A New Mutation (Arg251Trp) in the Ca2+ Binding Site of Factor X Protease Domain Appears to be Responsible for the Defect in the Extrinsic Pathway Activation of Factor X Padua

Clinical and Applied Thrombosis/Hemostasis

Volumn 10, Issue 1, 2004, Pages 5-8

  Girolami, Antonio ^a,b   Vianello, Fabrizio ^a   Cabrio, Laura ^a   Lombardi, Anna Maria ^a  

^a UNIVERSITY OF PADUA MEDICAL SCHOOL   (Italy)

^b Institute of Medical Semeiotics   (Italy)

Author keywords

Factor X mutations; FX defects; FX variants

Indexed keywords

ARGININE; BLOOD CLOTTING FACTOR 10; BLOOD CLOTTING FACTOR 10 PADUA; TRYPTOPHAN; UNCLASSIFIED DRUG;

ADULT; AMINO ACID SUBSTITUTION; ARTICLE; BINDING SITE; CALCIUM BINDING; CASE REPORT; EXON; FEMALE; GENE AMPLIFICATION; GENE MUTATION; HETEROZYGOSITY; HOMOZYGOSITY; HUMAN; HUMAN CELL; INTRON; MOLECULAR MODEL; NUCLEIC ACID BASE SUBSTITUTION; NUCLEOTIDE SEQUENCE; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STABILITY; PROTHROMBIN TIME; SEQUENCE ANALYSIS;

EID: 2142662937     PISSN: 10760296     EISSN: None     Source Type: Journal    
DOI: 10.1177/107602960401000102     Document Type: Article

References (15)

1. James HL. Physiology and biochemistry of factor X. In: Bloom AL, Forbes CD, Thomas DP, Tuddenham EGD, eds. Haemostasis and Thrombosis. Edinburgh: Churchill Livingstone; 1994, p. 439.
2. Hoffman M, Monroe DM III. A cell-based model of hemostasis. Thromb Haemost 2001;85:958.
3. Girolami A, Vicarioto M, Ruzza G, Cappellato G, Vergolani A. Factor X Padua: A 'new' congenital factor X abnormality with a defect only in the extrinsic system. Acta Haematol 1985;73:31.
4. Girolami A, Molaro G, Lazzarin M, Scarpa R, Brunetti A. A "new" congenital haemorrhagic condition due to the presence of an abnormal factor X (factor X Friuli): Study of a large kindred. Br J Haematol 1970;19:179.
5. Simioni P, Vianello F, Kalafatis M, et al. A dysfunctional factor X (factor X San Giovanni Rotondo) present at homozygous and double heterozygous level: Identification of a novel microdeletion (delC556) and missense mutation (Lys(408)→Asn) in the factor X gene. A study of an Italian family. Thromb Res 2001;101:219.
6. Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227:680.
7. James HL, Girolami A, Fair DS. Molecular defect in coagulation factor X Friuli results from a substitution of serine for proline at position 343. Blood 1991;77:317.
8. Vianello F, Lombardi AM, Dal Bello F, Zanon E, Cabrio L, Girolami A. Conformation sensitive gel electrophoresis for a simple and accurate detection of factor X mutations. Thromb Res 2002;107:51.
9. Guex N, Peitsch MC. SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling. Electrophoresis 1997;18:14.
10. Venkateswaren D, Perera L, Darden T, Pedersen LG. Structure and dynamics of zymogen human blood coagulation factor X. Biophys J 2002;82:1190.
11. 2+-binding site in the serine protease domain of human factor VIIa and its role in tissue factor binding and development of catalytic activity. J Biol Chem 1995;270:15523.
12. 2+ binding site yet retains function. J Biol Chem 1994;269:21495.
13. Watzke HH, Lechner K, Roberts HR, et al. Molecular defect (Gla+14→Lys) and its functional consequences in a hereditary factor X deficiency (factor X "Vorarlberg"). J Biol Chem 1990;265:11982.
14. red FX deficiency. Thromb Haemost 2002; 88:236.
15. Cooper DN, Millar DS, Wacey A, Pemberton S, Tuddenham EG. Inherited factor X deficiency: Molecular genetics and pathophysiology. Thromb Haemost 1997;78:161.