Anovel fibrinogen variant (fibrinogen Seoul II; AαGln328Pro) characterized by impaired fibrin α-chain cross-linking

Blood

Volumn 108, Issue 6, 2006, Pages 1919-1924

  Park, Rojin ^b   Doh, Hyun Ju ^b   An, Seong Soo A ^b   Choi, Jong Rak ^b   Chung, Kwang Hoe ^b   Song, Kyung Soon ^a  

^a Yonsei University College of Medicine   (South Korea)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

BLOOD CLOTTING FACTOR 8; CALCIUM; FIBRIN; FIBRINOGEN; GLUTAMINE; POLYMER; THROMBIN; TISSUE PLASMINOGEN ACTIVATOR; BLOOD CLOTTING FACTOR 13A; CROSS LINKING REAGENT; FIBRINOGEN VARIANT; MULTIPROTEIN COMPLEX;

ADULT; ALPHA CHAIN; ARTICLE; CASE REPORT; CORRELATION ANALYSIS; CROSS LINKING; EMERGENCY WARD; GENE MUTATION; HEART INFARCTION; HUMAN; KOREA; MALE; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN PURIFICATION; RECURRENT DISEASE; RELATIVE; SCANNING ELECTRON MICROSCOPY; AFIBRINOGENEMIA; AGED; AMINO ACID SUBSTITUTION; BINDING SITE; BLOOD; BLOOD CLOTTING DISORDER; CHEMISTRY; CHILD; FEMALE; GENETICS; HETEROZYGOTE; IN VITRO STUDY; METABOLISM; MIDDLE AGED; POINT MUTATION;

ADULT; AFIBRINOGENEMIA; AGED; AMINO ACID SUBSTITUTION; BINDING SITES; BLOOD COAGULATION DISORDERS, INHERITED; CHILD; CROSS-LINKING REAGENTS; FACTOR XIIIA; FEMALE; FIBRINOGENS, ABNORMAL; HETEROZYGOTE; HUMANS; MALE; MICROSCOPY, ELECTRON, SCANNING; MIDDLE AGED; MULTIPROTEIN COMPLEXES; POINT MUTATION; TISSUE PLASMINOGEN ACTIVATOR;

EID: 33748685614     PISSN: 00064971     EISSN: 00064971     Source Type: Journal    
DOI: 10.1182/blood-2005-11-007591     Document Type: Article

References (35)

1. Doolittle RF, Spraggon G, Everse SJ. Three-dimensional structural studies on fragments of fibrinogen and fibrin. Curr Opin Struct Biol. 1998;8:792-798.
2. Drury DR, McMaster PD. The liver as the source of fibrinogen. J Exp Med. 1929;50:569-578.
3. Straub PW. A study of fibrinogen production by human liver slices in vitro by an immunoprecipitin method. J Clin Invest. 1963;42:130-136.
4. Mosesson MW. The roles of fibrinogen and fibrin in hemostasis and thrombosis. Semin Hematol. 1992;29:177-188.
5. Doolittle RF. Fibrinogen and fibrin. Annu Rev Biochem. 1984;53:195-229.
6. Tunc S, Maitz MF, Steiner G, Vazquez L, Pham MT, Salzer R. In situ conformational analysis of fibrinogen adsorbed on Si surfaces. Colloids Surf B Biointerfaces. 2005;42:219-225.
7. Weisel JW, Medved L. The structure and function of the αC domains of fibrinogen. Ann N Y Acad Sci. 2001;936:312-327.
8. Weisel JW. Fibrin assembly. Lateral aggregation and the role of the two pairs of fibrinopeptides. Biophys J. 1986;50:1079-1093.
9. Veklich YI, Gorkun OV, Medved LV, Nieuwenhuizen W, Weisel JW. Carboxyl-terminal portions of the α chains of fibrinogen and fibrin: localization by electron microscopy and the effects of isolated αC fragments on polymerization. J Biol Chem. 1993;268:13577-13585.
10. Lorand L. Factor XIII: structure, activation, and interactions with fibrinogen and fibrin. Ann N Y Acad Sci. 2001;936:291-311.
11. Lorand L. Sol Sherry lecture in thrombosis: research on clot stabilization provides clues for improving thrombolytic therapies. Arterioscler Thromb Vasc Biol. 2000;20:2-9.
12. Diagnostica Stago. Databases of fibrinogen variants. http://www.geht.org/ fr/pages/pratique-Base_UK_B.html. Accessed October 10, 2005.
13. Fretto LJ, Ferguson EW, Steinman HM, McKee PA. Localization of the alpha-chain crosslink acceptor sites of human fibrin. J Biol Chem. 1978;253:2184-2195.
14. Lefebvre P, Velasco PT, Dear A, et al. Severe hypodysfibrinogenemia in compound heterozygotes of the fibrinogen AαIVS4+1G → T mutation and an AαGln328 truncation (fibrinogen Keokuk). Blood. 2004;103:2571-2576.
15. Ciulla TA, Sklar RM, Hauser SL. A simple method for DNA purification from peripheral blood. Anal Biochem. 1988;319:537-541.
16. Clauss A. Rapid physiological coagulation method in determination of fibrinogen. Acta Haematol. 1957;17:237-246.
17. Saiki RK, Chang CA, Levenson CH, et al. Diagnosis of sickle cell anemia and beta-thalassemia with enzymatically amplified DNA and non-radioactive allele-specific oligonucleotide probes. N Engl J Med. 1988;319:537-541.
18. Hirota-Kawadobora M, Terasawa F, Yonekawa O, et al. Fibrinogens Kosai and Ogasa: Bβ15Gly → Cys (GGT → TGT) substitution associated with impairment of fibrinopeptide B release and lateral aggregation. J Thromb Haemost. 2003;1:275-283.
19. Weisel JW, Nagaswami C. Computer modeling of fibrin polymerization kinetics correlated with electron microscope and turbidity observations: clot structure and assembly are kinetically controlled. Biophys J. 1992;63:111-128.
20. Cottrell BA, Strong DD, Watt KW, Doolittle RF. Amino acid sequence studies on the α chain of human fibrinogen: exact location of cross-linking acceptor sites. Biochemistry. 1979;18: 5405-5410.
21. Neerman-Arbez M, de Moerloose P, Bridel C, et al. Mutations in the fibrinogen Aα gene account for the majority of cases of congenital afibrinogenemia. Blood. 2000;96:149-152.
22. Neerman-Arbez M, de Moerloose P, Honsberger A, et al. Molecular analysis of the fibrinogen gene cluster in 16 patients with congenital afibrinogenemia: novel truncating mutations in the FGA and FGG genes. Hum Genet. 2001;108:237-240.
23. Yohannan S, Yang D, Faham S, Boulting G, Whitelegge J, Bowie JU. Proline substitutions are not easily accommodated in a membrane protein. J Mol Biol. 2004;341:1-6.
24. Barlow DJ, Thornton JM. Helix geometry in proteins. J Mol Biol. 1988;201:601-619.
25. Chou PY, Fasman GD. Prediction of protein conformation. Biochemistry. 1974;13:222-245.
26. von Heijne G. Proline kinks in transmembrane alpha-helices. J Mol Biol. 1991;218:499-503.
27. Riek RP, Rigoutsos I, Novotny J, Graham RM. Non-alpha-helical elements modulate polytopic membrane protein architecture. J Mol Biol. 2001;306:349-362.
28. Ryan EA, Mockros LF, Weisel JW, Lorand L. Structural origins of fibrin clot rheology. Biophys J. 1999;77:2813-2826.
29. Matsuka YV, Medved LV, Migliorini MM, Ingham KC. Factor XIIIa-catalyzed cross-linking of recombinant alpha C fragments of human fibrinogen. Biochemistry. 1996;35:5810-5816.
30. 4 preferentially into the fibrin(ogen) αC-domains. Biochemistry. 2004;43:10748-10756.
31. Maekawa H, Yamazumi K, Muramatsu S, et al. An Aα Ser-434 to N-glycosylated Asn substitution in a dysfibrinogen, fibrinogen Caracas II, characterized by impaired fibrin gel formation. J Biol Chem. 1991;266:11575-11581.
32. Hamano A, Mimuro J, Aoshima M, et al. Thrombophilic dysfibrinogen Tokyo V with the amino acid substitution of γ Ala327Thr: formation of fragile but fibrinolysis-resistant fibrin clots and its relevance to arterial thromboembolism. Blood. 2004;103:3045-3050.
33. Standeven KF, Grant PJ, Carter AM, Scheiner T, Weise JW, Ariëns RA. Functional analysis of the fibrinogen Aα, the312Ala polymorphism: effects on fibrin structure and function. Circulation. 2003;107:2326-2330.
34. Tsurupa G, Medved L. Identification and characterization of novel tPA- and plasminogen-binding sites within fibrin(ogen) alpha C-domains. Biochemistry. 2001;40:801-808.
35. Doolittle RF. Structural basis of the fibrinogen-fibrin transformation: contributions from X-ray crystallography. Blood Rev. 2003:17;33-41.