Human Mutation. 1993 In press
    PubMedGoogle Scholar
  • 27 Olds RJ, Lane DA, Finazzi G, Barbui T, Thein SL. A frameshift mutation leading to type 1 antithrombin deficiency and thrombosis. Blood 1990; 76: 2182-2186
    PubMedGoogle Scholar
  • 28 Gandrille S, Vidaud D, Emmerich J, Clauser E, Sie P, Fiessinger JN, Alhenc-Gelas M, Priollet P, Aiach M. Molecular basis for hereditary antithrombin III quantitative deficiencies: a stop codon in exon IIIa and a frameshift in exon VI. Brit J Haematol 1991; 78: 414-420
    CrossrefPubMedGoogle Scholar
  • 29 Olds RJ, Lane DA, Ireland H, Finazzi G, Barbui T, Abildgaard U, Girolami A, Thein SL. A common point mutation producing type Ia antithrombin III deficiency: AT129 CGA to TGA (Arg to Stop). Thrombos Res 1991; 64: 621-625
    CrossrefPubMedGoogle Scholar
  • 30 Tomonori A, Iwahana H, Yoshimoto K, Shigekiyo T, Saito S, Itakura M. Two new nonsense mutations in type Ia antithrombin III deficiency at Leu 140 and Arg 197. Thromb Haemostas 1992; 68: 455-459
    PubMedGoogle Scholar
  • 31 Berg LP, Grundy CB, Thomas F, Millar DS, Green PJ, Slomski R, Reiss J, Kakkar VV, Cooper DN. De novo splice site mutation in the antithrombin III (AT3) gene causing recurrent venous thrombosis: demonstration of exon skipping by ectopic transcript analysis. Genomics 1992; 13: 1359-1361
    CrossrefPubMedGoogle Scholar
  • 32 Vidaud D, Emmerich J, Sirieix ME, Sie P, Alhenc-Gelas M, Aiach M. Molecular basis for antithrombin III type I deficiency: 3 novel mutations located in exon IV. Blood 1991; 78: 2305-2309
    PubMedGoogle Scholar
  • 33 Grundy CB, Thomas F, Millar DS, Krawczak M, Melissari E, Lindo V, Moffat E, Kakkar VV, Cooper DN. Recurrent deletion in the human antithrombin III gene. Blood 1991; 78: 1027-1032
    PubMedGoogle Scholar
  • 34 Grundy CB, Holding S, Millar DS, Kakkar VV, Cooper DN. A novel missense mutation in the antithrombin III gene (Ser 349 to Pro) causing recurrent venous thrombosis. Human Genet 1992; 88: 707-708
    CrossrefPubMedGoogle Scholar
  • 35 Vidaud D, Gandrille S, Emmerich J, Sirieix M, Alhenc-Gelas M, Fiessinger JN, Sie P, Gouault M, Aiach M. Identification of 6 novel mutations responsible for type I AT III deficiencies. Thromb Haemostas 1991; 65: 762
    PubMedGoogle Scholar
  • 36 White D, Abraham G, Carter C, Kakkar VV, Cooper DN. A novel missense mutation in the antithrombin III gene (Ala 387 to Val) causing recurrent venous thrombosis. Hum Genet. 1992 In press
    PubMedGoogle Scholar
  • 37 Vidaud D, Sireix ME, Ahlenc-Gelas M, Chadeuf G, Aillaud MF, Juhan-Vague I, Aiach M. A double heterozygosity in 2 brothers with antithrombin (ATIII) deficiency due to the association of an Arg 47 to His mutation with a 9 base pair (bp) deletion in exon VI. Thromb Haemostas 1991; 65: 838
    PubMedGoogle Scholar
  • 38 Fernandez-Rachubinski RA, Rachubinski RA, Blajchman MA. Partial deletion of antithrombin III allele in a kindred with a type I deficiency. Blood 1992; 80: 1476-1485
    PubMedGoogle Scholar
  • 39 Olds RJ, Lane DA, Chowdury V, Samson D, DeStafano V, Leone G, Wiesel ML, Cazenave JP, Conard J, Thein SL. Major rearrangements within the antithrombin gene locus: an unusual cause for antithrombin deficiency. Brit J Haematol 1992; 40
    PubMedGoogle Scholar
  • 40 Winter JH, Bennett B, Watt JL, Brown T, San RomanC, Schinzel A, King J, Cooke PJL. Confirmation of linkage between antithrombin III and Duffy blood group and assignment of AT3 to lq22-25. Annal Human Genet 1982; 26: 29-34
    PubMedGoogle Scholar
  • 41 Prochownik EV, Antonarakis S, Bauer KA, Rosenberg RD, Fearon ER, Orkin SH. Molecular heterogeneity of inherited antithrombin III deficiency. N Engl J Med 1983; 308: 1549-1552
    CrossrefPubMedGoogle Scholar
  • 42 Bock SC, Prochownik EV. Molecular genetic survey of 16 kindreds with hereditary antithrombin III deficiency. Blood 1987; 70: 1273-1278
    PubMedGoogle Scholar
  • 43 Devraj-Kizuk R, Chui DHK, Prochownik EV, Carter CJ, Ofosu FA, Blajchman MA. Antithrombin III Hamilton: a gene with a point mutation (guanine to adenine) in codon 382 causing impaired serine protease reactivity. Blood 1988; 72: 1518-1523
    PubMedGoogle Scholar
  • 44 Austin RC, Rachubinsky RA, Ofosu FA, Blajchman MA. Antithrombin-III-Hamilton, Ala 382 to Thr: an antithrombin-III variant that acts as a substrate but not an inhibitor of α-thrombin and Factor Xa. Blood 1991; 77: 2185-2189
    PubMedGoogle Scholar
  • 45 Perry DJ, Carrell RW. CpG dinucleotides are “hotspots” for mutation in the antithrombin III gene. Twelve variants identified using the polymerase chain reaction. Mol Biol Med 1989; 6: 239-243
    PubMedGoogle Scholar
  • 46 Ireland H, Lane DA, Thompson E, Walker ID, Blench I, Morris HR, Freyssinet JM, Grunebaun L, Olds R, Thein SL. Antithrombin Glasgow II: alanine to threonine mutation in the serpin P12 position, resulting in a substrate reaction with thrombin. Brit J Haematol 1991; 79: 70-74
    CrossrefPubMedGoogle Scholar
  • 47 Caso R, Lane DA, Thompson EA, Olds RJ, Thein SL, Panico M, Blench I, Morris H, Freyssinet JM, Aiach M, Rodeghiero F, Finazzi G. Antithrombin Vicenza, Ala 384 to Pro (GCA to CCA) mutation transforming the inhibitor into a substrate. Brit J Haematol 1991; 77: 87-92
    CrossrefPubMedGoogle Scholar
  • 48 Mohlo-Sabatier P, Aiach M, Gaillard I, Fiessinger JN, Fischer AM, Chadeuf G, Clauser E. Molecular characterization of antithrombin III (ATIII) variants using polymerase chain reaction. Identification of the ATIII Charleville as an Ala 384 Pro mutation. J Clin Invest 1989; 84: 1236-1241
    CrossrefPubMedGoogle Scholar
  • 49 Perry DJ, Harper PL, Fairham S, Daly M, Carrell RW. Antithrombin Cambridge, 384 Ala to Pro: A new variant identified using the polymerase chain reaction. FEBS Letts 1989; 254: 174-176
    CrossrefPubMedGoogle Scholar
  • 50 Penwarchuk WJ, Fernandez-Rachubinski F, Rachubinski RA, Blajchman MA. Antithrombin III Sudbury, an Ala 384 to Pro mutation with abnormal thrombin binding activity and thrombotic diathesis. Thrombos Res 1990; 59: 793-798
    CrossrefPubMedGoogle Scholar
  • 51 Perry DJ, Daly M, Harper PL, Tait RC, Price J, Walker ID, Carrell RW. Antithrombin Cambridge II, 384 Ala to Ser. Further evidence of the role of the reactive centre loop in the inhibitory function of the serpin. FEBS Letts 1991; 285: 248-250
    CrossrefPubMedGoogle Scholar
  • 52 Blajchman MA, Fernandez-Rachubinsky F, Sheffield WP, Austin RC, Schulman S. Antithrombin III Stockholm: a codon 392 (Gly to Asp) mutation with normal heparin binding an impaired serine protease reactivity. Blood 1992; 79: 1428-1434
    PubMedGoogle Scholar
  • 53 Erdjument H, Lane DA, Ireland H, Panico M, DiMarzo V, Blench I, Morris HR. Formation of a covalent disulfide-linked antithrombin complex by an antithrombin variant, antithrombin Northwick Park. J Biol Chem 1987; 262: 13381-13384
    PubMedGoogle Scholar
  • 54 Erdjument H, Lane DA, Panico M, diMarzo V, Morris HR. Single amino acid substitutions in the reactive site of antithrombin leading to thrombosis. Congenital subsitution of arginine 393 to cysteine in antithrombin Northwick Park and to histidine in antithrombin Glasgow. J Biol Chem 1988; 263: 5589-5593
    PubMedGoogle Scholar
  • 55 Erdjument H, Lane DA, Ireland H, DiMarzo V, Panico M, Morris HR, Tripodi A, Mannucci PM. Antithrombin Milano, single amino acid subsitution at the reactive site, Arg 393 to Cys. Thromb Haemostas 1988; 60: 471-475
    PubMedGoogle Scholar
  • 56 Ireland H, Lane DA, Thompson E, Olds R, Thein SL, Hach-Wunderle V, Scharrer I. Antithrombin Frankfurt I: arginine to cysteine substitution at the reactive site and formation of a variant antithrombin-albumin covalent complex. Thromb Haemostas 1991; 65: 913
    PubMedGoogle Scholar
  • 57 Lane DA, Erdjument H, Flynn A, DiMarzo V, Panico M, Morris H, Greaves M, Dolan G, Preston FE. Antithrombin Sheffield: amino acid substitution at the reactive site (Arg 393 to His) causing thrombosis. Brit J Haematol 1989; 71: 91-96
    CrossrefPubMedGoogle Scholar
  • 58 Erdjument H, Lane DA, Panico M, DiMarzo V, Morris HR, Bauer K, Rosenberg RD. Antithrombin Chicago, amino acid substitution of arginine 393 to histidine. Thrombos Res 1989; 54: 613-619
    CrossrefPubMedGoogle Scholar
  • 59 Lane DA, Erdjument H, Thompson E, Panico M, DiMarzo V, Morris HR, Leone G, De Stefano V, Thein SL. A novel amino acid substitution in the reactive site of a congenital variant antithrombin. Antithrombin Pescara, Arg 393 to Pro, caused by CGT to CCT mutation. J Biol Chem 1989; 264: 10200-10204
    PubMedGoogle Scholar
  • 60 Owen MC, George PM, Lane DA, Boswell DR. P1 variant antithrombins Glasgow (393 Arg to His) and Pescara (303 Arg to Pro) have increased heparin affinity and are resistant to catalytic cleavage by elastase. Implications for the heparin activation mechanism. FEBS Letts 1991; 280: 216-220
    CrossrefPubMedGoogle Scholar
  • 61 Stephens AW, Thalley BS, Hirs CHW. Antithrombin Denver, a reactive site variant. J Biol Chem 1987; 262: 1044-1048
    PubMedGoogle Scholar
  • 62 Olds RJ, Lane D, Caso R, Tripodi A, Mannucci PM, Thein SL. Antithrombin III Milano 2: a single base substitution in the thrombin binding domain detected with PCR and direct genomic sequencing. Nucleic Acid Res 1989; 17: 10511
    CrossrefPubMedGoogle Scholar
  • 63 Brennan SO, Borg JY, George PM, Soria C, Soria J, Caen J, Carrell RW. New carbohydrate site in mutant antithrombin (7lle-Asn) with decreased heparin affinity. FEBS Letts 1988; 237: 118-122
    CrossrefPubMedGoogle Scholar
  • 64 Borg JY, Brennan SO, Carrell RW, George P, Perry DJ, Shaw J. Antithrombin Rouven IV 24 Arg to Cys. The amino terminal contribution to heparin binding. FEBS Letts 1990; 266: 163-166
    CrossrefPubMedGoogle Scholar
  • 65 Chang JY, Tran TH. Antithrombin Basel. Identification of a Pro-Leu substitution in a hereditary abnormal antithrombin with impaired heparin cofactor activity. J Biol Chem 1986; 261: 1174-1176
    PubMedGoogle Scholar
  • 66 Daly M, Ball R, O’Meara A, Hallinan FM. Identification and characterisation of an antithrombin III mutant (AT Dublin 2) with marginally decreased heparin reactivity. Thrombos Res 1989; 56: 503-513
    CrossrefPubMedGoogle Scholar
  • 67 KoiDe T, Odani S, Takahashi K, Ono T, Sakuragawa N. Antithrombin III Toyama; replacement of Arginine 47 by Cysteine in hereditary abnormal antithrombin III that lacks heparin-binding ability. Proc Natl Acad Sci USA 1984; 81: 289-293
    CrossrefPubMedGoogle Scholar
  • 68 Duchange N, Chasse JF, Cohen GN, Zakin MM. Identification of a mutation leading to cysteine replacement in a silent deficiency. Nucleic Acid Res 1986; 14: 2408
    CrossrefPubMedGoogle Scholar
  • 69 Brunel F, Duchange N, Fischer AM, Cohen GN, Zakin MM. Antithrombin III Alger: a new case of Arg 47 – Cys mutation. Amer J Haematol 1987; 25: 223-224
    PubMedGoogle Scholar
  • 70 Olds RJ, Lane DA, Caso R, Girolami A, Thein SL. Antithrombin III Padua II: a single base substitution in exon 2 detected using PCR and direct genomic sequencing. Nucleic Acid Res 1990; 18: 1926
    CrossrefPubMedGoogle Scholar
  • 71 Owen MC, Shaw GJ, Grau E, Fontcuberta J, Carrell RW, Boswell DR. Molecular characterisation of antithrombin Barcelona 2: 47 arginine to cysteine. Thrombos Res 1989; 55: 451-457
    CrossrefPubMedGoogle Scholar
  • 72 Femandez-Rachubinski F, Rachubinski R, Blajchman MA. Genetic characterisation of kindreds with antithrombin III (AT-III) deficiency using selected amplification of the gene. Blood 1990; 76: 506a
    PubMedGoogle Scholar
  • 73 Ueyama H, Murakami T, Nishiguchi S, Maeda S, Hashimoto Y, Okajima K, Shimada K, Araki S. Antithrombin Kumamoto. Identification of a point mutation and genotype analysis of the family. Thromb Haemostas 1990; 63: 231-234
    PubMedGoogle Scholar
  • 74 Borg JY, Owen MC, Soria C, Soria J, Caen J, Carrell RW. Arginine 47 is a prime heparin binding site in antithrombin. A new variant Rouen II, 47 Arg to Ser. J Clin Invest 1988; 81: 1292-1296
    CrossrefPubMedGoogle Scholar
  • 75 Owen MC, Borg JY, Soria C, Soria J, Caen J, Carrell RW. Heparin binding defect in new antithrombin III variant: Rouen, 47 Arg to His. Blood 1987; 69: 1275-1279
    PubMedGoogle Scholar
  • 76 Caso R, Lane DA, Thompson E, Zangouras D, Panico M, Morris H, Olds RJ, Thein SL, Girolami A. Antithrombin Padua I: impaired heparin binding caused by an Arg 47 to His (CGT to CAT) substitution. Thrombos Res 1990; 58: 185-190
    CrossrefPubMedGoogle Scholar
  • 77 Wolf M, Boyer-Neumann C, Mohlo-Sabatier P, Neumann C, Meyer D, Larrieu MJ. Familial variant of antithrombin III (ATIII Bligny, 47 Arg to His) associated with protein C deficiency. Thromb Haemostas 1990; 63: 215-219
    PubMedGoogle Scholar
  • 78 Olds RJ, Lane DA, Boisclair M, Sas G, Bock SC, Thein SL. Antithrombin Budapest 3: an antithrombin variant with reduced heparin affinity resulting from the substitution L99F. FEBS Letts 1992; 300: 241-246
    CrossrefPubMedGoogle Scholar
  • 79 Gandrille S, Aiach M, Lane DA, Vidaut D, Mohlo-Sabatier P, Caso R, de Moerloose P, Fiessinger JN, Clauser E. Important role of Arg 129 in heparin binding site of antithrombin III: identification of novel mutation Arg 129 to Gin. J Biol Chem 1990; 265: 18997-19001
    PubMedGoogle Scholar
  • 80 Olds RJ, Thein SL, Ireland H, Lane DA, Boisclair M, Conard J, Horellou MH. Identification of 402 phenylalanine as a functionally important residue in antithrombin. Thromb Haemostas 1991; 65: 670
    PubMedGoogle Scholar
  • 81 Bock SC, Silberman JA, Wikoff W, Abildgaard U, Hultin MB. Identification of a threonine for alanine substitution at residue 404 of antithrombin III Oslo suggests integrity of the 404-407 region is important for maintaining normal inhibitor levels. Thromb Haemostas 1989; 62: 494
    PubMedGoogle Scholar
  • 82 Nakagawa M, Tanaka S, Tsuji H, Takada O, Ono T. Congenital antithrombin deficiency (ATIII Kyoto): identification of a point mutation altering arginine-406 to methionine behind the reactive site. Thrombos Res 1991; 64: 101-108
    CrossrefPubMedGoogle Scholar
  • 83 Bock SC, Marrinan JA, Radziejewska E. Antithrombin III Utah: proline 407 to leucine mutation in a highly conserved region near the inhibitor reactive site. Biochemistry 1988; 27: 6171-6178
    CrossrefPubMedGoogle Scholar
  • 84 Olds RJ, Lane DA, Caso R, Panico M, Morris HR, Sas G, Dawes J, Thein SL. Antithrombin III Budapest: a single amino acid substitution (429 Pro to Leu) in a region highly conserved in the serpin super family. Blood 1992; 79: 1206-1212
    PubMedGoogle Scholar
  • 85 Bock SC, Levitan DJ. Characterisation of an unusual length polymorphism 5′ to the antithrombin III gene. Nucleic Acid Res 1983; 11: 8569-8582
    CrossrefPubMedGoogle Scholar
  • 86 Bock SC, Radziejewska E. A Nhe 1 RFLP in the human antithrombin III gene (lq23-25) (AT3). Nucleic Acid Res 1991; 19: 2519
    PubMedGoogle Scholar
  • 87 Daly ME, Perry DJ. Dde I polymorphism in intron 5 in the antithrombin III gene. Nucleic Acid Res 1990; 18: 5583
    PubMedGoogle Scholar
  • 88 Daly M, Bruce D, Perry DJ, Price J, Harper PL, O’Meara A, Carrell RW. Antithrombin Dublin (-3 Val to Glu): an N-terminal variant which has an aberrant signal peptide cleavage site. FEBS Letts 1990; 273: 87-90
    CrossrefPubMedGoogle Scholar
  • 89 Wu S, Seino S, Bell GI. Human antithrombin III (AT3) gene length polymorphism revealed by the polymerase chain reaction. Nucl Acids Res 1989; 17: 6433
    CrossrefPubMedGoogle Scholar
  • 90 Bock SC, Wion KL, Vehar GA, Lawn RM. Cloning and expression of the cDNA for human antithrombin III gene. Nucleic Acid Res 1982; 10: 8113-8125
    CrossrefPubMedGoogle Scholar
  • 91 Prochownik EV, Markham AF, Orkin SH. Isolation of a cDNA clone for human antithrombin III. J Biol Chem 1983; 258: 8389-8393
    PubMedGoogle Scholar
  • 92 Chandra T, Stackhouse R, Kidd VJ, Woo SLC. Isolation and sequence characterisation of a cDNA clone of human antithrombin III. Proc Natl Acad Sci USA 1983; 80: 184-258
    PubMedGoogle Scholar
  • 93 Prochownik EV, Orkin SH. In vivo transcription of a human antithrombin III “minigene”. J Biol Chem 1984; 259: 15386-15392
    PubMedGoogle Scholar
  • 94 Prochownik EV, Bock SC, Orkin SH. Intron structure of the human antithrombin III gene differs from that of other members of the serine protease inhibitor superfamily. J Biol Chem 1985; 260: 9608-9612
    PubMedGoogle Scholar
  • 95 Jagd S, Vibe-Pedersen K, Magnusson S. Location of two of the introns in the antithrombin-III gene. FEBS Letts 1985; 193: 213-216
    CrossrefPubMedGoogle Scholar