메뉴 건너뛰기




Volumn 94, Issue 1, 2005, Pages 53-59

In vitro expression demonstrates impaired secretion of the γAsn319, Asp320 deletion variant fibrinogen

Author keywords

chain; Assembly; Dysfibrinogen; Pulse chase analysis; Secretion

Indexed keywords

ASPARAGINE; ASPARTIC ACID; FIBRINOGEN;

EID: 22144452576     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1160/TH05-02-0134     Document Type: Article
Times cited : (8)

References (26)
  • 1
    • 0030199185 scopus 로고    scopus 로고
    • Fibrinogen and fibrin-proteins with complex roles in hemostasis and thrombosis
    • Blomback B. Fibrinogen and fibrin-proteins with complex roles in hemostasis and thrombosis. Thromb Res 1996; 83: 1-75.
    • (1996) Thromb. Res. , vol.83 , pp. 1-75
    • Blomback, B.1
  • 3
    • 0021233991 scopus 로고
    • Fibrinogen precursors. Order of assembly of fibrinogen chains
    • Yu S, Sher B, Kudryk B et al. Fibrinogen precursors. Order of assembly of fibrinogen chains. J Biol Chem 1984; 259: 10574-81.
    • (1984) J. Biol. Chem. , vol.259 , pp. 10574-10581
    • Yu, S.1    Sher, B.2    Kudryk, B.3
  • 4
    • 0027418768 scopus 로고
    • Biosynthesis of human fibrinogen. Subunit interactions and potential intermediates in the assembly
    • Huang S, Mulvihill ER, Farrell DH et al. Biosynthesis of human fibrinogen. Subunit interactions and potential intermediates in the assembly. J Biol Chem 1993; 268: 8919-26.
    • (1993) J. Biol. Chem. , vol.268 , pp. 8919-8926
    • Huang, S.1    Mulvihill, E.R.2    Farrell, D.H.3
  • 5
    • 0029661284 scopus 로고    scopus 로고
    • The role of βγ and αγ complexes in the assembly of human fibrinogen
    • Huang S, Cao Z, Chung DW et al. The role of βγ and αγ complexes in the assembly of human fibrinogen. J Biol Chem 1996; 271: 27942-7.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27942-27947
    • Huang, S.1    Cao, Z.2    Chung, D.W.3
  • 6
    • 0034964312 scopus 로고    scopus 로고
    • Fibrinogen biosynthesis. Assembly, intracellular degradation, and association with lipid synthesis and secretion
    • Redman CM, Xia H. Fibrinogen biosynthesis. Assembly, intracellular degradation, and association with lipid synthesis and secretion. Ann New York Acad Sci USA 2001; 936: 480-95.
    • (2001) Ann. New York Acad. Sci. USA , vol.936 , pp. 480-495
    • Redman, C.M.1    Xia, H.2
  • 7
    • 0037093069 scopus 로고    scopus 로고
    • Analysis of fibrinogen γ-chain truncations shows the C-terminus, particularly γIle387, is essential for assembly and secretion of this multichain protein
    • Okumura N, Terasawa F, Tanaka H et al. Analysis of fibrinogen γ-chain truncations shows the C-terminus, particularly γIle387, is essential for assembly and secretion of this multichain protein. Blood 2002; 99: 3654-60.
    • (2002) Blood , vol.99 , pp. 3654-3660
    • Okumura, N.1    Terasawa, F.2    Tanaka, H.3
  • 8
    • 32644455996 scopus 로고    scopus 로고
    • http://www.geht.org/databaseang/fibrinogen/
  • 9
    • 0035080856 scopus 로고    scopus 로고
    • Hypofibrinogenemia due to novel 316 Asp->Tyr substitution in the fibrinogen Bβ chain
    • Brennan SO, Wyatt JM, May S et al. Hypofibrinogenemia due to novel 316 Asp->Tyr substitution in the fibrinogen Bβ chain. Thromb Haemost 2001; 85: 450-3.
    • (2001) Thromb. Haemost. , vol.85 , pp. 450-453
    • Brennan, S.O.1    Wyatt, J.M.2    May, S.3
  • 10
    • 0032787011 scopus 로고    scopus 로고
    • Hypofibrinogenemia associated with a heterozygous missense mutation γ153Cys to Arg (Matsumoto IV): In vitro expression demonstrates defective secretion of the variant fibrinogen
    • Terasawa F, Okumura N, Kitano K et al. Hypofibrinogenemia associated with a heterozygous missense mutation γ153Cys to Arg (Matsumoto IV): In vitro expression demonstrates defective secretion of the variant fibrinogen. Blood 1999; 94: 4122-31.
    • (1999) Blood , vol.94 , pp. 4122-4131
    • Terasawa, F.1    Okumura, N.2    Kitano, K.3
  • 11
    • 0033882702 scopus 로고    scopus 로고
    • Fibrinogen Brescia. Hepatic endoplasmic reticulum storage and hypofibrinogenemia because of a γ284 Gly->Arg mutation
    • Brennan SO, Wyatt J, Medicina D et al. Fibrinogen Brescia. Hepatic endoplasmic reticulum storage and hypofibrinogenemia because of a γ284 Gly->Arg mutation. Am J Pathol 2000; 157; 189-96.
    • (2000) Am. J. Pathol. , vol.157 , pp. 189-196
    • Brennan, S.O.1    Wyatt, J.2    Medicina, D.3
  • 12
    • 0036707542 scopus 로고    scopus 로고
    • Novel fibrinogen γ375 Arg->Trp mutation (fibrinogen Aguadilla) causes hepatic endoplasmic reticulum storage and hypofibrinogenemia
    • Brennan SO, Maghzal G, Shneider BL et al. Novel fibrinogen γ375 Arg->Trp mutation (fibrinogen Aguadilla) causes hepatic endoplasmic reticulum storage and hypofibrinogenemia. Hepatology 2002; 36; 652-8.
    • (2002) Hepatology , vol.36 , pp. 652-658
    • Brennan, S.O.1    Maghzal, G.2    Shneider, B.L.3
  • 13
    • 0035905578 scopus 로고    scopus 로고
    • γ371 Thr->Ile substitution in the fibrinogen γD domain causes hypofibrinogenaemia
    • Brennan SO, Wyatt JM, Fellowes AP et al. γ371 Thr->Ile substitution in the fibrinogen γD domain causes hypofibrinogenaemia. Biochim Biophys Acta 2001; 1550: 183-8.
    • (2001) Biochim. Biophys. Acta , vol.1550 , pp. 183-188
    • Brennan, S.O.1    Wyatt, J.M.2    Fellowes, A.P.3
  • 14
    • 0038690591 scopus 로고    scopus 로고
    • Familial hypofibrinogenemia associated with heterozygous substitution of a conserved arginine residue; Bβ255 Arg->His (fibrinogen Merivale)
    • Maghzal GJ, Brennan SO, Fellows AP et al. Familial hypofibrinogenemia associated with heterozygous substitution of a conserved arginine residue; Bβ255 Arg->His (fibrinogen Merivale). Biochim Biophys Acta 2003; 1645: 146-51.
    • (2003) Biochim. Biophys. Acta , vol.1645 , pp. 146-151
    • Maghzal, G.J.1    Brennan, S.O.2    Fellows, A.P.3
  • 15
    • 0034651759 scopus 로고    scopus 로고
    • Missense mutations in the β fibrinogen gene cause congenital afibrinogenemia by impairing fibrinogen secretion
    • Duga S, Asselta R, Santagostino E et al. Missense mutations in the β fibrinogen gene cause congenital afibrinogenemia by impairing fibrinogen secretion. Blood 2000; 95: 1336-41.
    • (2000) Blood , vol.95 , pp. 1336-1341
    • Duga, S.1    Asselta, R.2    Santagostino, E.3
  • 16
    • 1642331679 scopus 로고    scopus 로고
    • Congenital afibrinogenemia: Intracellular retention of fibrinogen due to a novel W437G mutation in the fibrinogen Bβ-chain gene
    • Spena S, Asselta O, Duga S et al. Congenital afibrinogenemia: intracellular retention of fibrinogen due to a novel W437G mutation in the fibrinogen Bβ-chain gene. Biochim Biophys Acta 2003; 1639: 87-94.
    • (2003) Biochim. Biophys. Acta , vol.1639 , pp. 87-94
    • Spena, S.1    Asselta, O.2    Duga, S.3
  • 17
    • 0344305469 scopus 로고    scopus 로고
    • Congenital afibrinogenemia: Identification and expression of a missense mutation in FGB impairing fibrinogen secretion
    • Vu D, Bolton-Maggs PHB, Parr JR et al. Congenital afibrinogenemia: identification and expression of a missense mutation in FGB impairing fibrinogen secretion. Blood 2003; 102: 4413-5.
    • (2003) Blood , vol.102 , pp. 4413-4415
    • Vu, D.1    Bolton-Maggs, P.H.B.2    Parr, J.R.3
  • 18
    • 0142060996 scopus 로고    scopus 로고
    • Fibrinogen Otsu I: A γAsn319, γAsp320 deletion dysfibrinogen identified in an asymptomatic pregnant woman
    • Terasawa F, Hogan KA, Kani S et al. Fibrinogen Otsu I: a γAsn319, γAsp320 deletion dysfibrinogen identified in an asymptomatic pregnant woman. Thromb Haemost 2003; 90: 757-8.
    • (2003) Thromb. Haemost. , vol.90 , pp. 757-758
    • Terasawa, F.1    Hogan, K.A.2    Kani, S.3
  • 19
    • 0025816449 scopus 로고
    • A congenitally abnormal fibrinogen (Vlissingen) with a 6-base deletion in the γ-chain gene, causing defective calcium binding and impaired fibrin polymerization
    • Koopman J, Haverkate F, Briet E et al. 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.
    • (1991) J. Biol. Chem. , vol.266 , pp. 13456-13461
    • Koopman, J.1    Haverkate, F.2    Briet, E.3
  • 20
    • 0034625408 scopus 로고    scopus 로고
    • Recombinant fibrinogen Vlissingen/Frankfurt IV. The deletion of residues 319 and 320 from the γ-chain of fibrinogen alters calcium binding, fibrin polymerization, cross-linking, and platelet aggregation
    • Hogan KA, Gorkun OV, Lounes KC et al. Recombinant fibrinogen Vlissingen/Frankfurt IV. The deletion of residues 319 and 320 from the γ-chain of fibrinogen alters calcium binding, fibrin polymerization, cross-linking, and platelet aggregation. J Biol Chem 2000; 275: 17778-85.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17778-17785
    • Hogan, K.A.1    Gorkun, O.V.2    Lounes, K.C.3
  • 21
    • 0029831998 scopus 로고    scopus 로고
    • 308 Asn->Lys (AAT->AAG) mutation associated with bleeding tendency
    • 308 Asn->Lys (AAT->AAG) mutation associated with bleeding tendency. Br J Haematol 1996; 94: 526-8.
    • (1996) Br. J. Haematol. , vol.94 , pp. 526-528
    • Okumura, N.1    Furihata, K.2    Terasawa, F.3
  • 22
    • 0030725658 scopus 로고    scopus 로고
    • Severely impaired polymerization of recombinant fibrinogen γ-364 Asp-> His, the substitution discovered in a heterozygous individual
    • Okumura N, Gorkun OV, Lord ST. Severely impaired polymerization of recombinant fibrinogen γ-364 Asp-> His, the substitution discovered in a heterozygous individual. J Biol Chem 1997; 272: 29596-601.
    • (1997) J. Biol. Chem. , vol.272 , pp. 29596-29601
    • Okumura, N.1    Gorkun, O.V.2    Lord, S.T.3
  • 23
    • 0014223584 scopus 로고
    • Physicochemical studies of bovine fibrinogen. IV. Ultraviolet absorption and its relation to the structure of the molecule
    • Mihalyi E. Physicochemical studies of bovine fibrinogen. IV. Ultraviolet absorption and its relation to the structure of the molecule. Biochemistry 1968; 7: 208-23.
    • (1968) Biochemistry , vol.7 , pp. 208-223
    • Mihalyi, E.1
  • 24
    • 0034116650 scopus 로고    scopus 로고
    • A functional assay suggests that heterodimers exist in two C-terminal γ-chain dysfibrinogens: Matsumoto I and Vlissingen /Frankfurt IV
    • Hogan KA, Lord ST, Okumura N et al. A functional assay suggests that heterodimers exist in two C-terminal γ-chain dysfibrinogens: Matsumoto I and Vlissingen/Frankfurt IV. Thromb Haemost 2000; 83: 592-7.
    • (2000) Thromb. Haemost. , vol.83 , pp. 592-597
    • Hogan, K.A.1    Lord, S.T.2    Okumura, N.3
  • 25
    • 0027505548 scopus 로고
    • Characterization of purified recombinant fibrinogen: Partial phosphorylation of fibrinopeptide A
    • Binnie CG, Hettasch JM, Strickland E et al. Characterization of purified recombinant fibrinogen: Partial phosphorylation of fibrinopeptide A. Biochemistry 1993; 32: 107-13.
    • (1993) Biochemistry , vol.32 , pp. 107-113
    • Binnie, C.G.1    Hettasch, J.M.2    Strickland, E.3
  • 26
    • 13244277924 scopus 로고    scopus 로고
    • Neonatal bleeding and decreased plasma fibrinogen levels in mice modeled after the dysfibrinogen Vlissingen/Frankfurt IV
    • Hogan KA, Merenbloom BK, Kim HS et al. Neonatal bleeding and decreased plasma fibrinogen levels in mice modeled after the dysfibrinogen Vlissingen/Frankfurt IV. J Thromb Haemost 2004; 2: 1484-7.
    • (2004) J. Thromb. Haemost. , vol.2 , pp. 1484-1487
    • Hogan, K.A.1    Merenbloom, B.K.2    Kim, H.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.