Fibrinogens Bern IV, Bern V and Milano XI: Three dysfunctional variants with amino acid substitutions in the thrombin cleavage site of the Aα-chain

Blood Coagulation and Fibrinolysis

Volumn 10, Issue 2, 1999, Pages 93-99

  Stucki, B ^a   Zenhausern R ^a   Biedermann, B ^a   Baudo, F ^b   Redaelli, R ^b   Lammle B ^a   Furlan, Miha ^a  

^a UNIVERSITY OF BERN   (Switzerland)

^b OSPEDALE NIGUARDA CA GRANDA   (Italy)

Author keywords

Albumin; Dysfibrinogen; Fibrinogen variant; Fibrinolysis; Plasminogen; T PA

Indexed keywords

ALBUMIN; FIBRIN; FIBRINOGEN VARIANT; PLASMINOGEN; THROMBIN; TISSUE PLASMINOGEN ACTIVATOR;

AMINO ACID SUBSTITUTION; CASE REPORT; DYSFIBRINOGENEMIA; FIBRINOGEN DEFECT; FIBRINOLYSIS; GENE MUTATION; HEMATOLOGICAL PARAMETERS; HUMAN; NUCLEOTIDE SEQUENCE; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; REVIEW;

EID: 0032967114     PISSN: 09575235     EISSN: None     Source Type: Journal    
DOI: 10.1097/00001721-199903000-00006     Document Type: Review

References (30)

1. 1. Blombäck B, Blombäck M, Edman P, Hessel B. Human fibrinopeptides: isolation, characterization and structure. Biochim Biophys Acta 1966; 115: 371-396.
2. 2. Henschen AH. Human fibrinogen - structural variants and functional sites. Thromb Haemost 1993; 70: 42-47.
3. 3. Stubbs MT, Oschkinat H, Mayr I, Huber R, Angliker H, Stone SR, et al. The interaction of thrombin with fibrinogen. Eur J Biochem 1992; 206: 187-195.
4. 4. Soria J, Soria C, Samama M, Henschen AH, Southan C. Detection of fibrinogen abnormality in dysfibrinogenemia: special report on fibrinogen Metz characterized by an amino acid substitution located at the peptide bond cleaved by thrombin. In: Henschen A, Graeff H, Lottspeich F (editors): Fibrinogen: recent biochemical and medical aspects. Berlin, New York: Walter de Gruyter; 1982. pp. 129-143.
5. 5. Higgins DL, Shafer JA. Fibrinogen Petoskey, a dysfibrinogenemia characterized by replacement of Arg-Aα 16 by a histidyl residue. J Biol Chem 1981; 256: 12013-12017.
6. 6. Koopman J, Haverkate F. Hereditary variants of human fibrinogens. In: Bloom AL, Forbes CD, Thomas DP, Tuddenham EGD (editors): Haemostasis and thrombosis. Edinburgh: Churchill Livingstone; 1994. pp. 515-529.
7. 7. Clauss A. Gerinnungsphysiologische Schnellmethode zur Bestimmung des Fibrinogens. Acta Haematol 1957; 17: 237-246.
8. 8. Schulz FH. Eine einfache Bewertungsmethode von Leberparenchymschäden (volumetrische Fibrinbestimmung). Acta Hepatol 1955; 3: 306-310.
9. 9. Laurell CB. Quantitative estimation of proteins by electrophoresis in agarose gel containing antibodies. Ann Biochem 1966; 15: 45-52.
10. 10. Furlan M, Rupp C, Beck EA, Svendsen L. Effect of calcium and synthetic peptides on fibrin polymerization. Thromb Haemost 1982; 47: 118-121.
11. 11. 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.
12. 12. Kehl M, Lottspeich F, Henschen A. Analysis of human fibrinopeptides by high-performance liquid chromatography. Hoppe Seylers Z Physiol Chem 1981; 362: 1661-1664.
13. 13. Steinmann C, Bögli C, Jungo M, Lämmle B, Heinemann G, Wermuth B, et al. Fibrinogen Milano V: a congenital dysfibrinogenaemia with a γ 275 Arg→Cys substitution. Blood Coag Fibrinol 1994; 5: 463-471.
14. 14. Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680-685.
15. 15. Habeeb AFSA. Reaction of protein sulfhydryl groups with Ellmann's reagent. In: Hirs CHW, Timasheff SN (editors): Methods in enzymology. New York, London: Academic Press; 1972. pp. 457-464.
16. 16. Southan C. The elucidation of molecular defects in congenital dysfibrinogenaemia. In: Francis JL (editor): Fibrinogen, fibrin stabilisation and fibrinolysis. Chichester: Ellis Horwood; 1988. pp. 100-127.
17. 17. Ebert RF. Index of variant human fibrinogens. Boca Raton, Ann Arbor, Boston: CRC Press; 1991.
18. 44→Cys) form disulfide-linked fibrinogen-albumin complexes. Proc Natl Acad Sci USA 1992; 89: 3478-3482.
19. 19. Kamura T, Tsuda H, Yae Y, Hattori S, Ohga S, Shibata Y, et al. An abnormal fibrinogen Fukuoka II (Gly-Bβ15→Cys) characterized by defective fibrin lateral association and mixed disulfide formation. J Biol Chem 1995; 270: 29392-29399.
20. 16→Cys): biochemical and physiologic characterization. Blood 1991; 78: 1744-1752.
21. 21. Galanakis D, Spitzer S, Scharrer I. Unusual Aα16Arg→Cys dysfibrinogenaemic family: absence of normal Aα-chains from two of four heterozygous siblings. Blood Coag Fibrinol 1993; 4: 67-71.
22. 22. Gabriel DA, Muga K, Boothroyd EM. The effect of fibrin structure on fibrinolysis. J Biol Chem 1992; 267: 24259-24263.
23. 23. Verheijen JH, Nieuwenhuizen W, Wijngaards G. Activation of plasminogen by tissue activator is increased specifically in the presence of certain soluble fibrin(ogen) fragments. Thromb Res 1982; 27: 377-385.
24. 24. Norrman B, Wallen P, Ranby M. Fibrinolysis mediated by tissue plasminogen activator. Disclosure of a kinetic transition. Eur J Biochem 1985; 149: 193-200.
25. 25. Suenson E, Lutzen O, Thorsen S. Initial plasmindegradation of fibrin as the basis of a positive feedback mechanism in fibrinolysis. Eur J Biochem 1984; 140: 513-522.
26. 26. Hoylaerts M, Rijken DC, Lijnen HR, Collen D. Kinetics of the activation of plasminogen by human tissue plasminogen activator. Role of fibrin. J Biol Chem 1982; 257: 2912-2919.
27. 27. Nieuwenhuizen W. Sites in fibrin involved in the acceleration of plasminogen activation by t-PA. Possible role of fibrin polymerization. Thromb Res 1994; 75: 343-347.
28. 28. Suenson E, Petersen LC. Fibrin and plasminogen structures essential to stimulation of plasmin formation by tissue-type plasminogen activator. Biochim Biophys Acta 1986; 870: 510-519.
29. 29. Kaczmarek E, Lee MH, McDonagh J. Initial interaction between fibrin and tissue plasminogen activator. J Biol Chem 1993; 268: 2474-2479.
30. 30. Carr ME, Alving BM. Effect of fibrin structure on plasmin mediated dissolution of plasma clots. Blood Coag Fibrinol 1995; 6: 567-573.