메뉴 건너뛰기




Volumn 76, Issue 3, 1996, Pages 377-383

Normal binding of calcium to five fibrinogen variants with mutations in the carboxy terminal part of the γ-chain

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; FIBRINOGEN; FIBRINOGEN VARIANT; FIBRINOPEPTIDE; THROMBIN;

EID: 0029808926     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1055/s-0038-1650587     Document Type: Article
Times cited : (9)

References (42)
  • 2
    • 0018126726 scopus 로고
    • Calcium binding to human fibrinogen localization of two calcium specific sites
    • Lindsey GG, Brown G, Purves LR. Calcium binding to human fibrinogen localization of two calcium specific sites. Thromb Res 1978; 13: 345-50.
    • (1978) Thromb Res , vol.13 , pp. 345-350
    • Lindsey, G.G.1    Brown, G.2    Purves, L.R.3
  • 3
    • 0019487683 scopus 로고
    • Recalculation of calcium-binding properties of human and rat fibrin(ogen) and their degradation products
    • Nieuwenhuizen W, van Ruijven-Vermeer AM, Nooijen WJ, Vermond A, Haverkate F. Recalculation of calcium-binding properties of human and rat fibrin(ogen) and their degradation products. Thromb Res 1981; 22: 653-7.
    • (1981) Thromb Res , vol.22 , pp. 653-657
    • Nieuwenhuizen, W.1    Van Ruijven-Vermeer, A.M.2    Nooijen, W.J.3    Vermond, A.4    Haverkate, F.5
  • 4
    • 0020050917 scopus 로고
    • Potential role of the Aα chain in the binding of calcium to human fibrinogen
    • Marguerie G, Ardaillou N. Potential role of the Aα chain in the binding of calcium to human fibrinogen. Biochim Biophys Acta 1982; 701: 410-2.
    • (1982) Biochim Biophys Acta , vol.701 , pp. 410-412
    • Marguerie, G.1    Ardaillou, N.2
  • 5
    • 0020521569 scopus 로고
    • Evidence for the localization of a calcium-binding site in the amino-terminal disulphide knot of fibrin(ogen)
    • Nieuwenhuizen W, Vermond A, Hermans J. Evidence for the localization of a calcium-binding site in the amino-terminal disulphide knot of fibrin(ogen).Thromb Res 1983; 31: 81-6.
    • (1983) Thromb Res , vol.31 , pp. 81-86
    • Nieuwenhuizen, W.1    Vermond, A.2    Hermans, J.3
  • 6
    • 0018341686 scopus 로고
    • Calcium-binding properties of human fibrin(ogen) and degradation products
    • Nieuwenhuizen W, Vermond A, Nooijen WJ, Haverkate F. Calcium-binding properties of human fibrin(ogen) and degradation products. FEBS Lett 1979; 98: 257-9.
    • (1979) FEBS Lett , vol.98 , pp. 257-259
    • Nieuwenhuizen, W.1    Vermond, A.2    Nooijen, W.J.3    Haverkate, F.4
  • 7
    • 0024443424 scopus 로고
    • Fibrinogen sialic acid residues are low affinity calcium-binding sites that influence fibrin assembly
    • Dang CV, Shin CK, Bell WR, Nagaswami C, Weisel JW. Fibrinogen sialic acid residues are low affinity calcium-binding sites that influence fibrin assembly. J Biol Chem 1989; 264: 15104-8.
    • (1989) J Biol Chem , vol.264 , pp. 15104-15108
    • Dang, C.V.1    Shin, C.K.2    Bell, W.R.3    Nagaswami, C.4    Weisel, J.W.5
  • 8
    • 0023752048 scopus 로고
    • Deglycosylation of fibrinogen accelerates polymerization and increases lateral aggregation of fibrin fibers
    • Langer BG, Weisel JW, Dinauer PA, Nagaswami C, Bell WR. Deglycosylation of fibrinogen accelerates polymerization and increases lateral aggregation of fibrin fibers. J Biol Chem 1988; 263: 15056-63.
    • (1988) J Biol Chem , vol.263 , pp. 15056-15063
    • Langer, B.G.1    Weisel, J.W.2    Dinauer, P.A.3    Nagaswami, C.4    Bell, W.R.5
  • 9
    • 0027248850 scopus 로고
    • Sialic acid in fibrinogen. Effects of sialic acid on fibrinogen-fibrin conversion by thrombin and properties of asialofibrin clot
    • Okude M, Yamanaka A, Morimoto Y, Akihama S. Sialic acid in fibrinogen. Effects of sialic acid on fibrinogen-fibrin conversion by thrombin and properties of asialofibrin clot. Biol Pharm Bull 1993; 16: 448-52.
    • (1993) Biol Pharm Bull , vol.16 , pp. 448-452
    • Okude, M.1    Yamanaka, A.2    Morimoto, Y.3    Akihama, S.4
  • 10
    • 0022263169 scopus 로고
    • Localization of a fibrinogen calcium binding site between γ-subunit positions 311 and 336 by terbium fluorescence
    • Dang CV, Ebert RF, Bell WR. Localization of a fibrinogen calcium binding site between γ-subunit positions 311 and 336 by terbium fluorescence. J Biol Chem 1985; 260: 9713-9.
    • (1985) J Biol Chem , vol.260 , pp. 9713-9719
    • Dang, C.V.1    Ebert, R.F.2    Bell, W.R.3
  • 11
    • 0026576175 scopus 로고
    • Photoaffmity labeling of the primary fibrin polymerization site: Isolation and characterization of a labeled cyanogen bromide fragment corresponding to 7-chain residues 337-379
    • Shimizu A, Nagel GM, Doolittle RF. Photoaffmity labeling of the primary fibrin polymerization site: Isolation and characterization of a labeled cyanogen bromide fragment corresponding to 7-chain residues 337-379. Proc Natl Acad Sci USA 1992; 89: 2888-92.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 2888-2892
    • Shimizu, A.1    Nagel, G.M.2    Doolittle, R.F.3
  • 12
    • 0022481417 scopus 로고
    • Characterization of fibrinogen Milano I: Amino acid exchange γ 330 Asp → Val impairs fibrin polymerization
    • Reber P, Furlan M, Rupp C, Kehl A, Henschen A, Mannucci PM, Beck EA. Characterization of fibrinogen Milano I: amino acid exchange γ 330 Asp → Val impairs fibrin polymerization. Blood 1986; 67: 1751-6.
    • (1986) Blood , vol.67 , pp. 1751-1756
    • Reber, P.1    Furlan, M.2    Rupp, C.3    Kehl, A.4    Henschen, A.5    Mannucci, P.M.6    Beck, E.A.7
  • 13
    • 0023021611 scopus 로고
    • Three abnormal fibrinogen variants with the same amino acid substitution (γ 275 Arg → His): Fibrinogens Bergamo II, Essen and Perugia
    • Reber P, Furlan M, Henschen A, Kaudewitz H, Barbui T, Hilgard P, Nenci GG, Berrettini M, Beck EA. Three abnormal fibrinogen variants with the same amino acid substitution (γ 275 Arg → His): fibrinogens Bergamo II, Essen and Perugia. Thromb Haemost 1986; 56: 401-6.
    • (1986) Thromb Haemost , vol.56 , pp. 401-406
    • Reber, P.1    Furlan, M.2    Henschen, A.3    Kaudewitz, H.4    Barbui, T.5    Hilgard, P.6    Nenci, G.G.7    Berrettini, M.8    Beck, E.A.9
  • 14
    • 0027482187 scopus 로고
    • Fibrinogen Bern I: Substitution γ 337 Asn → Lys is responsible for defective fibrin monomer polymerization
    • 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.
    • (1993) Blood , vol.82 , pp. 2104-2108
    • Steinmann, C.1    Reber, P.2    Jungo, M.3    Lämmle, B.4    Heinemann, G.5    Wermuth, B.6    Furlan, M.7
  • 17
    • 0030066680 scopus 로고    scopus 로고
    • Fibrinogen Claro - Another dysfunctional fibrinogen variant with γ 275 arginine → histidine substitution
    • Steinmann C, Jungo M, Beck EA, Lämmle B, Furlan M. Fibrinogen Claro - another dysfunctional fibrinogen variant with γ 275 arginine → histidine substitution. Thromb Res 1996; 81: 145-50.
    • (1996) Thromb Res , vol.81 , pp. 145-150
    • Steinmann, C.1    Jungo, M.2    Beck, E.A.3    Lämmle, B.4    Furlan, M.5
  • 18
    • 0020024511 scopus 로고
    • Effect of calcium and synthetic peptides on fibrin polymerization
    • Furlan M, Rupp C, Beck EA, Svendsen L. Effect of calcium and synthetic peptides on fibrin polymerization. Thromb Haemost 1982; 47: 118-21.
    • (1982) Thromb Haemost , vol.47 , pp. 118-121
    • Furlan, M.1    Rupp, C.2    Beck, E.A.3    Svendsen, L.4
  • 19
    • 84969001783 scopus 로고
    • The attractions of proteins for small molecules and ions
    • Scatchard G. The attractions of proteins for small molecules and ions. Ann NY Acad Sci 1949; 51: 660-72.
    • (1949) Ann NY Acad Sci , vol.51 , pp. 660-672
    • Scatchard, G.1
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680-5.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 0017686536 scopus 로고
    • Protective effect of calcium in the plasmin degradation of fibrinogen and fibrin fragments D
    • Haverkate F, Timan G. Protective effect of calcium in the plasmin degradation of fibrinogen and fibrin fragments D. Thromb Res 1977; 10: 803-12.
    • (1977) Thromb Res , vol.10 , pp. 803-812
    • Haverkate, F.1    Timan, G.2
  • 22
    • 0020416055 scopus 로고
    • A fibrinogen fragment D (D intermediate) with calcium binding but without anticlotting properties
    • Nieuwenhuizen W, Voskuilen M, Vermond A, Haverkate F, Hermans J. A fibrinogen fragment D (D intermediate) with calcium binding but without anticlotting properties. Biochim Biophys Acta 1982; 707: 190-2.
    • (1982) Biochim Biophys Acta , vol.707 , pp. 190-192
    • Nieuwenhuizen, W.1    Voskuilen, M.2    Vermond, A.3    Haverkate, F.4    Hermans, J.5
  • 23
    • 0026594383 scopus 로고
    • Photoaffmity labeling of the primary fibrin polymerization site: Localization of the label to 7-chain Tyr-363
    • Yamazumi K, Doolittle RF. Photoaffmity labeling of the primary fibrin polymerization site: localization of the label to 7-chain Tyr-363. Proc Natl Acad Sci USA 1992; 89: 2893-6.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 2893-2896
    • Yamazumi, K.1    Doolittle, R.F.2
  • 24
    • 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, 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.
    • (1991) J Biol Chem , vol.266 , pp. 13456-13461
    • Koopman, J.1    Haverkate, F.2    Briët, E.3    Lord, S.T.4
  • 25
    • 0026802038 scopus 로고
    • Characterization of an abnormal fibrinogen Osaka V with the replacement of γ-arginine 375 by glycine. the lack of high affinity calcium binding to D-domains and the lack of protective effect of calcium on fibrinolysis
    • 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. The lack of high affinity calcium binding to D-domains and the lack of protective effect of calcium on fibrinolysis. J Biol Chem 1992; 267: 2753-9.
    • (1992) J Biol Chem , vol.267 , pp. 2753-2759
    • Yoshida, N.1    Hirata, H.2    Morigami, Y.3    Imaoka, S.4    Matsuda, M.5    Yamazumi, K.6    Asakura, S.7
  • 26
    • 0023731893 scopus 로고
    • Characterization of an apparently lower molecular weight γ-chain variant in fibrinogen Kyoto I. the replacement of γ-asparagine 308 by lysine which causes accelerated cleavage of fragment D1 by plasmin and the generation of a new plasmin cleavage site
    • 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. The replacement of γ-asparagine 308 by lysine which causes accelerated cleavage of fragment D1 by plasmin and the generation of a new plasmin cleavage site. J Biol Chem 1988; 263: 13848-56.
    • (1988) J Biol Chem , vol.263 , pp. 13848-13856
    • Yoshida, N.1    Terukina, S.2    Okuma, M.3    Moroi, M.4    Aoki, N.5    Matsuda, M.6
  • 28
    • 0025239558 scopus 로고
    • Polymerization defect of fibrinogen Baltimore III due to a γ Asn308 → le mutation
    • 308 → [le mutation. Blood 1990; 75: 1659-63.
    • (1990) Blood , vol.75 , pp. 1659-1663
    • Bantia, S.1    Bell, W.R.2    Dang, C.V.3
  • 29
    • 0027055525 scopus 로고
    • A detailed consideration of a principal domain of vertebrate fibrinogen and its relatives
    • Doolittle RF. A detailed consideration of a principal domain of vertebrate fibrinogen and its relatives. Protein Science 1992; 1: 1563-77.
    • (1992) Protein Science , vol.1 , pp. 1563-1577
    • Doolittle, R.F.1
  • 30
    • 0040119537 scopus 로고
    • Evidence for four different polymerization sites involved in human fibrin formation
    • Olexa SA, Budzynski AZ. Evidence for four different polymerization sites involved in human fibrin formation. Proc Natl Acad Sci USA 1980; 77: 1374-8.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 1374-1378
    • Olexa, S.A.1    Budzynski, A.Z.2
  • 31
    • 0029111701 scopus 로고
    • The role of fibrinogen D domain intermolecular association sites in the polymerization of fibrin and fibrinogen Tokyo II (γ 275 Arg → Cys)
    • Mosesson MW, Siebenlist KR, DiOrio JP, Matsuda M, Hainfeld JF, Wall JS. The role of fibrinogen D domain intermolecular association sites in the polymerization of fibrin and fibrinogen Tokyo II (γ 275 Arg → Cys). J Clin Invest 1995; 96: 1053-8.
    • (1995) J Clin Invest , vol.96 , pp. 1053-1058
    • Mosesson, M.W.1    Siebenlist, K.R.2    Diorio, J.P.3    Matsuda, M.4    Hainfeld, J.F.5    Wall, J.S.6
  • 32
    • 0021070892 scopus 로고
    • "Fibrinogen Tokyo II": An abnormal fibrinogen with an impaired polymerization site on the aligned DD domain of fibrin molecules
    • Matsuda M, Baba M, Morimoto K, Nakamikawa C. "Fibrinogen Tokyo II": an abnormal fibrinogen with an impaired polymerization site on the aligned DD domain of fibrin molecules. J Clin Invest 1983; 72: 1034-41.
    • (1983) J Clin Invest , vol.72 , pp. 1034-1041
    • Matsuda, M.1    Baba, M.2    Morimoto, K.3    Nakamikawa, C.4
  • 33
    • 0018800765 scopus 로고
    • 2- bridge within the chain of human fibrinogen
    • 2- bridge within the chain of human fibrinogen. Biochim Biophys Acta 1979; 577: 415-23.
    • (1979) Biochim Biophys Acta , vol.577 , pp. 415-423
    • Lawrie, J.S.1    Kemp, G.2
  • 34
    • 0026440134 scopus 로고
    • Heterozygous abnormal fibrinogen Osaka HI with the replacement of arginine-275 by histidine has an apparently higher molecular weight γ-chain variant
    • Yoshida N, Imaoka S, Hirata H, Matsuda M, Asakura S. Heterozygous abnormal fibrinogen Osaka HI with the replacement of arginine-275 by histidine has an apparently higher molecular weight γ-chain variant. Thromb Haemost 1992; 68: 534-8.
    • (1992) Thromb Haemost , vol.68 , pp. 534-538
    • Yoshida, N.1    Imaoka, S.2    Hirata, H.3    Matsuda, M.4    Asakura, S.5
  • 35
    • 0023755597 scopus 로고
    • Substitution of γ Arg-275 by Cys in an abnormal fibrinogen, "fibrinogen Osaka II", Evidence for a unique solitary cystine structure at the mutation site
    • Terukina S, Matsuda M, Hirata H, Takeda Y, Miyata T, Takao T, Shimonishi Y. Substitution of γ Arg-275 by Cys in an abnormal fibrinogen, "fibrinogen Osaka II", Evidence for a unique solitary cystine structure at the mutation site. J Biol Chem 1988; 263: 13579-87.
    • (1988) J Biol Chem , vol.263 , pp. 13579-13587
    • Terukina, S.1    Matsuda, M.2    Hirata, H.3    Takeda, Y.4    Miyata, T.5    Takao, T.6    Shimonishi, Y.7
  • 36
    • 0023860974 scopus 로고
    • An apparently higher molecular weight γ-chain variant in a new congenital abnormal fibrinogen Tochigi characterized by the replacement of γ arginine-275 by cysteine
    • Yoshida N, Ota K, Moroi M, Matsuda M. An apparently higher molecular weight γ-chain variant in a new congenital abnormal fibrinogen Tochigi characterized by the replacement of γ arginine-275 by cysteine. Blood 1988; 71: 480-7.
    • (1988) Blood , vol.71 , pp. 480-487
    • Yoshida, N.1    Ota, K.2    Moroi, M.3    Matsuda, M.4
  • 37
    • 0024559787 scopus 로고
    • A γ methionine-310 to threonine substitution and consequent N-glycosylation at γ asparagine-308 identified in a congenital dysfibrinogenemia associated with posttraumatic bleeding, fibrinogen Asahi
    • Yamazumi K, Shimura K, Terukina S, Takahashi N, Matsuda M. A γ methionine-310 to threonine substitution and consequent N-glycosylation at γ asparagine-308 identified in a congenital dysfibrinogenemia associated with posttraumatic bleeding, fibrinogen Asahi. J Clin Invest 1989; 83: 1590-7.
    • (1989) J Clin Invest , vol.83 , pp. 1590-1597
    • Yamazumi, K.1    Shimura, K.2    Terukina, S.3    Takahashi, N.4    Matsuda, M.5
  • 39
    • 0024495774 scopus 로고
    • Fibrinogen Nagoya, a replacement of glutamine-329 by arginine in the γ-chain that impairs the polymerization of fibrin monomer
    • Miyata T, Furukawa K, Iwanaga S. Takamatsu J, Saito H. Fibrinogen Nagoya, a replacement of glutamine-329 by arginine in the γ-chain that impairs the polymerization of fibrin monomer. J Biochem 1989; 105: 10-4.
    • (1989) J Biochem , vol.105 , pp. 10-14
    • Miyata, T.1    Furukawa, K.2    Iwanaga, S.3    Takamatsu, J.4    Saito, H.5
  • 40
    • 0024331906 scopus 로고
    • Fibrinogen Kyoto III: A congenital dysfibrinogen with a γ aspartic acid-330 to tyrosine substitution manifesting impaired fibrin monomer polymerization
    • Terukina S, Yamazumi K, Okamoto K, Yamashita H, Ito Y, Matsuda M. Fibrinogen Kyoto III: a congenital dysfibrinogen with a γ aspartic acid-330 to tyrosine substitution manifesting impaired fibrin monomer polymerization. Blood 1989; 74: 2681-7.
    • (1989) Blood , vol.74 , pp. 2681-2687
    • Terukina, S.1    Yamazumi, K.2    Okamoto, K.3    Yamashita, H.4    Ito, Y.5    Matsuda, M.6
  • 41
    • 0013625358 scopus 로고
    • Fibrinogen Bern I: A hereditary fibrinogen variant with defective conformational stabilization by calcium ions
    • Menschen A, Graeff H, Lottspeich F, eds. W de Gruyter, Berlin
    • 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: Fibrinogen: Recent Biochemical and Medical Aspects. Menschen A, Graeff H, Lottspeich F, eds. W de Gruyter, Berlin 1982; pp 167-81.
    • (1982) Fibrinogen: Recent Biochemical and Medical Aspects , pp. 167-181
    • Rupp, C.1    Kuyas, C.2    Häberli, A.3    Furlan, M.4    Perret, B.A.5    Beck, E.A.6
  • 42
    • 0024213684 scopus 로고
    • Normal plasmic cleavage of the γ-chain variant of "fibrinogen Saga" with an Arg-275 to His substitution
    • Yamazumi K, Terukina S, Onohara S, Matsuda M. Normal plasmic cleavage of the γ-chain variant of "fibrinogen Saga" with an Arg-275 to His substitution. Thromb Haemost 1988; 60: 476-80.
    • (1988) Thromb Haemost , vol.60 , pp. 476-480
    • Yamazumi, K.1    Terukina, S.2    Onohara, S.3    Matsuda, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.