The natural occurrence of human fibrinogen variants disrupting inter-chain disulfide bonds (aαcys36gly, aαcys36arg and aαcys45tyr) confirms the role of n-terminal aα disulfide bonds in protein assembly and secretion

Haematologica

Volumn 96, Issue 8, 2011, Pages 1226-1230

  Hanss, Michel ^a,b   Pouymayou, Catherine ^c   Blouch, Marie Thérèse ^d   Lellouche, Franck ^e   Ffrench, Patrick ^a,b   Rousson, Robert ^a   Abgrall, Jean François ^d   Morange, Pierre Emmanuel ^c,f   Quélin, Florence ^g,h   de Mazancourt, Philippe ^g,h  

^a HOSPICES CIVILS DE LYON   (France)

^b EDOUARD HERRIOT HOSPITAL   (France)

^c TIMONE HOSPITAL   (France)

^d BREST UNIVERSITY HOSPITAL   (France)

^e Laboratoire d'Hématologie Bactériologie   (France)

^f AIX MARSEILLE UNIVERSITY   (France)

^g CENTRE HOSPITALIER INTERCOMMUNAL   (France)

^h LABORATOIRE DES SCIENCES DU CLIMAT ET DE L ENVIRONNEMENT   (France)

Author keywords

Assembly; Disulfide bond; Fibrinogen; Secretion

Indexed keywords

ANTIGEN; ARGININE; BLOOD CLOTTING FACTOR; CYSTEINE; DISULFIDE; FIBRINOGEN; GLYCINE; TYROSINE;

ADULT; ALPHA CHAIN; AMINO TERMINAL SEQUENCE; ARTICLE; BETA CHAIN; CASE REPORT; DISULFIDE BOND; FEMALE; FIBRINOGEN BLOOD LEVEL; HETEROZYGOTE; HUMAN; HYPOFIBRINOGENEMIA; IN VIVO STUDY; MALE; MUTATIONAL ANALYSIS; NUCLEOTIDE SEQUENCE; PROTEIN ASSEMBLY; PROTEIN SECRETION; PROTEIN VARIANT; SITE DIRECTED MUTAGENESIS;

ADULT; AMINO ACID SUBSTITUTION; DISULFIDES; FEMALE; FIBRINOGEN; HETEROZYGOTE; HUMANS; MALE; MIDDLE AGED; MODELS, MOLECULAR; MUTATION; POLYMORPHISM, GENETIC; PROTEIN CONFORMATION;

EID: 79961035496     PISSN: 03906078     EISSN: 15928721     Source Type: Journal    
DOI: 10.3324/haematol.2010.029801     Document Type: Article

References (20)

1. Mosesson MW. Fibrinogen and fibrin structure and functions. J Thromb Haemost. 2005;3(8):1894-904.
2. Zhang JZ, Redman C. Fibrinogen assembly and secretion. Role of intrachain disulfide loops. J Biol Chem. 1996;271(47):30083-8.
3. Zhang JZ, Kudryk B, Redman CM. Symmetrical disulfide bonds are not necessary for assembly and secretion of human fibrinogen. J Biol Chem. 1993;268(15): 11278-82.
4. Zhang JZ, Redman CM. Role of interchain disulfide bonds on the assembly and secretion of human fibrinogen. J Biol Chem. 1994;269(1):652-8.
5. Redman CM, Xia H. Fibrinogen biosynthesis. Assembly, intracellular degradation, and association with lipid synthesis and secretion. Ann NY Acad Sci. 2001;936:480-95.
6. Huang S, Cao Z, Davie EW. The role of amino-terminal disulfide bonds in the structure and assembly of human fibrinogen. Biochem Biophys Res Commun. 1993; 190(2):488-95.
7. Platè M, Asselta R, Spena S, Spreafico M, Fagoonee S, Peyvandi F, et al. Congenital hypofibrinogenemia: characterization of two missense mutations affecting fibrinogen assembly and secretion. Blood Cells Mol Dis. 2008;41(3):292-7.
8. Hanss M, Biot F. A database for human fibrinogen variants. Ann NY Acad Sci. 2001; 936:89-90.
9. Kazal LA, Amsel S, Miller OP, Tocantins LM. The preparation and some properties of fibrinogen precipitated from human plasma by glycine. Proc Soc Exp Biol Med. 1963;113: 989-94.
10. Hanss M, Ffrench PO, Mornex JF, Chabuet M, Biot F, De Mazancourt P, et al. Two novel fibrinogen variants found in patients with pulmonary embolism and their families. J Thromb Haemost. 2003;1(6):1251-7.
11. Brennan SO, Fellowes AP, Faed JM, George PM. Hypofibrinogenemia in an individual with 2 coding (gamma82 A>G and Bbeta235 P>L) and 2 noncoding mutations. Blood. 2000;95(5):1709-13.
12. Niwa K, Takebe M, Sugo T, Kawata Y, Mimuro J, Asakura S, et al. A gamma Gly-268 to Glu substitution is responsible for impaired fibrin assembly in a homozygous dysfibrinogen Kurashiki I. Blood. 1996;87 (11):4686-94.
13. Brennan SO, Wyatt JM, Ockelford P, George PM. Defective fibrinogen polymerization associated with a novel γ279 Ala>Asp mutation. Br J Haematol. 2000; 108(2):236-40.
14. Doolittle RF, Yang Z, Mochalkin I. Crystal structure studies on fibrinogen and fibrin. Ann NY Acad Sci. 2001;936:31-43.
15. Sheen CR, Low J, Joseph J, Kotlyar E, George PM, Brennan SO. Fibrinogen Darlinghurst: hypofibrinogenaemia caused by a W253G mutation in the gamma chain in a patient with both bleeding and thrombotic complications. Thromb Haemost. 2006;96(5):685-7.
16. Pechik I, Madrazo J, Mosesson MW, Hernandez I, Gilliland GL, Medved L. Crystal structure of the complex between thrombin and the central E region of fibrin. Proc Natl Acad Sci USA. 2004;101 (9):2718-23.
17. Hanss M, Vergnes C, Rugeri L, Ffrench P, de Mazancourt P. A new electrophoretic variant of fibrinogen associated with venous thromboembolism, fibrinogen Bordeaux A α Arg439>Cys. J Thromb Haemost. 2008; 6(8):1422-4.
18. Asselta R, Duga S, Tenchini ML. The molecular basis of quantitative fibrinogen disorders. J Thromb Haemost. 2006;4 (10):2115-29.
19. Hanss M, Chevreaud C, Ffrench P, Négrier C, de Mazancourt P. Clinical and biological features of 3 cases of hypofibrinogenemia associated with 3 different mutations (γ.Ala341Thr, B β Tyr326Cys and A α Asp 496Asn). Thromb Haemost. 2007;98 (3):689-91.
20. Sheen CR, Brennan SO, Jabado N, George PM. Fibrinogen Montreal: a novel missense mutation (A α D496N) associated with hypofibrinogenaemia. Thromb Haemost. 2006;96(2):231-2.