Variation of factor VII 140s and 170s loops in fishes: Evolutionary aspects and comparison with mutations found in FVII deficiency

Thrombosis and Haemostasis

Volumn 90, Issue 6, 2003, Pages 1220-1222

  Freguia, Christian Furlan ^b   Toso, Raffaella ^b   Ferraresi, Paolo ^b   Pinotti, Mirko ^b   Bernardi, Francesco ^a  

^a UNIVERSITY OF FERRARA   (Italy)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

BLOOD CLOTTING FACTOR 7;

AMINO ACID SEQUENCE; BLOOD CLOTTING FACTOR 7 DEFICIENCY; COMPARATIVE STUDY; CONTROLLED STUDY; EVOLUTION; FISH; GENE AMPLIFICATION; GENE MUTATION; GENETIC VARIABILITY; GOLDFISH; HUMAN; LETTER; NONHUMAN; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; PUFFER FISH; SEQUENCE ANALYSIS; SPECIES COMPARISON; TROUT; ZEBRA FISH;

EID: 0346272806     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1055/s-0037-1613429     Document Type: Letter

References (17)

1. Davie EW, Fujikawa K, Kiesel W. The coagulation cascade: Initiation, maintenance, and regulation. Biochemistry 1991; 30: 10363-70.
2. Pike ACW, Brzozowsk AM, Roberts SM, et al. Structure of human factor VIIa and its implications for the triggering of blood coagulation. Proc Natl Acad Sci USA 1999; 96: 8925-30.
3. Kemall-Cook G, Johnson DJL, Tuddenham EGD, et al. Crystal structure of active site-inhibited human coagulation Factor VII (des-Gla). J Struct Biol 1999; 127: 213-23.
4. Bodi A, Kaslik G, Venekei I, et al. Structural determinants of the half-life and cleavage site preference in the autolytic inactivation of chymotrypsin. Eur J Biochem 2001; 268: 6238-46.
5. Jin J, Perera L, Stafford D, et al. Four loops of the catalytic domain of factor VIIa mediate the effect of the first EGF-like domain substitution on factor VIIa catalytic activity. J Mol Biol 2001; 307: 1068-79.
6. Greer J. Comparative modelling methods: Application to the family of the mammalian serine protease. Proteins 1990; 7: 317-34.
7. Sheehan J, Templer M, Gregory M, et al. Demonstration of the extrinsic coagulation pathway in teleostei: Identification of zebrafish coagulation factor VII. Proc Natl Acad Sci USA 2001; 98: 8768-73.
8. Davidson CL, Hirt RP, Lal K, et al. Molecular evolution of the vertebrate blood coagulation network. Thromb Haemost 2003; 89: 420-8.
9. Hanumanthaiah R, Day K, Jagadeeswaran P. Comprehensive analysis of blood coagulation pathways in teleostei: Evolution of coagulation factor genes and identification of zebrafish factor VIII. Blood Cells Mol Dis 2002; 29: 57-68.
10. Nelson JP. Fishes of the World, 3rd Edition. John Wiley & Sons, Inc., New York; 1994.
11. Thompson JD, Higgins DG, Gibson TJ. Clustal W. Improving sequence alignment through sequence weighting; Position-specific gap penalties and weight matrix choice. Nucleic Acids Res 1994; 22: 4673-80.
12. Felsenstein J. PHYLIP (Phylogeny Inference Package) Version 3.5c. Distributed by the author. Department of Genetics, University of Washington, Seattle, 1993.
13. Felsenstein J. PHYLIP, Phylogeny Inference Package (Version 3.2). Cladistics 1989; 5: 164-6.
14. Ruf W. Factor VIIa residue Arg290 is required for efficient activation of the macromolecular substrate factor X. Biochemistry 1994; 33: 11631-36.
15. Toso R, Pinotti M, High KA, et al. A frequent human coagulation factor VII mutation (A294V, c152) in loop 140s affects the interaction with activators, tissue factor and substrate. Biochem J 2002; 363: 411-6.
16. Soejima K, Mizuguchi J, Yuguchi M, et al. Factor VIIa modified in the 170 loops shows enhanced catalytic activity but does not change the zymogen-like property. J Biol Chem 2001; 276: 17229-35.
17. McVey JH, Boswell E, Mumford AD, et al. Factor VII deficiency and the FVII mutation database. Hum Mutat 2001; 17: 3-17.