Fibrinogen St. Gallen I (γ 292 Gly→Val): Evidence for structural alterations causing defective polymerization and fibrinogenolysis

Thrombosis and Haemostasis

Volumn 81, Issue 2, 1999, Pages 268-274

  Stucki, Bettina ^a   Schmutz, Peter ^a   Schmid, Luzius ^b   Haeberli, André ^a   Lämmle, Bernhard ^a   Furlan, Miha ^a  

^a UNIVERSITY OF BERN   (Switzerland)

^b CANTONAL HOSPITAL ST GALLEN   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

BATROXOBIN; CALCIUM; EDETIC ACID; FIBRIN MONOMER; FIBRINOGEN; FIBRINOPEPTIDE A; FIBRINOPEPTIDE B; GLYCINE; PLASMIN; THROMBIN; VALINE;

ADULT; AMINO ACID SUBSTITUTION; ARTICLE; BINDING SITE; BLOOD CLOTTING TEST; CARBOXY TERMINAL SEQUENCE; CASE REPORT; CONTROLLED STUDY; CRYSTAL STRUCTURE; EXON; FEMALE; FIBRINOGEN BLOOD LEVEL; FIBRINOGEN METABOLISM; FIBRINOGENOLYSIS; GENE MUTATION; GENE SEQUENCE; HUMAN; MOLECULAR MODEL; NUCLEIC ACID BASE SUBSTITUTION; POLYMERIZATION; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN SECRETION; PROTEIN STRUCTURE; THROMBIN TIME;

EID: 0033037749     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1055/s-0037-1614456     Document Type: Article

References (28)

1. Ebert RF. Index of variant human fibrinogens. Boca Raton, Ann Arbor, Boston: CRC Press 1991.
2. Yee VC, Pratt KP, Côté HCF, Le Trong I, Chung DW, Davie EW, Stenkamp RE, Teller DC. Crystal structure of a 30 kDa C-terminal fragment from the γ chain of human fibrinogen. Structure 1997; 5: 125-38.
3. Spraggon G, Everse SJ, Doolittle RF. Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin. Nature 1997; 389: 455-62.
4. Beck EA, Charache P, Jackson DP. A new inherited coagulation disorder caused by an abnormal fibrinogen ("fibrinogen Baltimore"). Nature 1965; 208: 143-5.
5. 292Gly → Val (GGC → GTC) mutation. Blood 1990; 76: 2279-83.
6. Clauss A. Gerinnungsphysiologische Schnellmelhode zur Bestimmung des Fibrinogens. Acta Haematol 1957; 17: 237-46.
7. Schulz FH. Eine einfache Bewertungsmethode von Leberparenchymschäden (volumetrische Fibrinbestimmung). Acta Hepatol 1955; 3: 306-10.
8. Laurell CB. Quantitative estimation of proteins by electrophoresis in agarose gel containing antibodies. Anal Biochem 1966; 15: 45-52.
9. Furlan M, Rupp C, Beck EA, Svendsen L. Effect of calcium and synthetic peptides on fibrin polymerization. Thromb Haemost 1982; 47: 118-21.
10. Bögli C, Hofer A, Baudo F, Redaelli R, Furlan M. Fibrinogen Milano IV, another case of congenital dysfibrinogenemia with an abnormal fibrinopeptide A release (Aα 16 Arg → His). Haemostasis 1992; 22: 7-11.
11. Kehl M, Lottspeich F, Henschen A. Analysis of human fibrinopeptides by high-performance liquid chromatography. Hoppe Seylers Z Physiol Chem 1981; 362: 1661-4.
12. Furlan M, Stucki B, Steinmann C, Jungo M, Lämmle B. Normal binding of calcium to five fibrinogen variants with mutations in the carboxy terminal part of γ-chain. Thromb Haemost 1996; 76: 377-83.
13. Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680-5.
14. Scatchard G. The attractions of proteins for small molecules and ions. Ann NY Acad Sci 1949; 51: 660-72.
15. Steinmann C, Bögli C, Jungo M, Lämmle B, Heinemann G, Wermuth B, Redaelli R, Baudo F, Furlan M. Fibrinogen Milano V: a congenital dysfibrinogenaemia with a γ 275 Arg → Cys substitution. Blood Coag Fibrinol 1994; 5: 463-71.
16. Pratt KP, Côté HCF, Chung DW, Sienkamp RE, Davie EW. The primary fibrin polymerization pocket: Three-dimensional structure of a 30-kDa C-terminal γ chain fragment complexed with the peptide Gly-Pro-Arg-Pro. Proc Natl Acad Sci USA 1997; 94: 7176-81.
17. Menschen A, McDonagh J, Fibrinogen, fibrin and factor XIII. In: Zwaal and Hemker (eds). Blood coagulation. Amsterdam: Elsevier 1986; 171-241.
18. Soria J, Soria C, Samama M, Tabori S, Kehl M, Menschen A, Nieuwenhuizen W, Rimon A, Tatarski I. Fibrinogen Haifa: fibrinogen variant with absence of protective effect of calcium on plasmin degradation of gamma chains. Thromb Haemost 1987; 57: 310-3.
19. Koopman J, Haverkate F, Briët E, Lord ST. A congenitally abnormal fibrinogen (Vlissingen) with a 6-base deletion in the γ-chain gene, causing defective calcium binding and impaired fibrin polymerization. J Biol Chem 1991; 266: 13456-61.
20. Rupp C, Kuyas C, Häberli A, Furlan M, Perret BA, Beck EA. Fibrinogen Bern I: a hereditary fibrinogen variant with defective conformational stabilization by calcium ions. In: Henschen, Graeff and Lottspeich (eds). Fibrinogen - recent biochemical and medical aspects. Berlin, New York: Walter de Gruyter 1982; 167-81.
21. Steinmann C, Reber P, Jungo M, Lämmle B, Heinemann G, Wermuth B, Furlan M. Fibrinogen Bern I: substitution γ 337 Asn → Lys is responsible for defective fibrin monomer polymerization. Blood 1993; 82: 2104-8.
22. Yoshida N, Hirata H, Morigami Y, Imaoka S, Matsuda M, Yamazumi K, Asakura S. Characterization of an abnormal fibrinogen Osaka V with the replacement of γ-arginine 375 by glycine. J Biol Chem 1992; 267: 2753-9.
23. Yoshida N, Terukina S, Okuma M, Moroi M, Aoki N, Matsuda M. Characterization of an apparently lower molecular weight γ-chain variant in fibrinogen Kyoto I. J Biol Chem 1988; 263: 13848-56.
24. Yoshida N, Imaoka S, Hirata H, Matsuda M, Asakura S. Heterozygous abnormal fibrinogen Osaka III with the replacement of γ arginine-275 by histidine has an apparently higher molecular weight γ-chain variant. Thromb Haemost 1992; 68: 534-8.
25. Everse SJ, Spraggon G, Doolittle RF. A three-dimensional consideration of variant human fibrinogens. Thromb Haemost 1998; 80: 1-9.
26. Yamazumi K, Doolittle RF. Photoaffinity labeling of the primary fibrin polymerization site: localization of the label to γ-chain Tyr-363. Proc Natl Acad Sci USA 1992; 89: 2893-6.
27. Shimizu A, Nagel GM, Doolittle RF. Photoaffinity labeling of the primary fibrin-polymerization site: isolation of a cyanogen bromide fragment corresponding to γ-chain residues 337-379. Proc Natl Acad Sci USA 1992; 89: 2888-92.
28. Mosesson MW. Fibrinogen and fibrin polymerization: appraisal of the binding events that accompany fibrin generation and fibrin clot assembly. Blood Coag Fibrinol 1997; 8: 257-67.