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Thromb Haemost 1996; 76(03): 283-291
DOI: 10.1055/s-0038-1650573
Original Article
Schattauer GmbH Stuttgart

Ala244Val Is a Common, Probably Ancient Mutation Causing Factor VII Deficiency in Moroccan and Iranian Jews

Hannah Tamary
1   The Pediatric Hematology Oncology Center, Schneider Children’s Medical Center of Israel, Tel Hashomer, Israel
2   Pediatric Hematology Oncology Laboratory, Felsenstein Research Center, Beilinson Medical Campus, Petah Tiqva, Tel Hashomer, Israel
,
Yonit Fromovich
2   Pediatric Hematology Oncology Laboratory, Felsenstein Research Center, Beilinson Medical Campus, Petah Tiqva, Tel Hashomer, Israel
,
Lea Shalmon
2   Pediatric Hematology Oncology Laboratory, Felsenstein Research Center, Beilinson Medical Campus, Petah Tiqva, Tel Hashomer, Israel
,
Ziv Reich
3   Departments of Organic Chemistry, Tel Hashomer, Israel
,
Orly Dym
4   Structural Biology, Weizmann Institute of Science, Rehovot, Tel Hashomer, Israel
,
Naomi Lanir
5   Thrombosis and Hemostatis Unit, Rambam Medical Center, Haifa, Tel Hashomer, Israel
,
Benjamin Brenner
5   Thrombosis and Hemostatis Unit, Rambam Medical Center, Haifa, Tel Hashomer, Israel
,
Michael Paz
6   Department of Pediatrics, Ziv Hospital, Safad, Tel Hashomer, Israel
,
Anthony S Luder
6   Department of Pediatrics, Ziv Hospital, Safad, Tel Hashomer, Israel
,
Orit Blau
2   Pediatric Hematology Oncology Laboratory, Felsenstein Research Center, Beilinson Medical Campus, Petah Tiqva, Tel Hashomer, Israel
,
Michael Korostishevsky
7   Department of Human Genetics, Sackler School of Medicine, Tel Aviv University, Tel Hashomer, Israel
,
Rina Zaizov
1   The Pediatric Hematology Oncology Center, Schneider Children’s Medical Center of Israel, Tel Hashomer, Israel
2   Pediatric Hematology Oncology Laboratory, Felsenstein Research Center, Beilinson Medical Campus, Petah Tiqva, Tel Hashomer, Israel
,
Uri Seligsohn
8   Institute of Thrombosis and Hemostasis, Department of Hematology, Chaim Sheba Medical Center, Tel Hashomer, Israel
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Publikationsverlauf

Received: 07. November 1995

Accepted after resubmission13. Mai 1996

Publikationsdatum:
10. Juli 2018 (online)

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Summary

We investigated the molecular basis for factor VII (FVII) deficiency in Israel and found that 13 patients were homozygous and 10 heterozygous for a C to T substitution at nucleotide 10648 of the FVII gene. This predicted an Ala244Val change and was associated with decreased FVII activity and antigen level. Of the 36 Ala244Val positive alleles, 20 were observed in patients of Moroccan origin, 10 in Iranian-Jewish patients and 6 in patients of other origins. A computer model of the serine protease domain of FVII suggested that the Ala244Val substitution may cause distortion of the entire protein structure. Intragenic polymorphic sites analyses disclosed a founder effect for the Moroccan and Iranian-Jewish patients. A survey of the Ala244Val mutation revealed an allele frequency of 1:42.5 in Moroccan Jews and 1:40 in Iranian Jews. As Moroccan Jews have been separated from Iranian Jews for more than two millennia, the data suggest that the Ala244Val mutation occurred in ancient times.

 

  • References

  • 1 Broze Jr GJ, Majeras PW. Purification and properties of human coagulation factor VII. J Biol Chem 1980; 255: 1242-1247
    PubMedSuche in Google Scholar
  • 2 Osterud B, Rapaport SI. Activation of factor IX by the reaction product of tissue factor and factor VII: Additional pathway for initiating blood coagulation. Proc Natl Acad Sci USA 1977; 74: 5260-5264
    CrossrefPubMedSuche in Google Scholar
  • 3 Furie B, Furie BC. Molecular and cellular biology of blood coagulation. N Engl J Med 1992; 326: 800-806
    CrossrefPubMedSuche in Google Scholar
  • 4 Seligsohn U, Osterud B, Brown SF, Griffin JH, Rapaport SI. Activation of human factor VII in plasma and in purified systems; roles of activated factor IX, kallikrein and activated factor XII. J Clin Invest 1979; 64: 1056-1065
    CrossrefPubMedSuche in Google Scholar
  • 5 Nakagaki T, Foster DC, Berkner KL, Kisiel W. Initiation of the extrinsic pathway of blood coagulation: evidence for the tissue factor dependent autoactivation of human coagulation factor VII. Biochemistry 1991; 30: 10819-10824
    CrossrefPubMedSuche in Google Scholar
  • 6 de Grouchy J, Dautzenberg MD, Turleau C, Beguin S, Chavin-Colin F. Regional mapping of clotting factors VII and X to 13q34. Expression of factor VII through chromosome 8. Hum Genet 1984; 66: 230-233
    PubMedSuche in Google Scholar
  • 7 O’Hara PJ, Grant FJ, Haldeman BA, Gray CL, Insley MY, Hagen FS, Murray MJ. Nucleotide sequence of the gene coding for human factor VII, a vitamin K-dependent protein participating in blood coagulation. Proc Natl Acad Sci USA 1987; 84: 5158-5162
    CrossrefPubMedSuche in Google Scholar
  • 8 Yoshitake S, Schach BG, Foster DC, Davie EW, Kurachi K. Nucleotide sequence of the gene for human factor IX (antihemophilic factor B). Biochemistry 1985; 24: 3736-3750
    CrossrefPubMedSuche in Google Scholar
  • 9 Leytus SP, Foster DC, Kurachi K, Davie EW. Gene for human factor X: A blood coagulation factor whose gene organization is essentially identical with that of factor IX and protein C. Biochemistry 1986; 25: 5098-5102
    CrossrefPubMedSuche in Google Scholar
  • 10 Alexander B, Goldstein R, Landwehr G, Cook CD. Congenital SPCA deficiency: A hitherto unrecognized coagulation defect with hemorrhage rectified by serum and serum reactions. J Clin Invest 1951; 30: 237-246
    CrossrefPubMedSuche in Google Scholar
  • 11 Ragni MV, Lewis JH, Spero JA, Hasiba U. Factor VII deficiency. Am J Hematol 1981; 10: 79-88
    CrossrefPubMedSuche in Google Scholar
  • 12 Mariani G, Mazzucconi MG. Factor VII congenital deficiency. Clinical picture and classification of the variants. Haemostatis 1983; 13: 169-177
    PubMedSuche in Google Scholar
  • 13 Briet E, Loeliger EA, Van Tilburg NH, Veltkamp IJ. Molecular variant of factor VII. Thromb Haemost 1976; 35: 289-294
    Thieme ConnectPubMedSuche in Google Scholar
  • 14 Triplett DA, Brandt JT, McGann Batard MA, Schaeffer Dixon JL, Fair DS. Hereditary factor VII deficiency: heterogeneity defined by combined functional and immunochemical analysis. Blood 1985; 66: 1284-1287
    PubMedSuche in Google Scholar
  • 15 Girolami A, Falezza G, Patrassi G, Stenico M, Vettore L. Factor VII Verona coagulation disorder: double heterozygosis with an abnormal factor VII and heterozygous factor VII deficiency. Blood 1977; 50: 603-610
    PubMedSuche in Google Scholar
  • 16 Girolami A, Cattarozzi G, Dal Bo Zanon R, Celia G, Toffanin F. Factor VII Padua another factor VII abnormality with defective of brain thromboplastin activation and complex hereditary pattern. Blood 1979; 54: 46-53
    PubMedSuche in Google Scholar
  • 17 Mariani G, Mazzucconi MG, Hermans J, Ciavarella N, Faiella A, Hassan HJ, Mannucci PM, Nenci GG, Orlando M, Romoli D, Mandelli F. Factor VII deficiency: immunological characterization of genetic variants and detection of carriers. Br J Haematol 1981; 48: 7-14
    PubMedSuche in Google Scholar
  • 18 O’Brien DP, Gale KM, Anderson JS, McVey JH, Miller GJ, Meade TW, Tuddenham EGD. Purification and characterization of factor VII 304-Gln: a variant molecule with reduced activity isolated from a clinically unaffected male. Blood 1991; 78: 132-140
    PubMedSuche in Google Scholar
  • 19 Millar DS, Cooper DN, Kakkar VV, Schwartz M, Scheibel E. Prenatal exclusion of severe factor VII deficiency by DNA sequencing. Lancet 1992; 339: 1359
    PubMedSuche in Google Scholar
  • 20 Bemardi F, Patracchini P, Gemmati D, Ferrati M, Arcieri P, Papacchini M, Redaelli R, Baudo F, Mariani G, Marchetti G. Molecular analysis of factor VII deficiency in Italy: a frequent mutation (FVII Lazio) in a repeated intronic region. Human Genet 1993; 92: 446-450
    CrossrefPubMedSuche in Google Scholar
  • 21 Takamiya O, Kemball-Cook G, Martin DMA, Cooper DN, Von Felten A, Meili E, Hann I, Prangnell DR, Lumley H, Tuddenham EGD, McVey JH. Detection of missense mutations by single-strand conformational polymorphism (SSCP) analysis in five dysfunctional variants of coagulation factor VII. Hum Mol Genet 1993; 2: 1355-1359
    CrossrefPubMedSuche in Google Scholar
  • 22 Marchetti G, Ferrati M, Patracchini P, Redaelli R, Bemardi F. A missense mutation (178Cys to Tyr) and two neutral dimorphisms (115His and 333Ser) in the human coagulation factor VII gene. Hum Mol Genet 1993; 2: 1055-1056
    CrossrefPubMedSuche in Google Scholar
  • 23 Bemardi F, Liney DL, Patracchini PP, Gemmati D, Legnani C, Arcieri P, Pinotti M, Redaelli R, Ballerini G, Pemberton S, Wacey AI, Mariani G, Tuddenham EGD, Marchetti G. Molecular defects in CRM+factor VII deficiencies: modelling of missense mutations in catalytic domain of FVII. Br J Haematol 1994; 86: 610-618
    CrossrefPubMedSuche in Google Scholar
  • 24 Ohiwa M, Hayashi T, Wada H, Minamikawa K, Shirakawa S, Suzuki K. Factor VII Mie: Homozygous asymptomatic type I deficiency caused by an amino acid substitution of His (CAC) for Arg (247) (CGC) in the catalytic domain. Thromb Haemost 1994; 71: 773-777
    Thieme ConnectPubMedSuche in Google Scholar
  • 25 Chaing S, Clarke B, Sridhara S, Chu K, Friedman P, VanDusen W, Roberts HR, Blajchman M, Monroe DM, High KA. Severe factor VII deficiency caused by mutations abolishing the cleavage site for activation and altering binding to tissue factor. Blood 1994; 83: 3524-3535
    PubMedSuche in Google Scholar
  • 26 Arbini AA, Bodkin D, Lopaciuk S, Bauer KA. Molecular analysis of Polish patients with factor VII deficiency. Blood 1994; 84: 2214-2220
    PubMedSuche in Google Scholar
  • 27 Tuddenham EGD, Pemberton S, Cooper DN. Inherited factor VII deficiency: genetic and molecular pathology. Thromb Haemost 1995; 74: 313-321
    Thieme ConnectPubMedSuche in Google Scholar
  • 28 Seligsohn U, Shani M, Ramot B, Adam A, Sheba C. Dubin-Johnson syndrome in Israel. II. Association with Factor-VII deficiency. Quart J Med 1970; 39: 569-584
    PubMedSuche in Google Scholar
  • 29 Goodman RM. A perspective on genetic diseases among the Jewish people. In: Genetic diseases among Ashkenazic Jews. Goodman RM, Motulsky AG, eds. New York: Raven Press 1979: 1-17
    PubMedSuche in Google Scholar
  • 30 Ben-Ezzer J, Rimington C, Shani M, Seligsohn U, Sheba C, Szeinberg A. Abnormal excretion of the isomers of urinary coproporphyrin by patients with Dubin-Johnson syndrome in Israel. Clin Sci 1971; 40: 17-30
    CrossrefPubMedSuche in Google Scholar
  • 31 Poncz M, Solowiejczyk D, Harpel B, Mory Y, Schwartz E, Surrey S. Construction of human gene libraries from small amounts of peripheral blood: analysis of beta-like globin genes. Hemoglobin 1982; 6: 27-36
    CrossrefPubMedSuche in Google Scholar
  • 32 Seligsohn U, Osterud B, Rapaport SI. Coupled amidolytic assay for factor VII: its use with a clotting assay to determine the activity state of factor VII. Blood 1978; 52: 978-988
    PubMedSuche in Google Scholar
  • 33 Thein SL, Hinton J. A simple and rapid method of direct sequencing using Dynabeads. Br J Haematol 1991; 79: 113-115
    CrossrefPubMedSuche in Google Scholar
  • 34 Green F, Kelleher C, Wilkes H, Temple A, Meade T, Humphries S. A common genetic polymorphism associated with lower coagulation factor VII levels in healthy individuals. Arterioscler Thromb 1991; 11: 540-546
    CrossrefPubMedSuche in Google Scholar
  • 35 Bemardi F, Marchetti G, Pinotti M, Baroncini C, Papcchini M, Zepponi E, Ursicino N, Chiarotti F, Mariani G. Factor VII gene polymorphism contribute about one third of the factor VII level variation in plasma. Arterioscler Thromb Vascular Biol 1996; 16: 72-76
    PubMedSuche in Google Scholar
  • 36 Sneath PH, Sokal RR. Numerical Taxonomy. W. H. Freeman and Company, San Francisco, CA, USA 1971
    PubMedSuche in Google Scholar
  • 37 Needleman SB, Wiinsch CD. A general method applicable to the search for similarities in the amino acid sequence of two proteins. J Mol Biol 1970; 48: 443-453
    CrossrefPubMedSuche in Google Scholar
  • 38 Greer J. Comparative modeling methods: application to the family of the mammalian serine proteases. Proteins 1990; 7: 317-334
    CrossrefPubMedSuche in Google Scholar
  • 39 Bernstein FC, Koetzle TF, Williams GJ, Meyer Jr EF, Brice MD, Rodger JR, Kennard O, Shimanouchi T, Tasumi M. The Protein Data Bank: a computer-based archival file for macromolecular structures. J Mol Biol 1977; 112: 535-542
    CrossrefPubMedSuche in Google Scholar
  • 40 Krulis PJ, Jones TA. Determination of three-dimensional protein structure from nuclear magnetic resonance data using fragments of known structures. Protein 1987; 2: 188-201
    PubMedSuche in Google Scholar
  • 41 Barker D, Schafer M, White R. Restriction sites containing CpG show a higher frequency of polymorphism in human DNA. Cell 1984; 36: 131-138
    CrossrefPubMedSuche in Google Scholar
  • 42 Greer J. Comparative model-building of the mammalian serine proteases. J Mol Biol 1981; 153: 1027-1042
    CrossrefPubMedSuche in Google Scholar
  • 43 Read RJ, Brayer GD, Jurasek L, James MN. Critical evaluation of comparative model building of Streptomyces griseus trypsin. Biochemistry 1984; 23: 6570-6575
    CrossrefPubMedSuche in Google Scholar
  • 44 Miyata T, Sakai T, Sugimoto M, Naka H, Yamamoto K, Yoshioka A, Fukui H, Mitsui K, Kamiya K, Umeyama H, Iwangag S. Factor IX Amagasaki: a new mutation in the catalytic domain resulting in the loss of both coagulant and esterase activities. Biochemistry 1991; 30: 11286-11291
    CrossrefPubMedSuche in Google Scholar
  • 45 Geddes VA, Le Bonniec BF, Louie GV, Brayer GD, Thompson AR, MacGillivray RT. A moderate form of hemophilia B is caused by a novel mutation in the protease domain of factor IXVancouver. J Biol Chem 1989; 264: 4689-4697
    PubMedSuche in Google Scholar
  • 46 Greer J. Model of a specific interaction. Salt bridges form between prothrombin and its activating enzyme blood clotting factor Xa. J Mol Biol 1981; 153: 1043-1053
    CrossrefPubMedSuche in Google Scholar
  • 47 Furie B, Bing DH, Feldmann RJ, Robison DJ, Bumier JP, Furie BC. Computer-generated models of blood coagulation factor Xa, factor IXa, and thrombin based upon structural homology with other serine proteases. J Biol Chem 1982; 257: 3875-3881
    PubMedSuche in Google Scholar
  • 48 Cool DE, Edgell SC, Louie GV, Zoller MJ, Brayer GD, MacGillivray RT. A characterization of human blood coagulation factor XII cDNA. Prediction of the primary structure of factor XII and the tertiary structure of (3-factor Xlla. J Biol Chem 1985; 260: 13666-13676
    PubMedSuche in Google Scholar
  • 49 Koeberl DD, Bottema CDK, Ketterling RP, Bridge PJ, Lillicrap DP, Somer SS. Mutations causing hemophilia B: direct estimate of the underlying rates of spontaneous germ-line transitions, transversions and deletions in the human gene. Am J Hum Genet 1990; 47: 202-217
    PubMedSuche in Google Scholar
  • 50 Wacey AI, Pemberton S, Cooper DN, Kakkar VV, Tuddenham EGD. A molecular model of the serine protease domain of activated protein C: application to the study of missense mutations causing protein C deficiency. Br J Hematol 1993; 84: 290-300
    CrossrefPubMedSuche in Google Scholar
  • 51 Humphries SE, Lane A, Dawson S, Green FR. The study of gene-environ-ment interactions that influence thrombosis and fibrinolysis. Arch Pathol Lab Med 1992; 116: 1322-1329
    PubMedSuche in Google Scholar
  • 52 Arbini AA, Bauer KA. Reduced plasma factor VII coagulant activity due to the Arg 353 Gin polymorphism in the factor VII gene results from defective secretion. Blood (abstr) 1994; 84: 333a
    PubMedSuche in Google Scholar