Fibrinogen Matsumoto V: a Variant with Aα19 Arg → Gly (AGG → GGG)

 

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Summary

Fibrinogen Matsumoto V (M-V) is a dysfibrinogen identified in a 52-year-old woman with systemic lupus erythematous. The triplet AGG encoding the amino acid residue Aα19 was replaced by GGG, resulting in the substitution of Arg→Gly. Residue Aα19 has been shown to be one of the most important amino acids in the so-called ‘A’ site or α-chain knob. The thrombin-catalyzed release of fibrinopeptide A from M-V fibrinogen was only slightly delayed yet release of fibrinopeptide B was significantly delayed. Both thrombin-catalyzed fibrin polymerization and fibrin monomer polymerization were markedly impaired compared to normal fibrinogen. In addition, reptilase-catalyzed fibrin polymerization of M-V was much more impaired than thrombin-catalyzed fibrin polymerization. These results indicate ‘B’ and/or ‘b’ site of M-V fibrinogen play a more important role in thrombin- catalyzed fibrin polymerization than that of normal control fibrinogen.

• References

• 1 Pratt KP, Côté HCF, Chung DW, Stenkamp RE, Davie EW. The primary fibrin polymerization pocket: Three-dimensional structure of a 30-kDa C-terminal 7 chain fragment complexed with the peptide Gly-Pro-Arg-Pro. Proc Natl Acad Sci USA 1997; 94: 7176-81.
  CrossrefPubMedGoogle Scholar
• 2 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.
  CrossrefPubMedGoogle Scholar
• 3 Everse SJ, Spraggon G, Veerapandian L, Riley M, Doolittle RF. Crystal structure of fragment Double-D from human fibrin with two different bound ligands. Biochemistry 1998; 37: 8637-42.
  CrossrefPubMedGoogle Scholar
• 4 Laudano AP, Doolittle RF. Synthetic peptide derivatives that bind to fibrinogen and prevent the polymerization fibrin monomers. Proc Natl Acad Sci USA 1978; 75: 3085-9.
  CrossrefPubMedGoogle Scholar
• 5 Laudano AP, Doolittle RF. Studies on synthetic peptides that bind to fibrinogen and prevent fibrin polymerization. Structural requirements, number of binding sites, and species differences. Biochemistry 1980; 19: 1013-9.
  CrossrefPubMedGoogle Scholar
• 6 Blombäck B, Hessel B, Fields R, Procyk R. Fibrinogen Aarhus: an abnormal fibrinogen with Aα19 Arg→Gly substitution. In Fibrinogen 3. Biochemistry, biological functions, gene regulation and expression. Mosesson MW, Amrani DL, Siebenlist KR, DiOrio JP. eds Elsevier Science Publishers BV; Amsterdam: 1988: 263-6.
  Google Scholar
• 7 Dempfle C-EH, Henschen A. Fibrinogen Mannheim I – Identification of an Aα19 Arg→Gly substitution in dysfibrinogenaemia associated with bleeding tendency. In Fibrinogen 4. Current basic and clinical aspects. Matsuda M, Iwanaga S, Takada A, Henschen A. eds Elsevier Science Publishers BV; Amsterdam; 1990: 159-66.
  Google Scholar
• 8 Yamaguchi S, Sugo T, Hashimoto Y, Kimura K, Okajima K, Matsuda M. Fibrinogen Kumamoto with an Aα Arg-19 to Gly substitution has reduced affinity for thrombin possible relevance to thrombosis. Jap J Thromb Haemost 1997; 8: 382-92.
  PubMedGoogle Scholar
• 9 Brennan SO, Ridgway H, Stormorken H, Brosstad F, George PM. Characterisation of fibrinogen Oslo IV by electrospray mass spectrometry. Thromb Haemost 1997; 77: 1040-1.
  Article in Thieme ConnectPubMedGoogle Scholar
• 10 Bolliger-Stucki B, Bucciarelli P, Lämmle B, Furlan M. Fibrinogen Milano XIII (Aα19 Arg→Gly): a dysfunctional variant with an amino acid substitution in the N-terminal polymerization site. Thromb Res 1999; 96: 399-405.
  CrossrefPubMedGoogle Scholar
• 11 Kudryk B, Blombäck B, Blombäck M. Fibrinogen Detroit – an abnormal fibrinogen with non-functional NH₂-terminal polymerization domain. Thromb Res 1976; 9: 25-36.
  CrossrefPubMedGoogle Scholar
• 12 Southan C, Henschen A, Lottspeich F. The search for molecular defects in abnormal fibrinogens. In Fibrinogen. Recent biochemical and medical aspects. Henschen A, Graeff H, Lottspeich F. eds Walter de Gruyter; Berlin: 1982: 153-66.
  Google Scholar
• 13 Wada Y, Niwa K, Maekawa H, Asakura S, Sugo T, Nakamikawa M, Auerswald G, Popp M, Matsuda M. A new type of congenital dysfibrinogen, fibrinogen Bremen, with an Aα Gly-17 to Val substitution associated with hemorrhagic diathesis and delayed would healing. Thromb Haemost 1993; 70: 397-403.
  Article in Thieme ConnectPubMedGoogle Scholar
• 14 Uotani C, Miyata T, Kumabashiri I, Asakura H, Saito M, Matsuda T, Kajiyama S, Iwanaga S. Fibrinogen Kanazawa: a congenital dysfibrinogenaemia with delayed polymerization having a replacement of proline-18 by leucine in the Aα-chain. Blood Coagulation Fibrinolysis 1991; 2: 413-7.
  CrossrefPubMedGoogle Scholar
• 15 Yoshida N, Okuma M, Hirata H, Matsuda M, Yamazumi K, Asakura S. Fibrinogen Kyoto II, a new congenitally abnormal molecule, characterized by the replacement of Aα proline-18 by leucine. Blood 1991; 78: 149-53.
  PubMedGoogle Scholar
• 16 Brennan SO, Hammonds B, George PM. Aberrant hepatic processing causes removal of activation peptide and primary polymerisation site from fibrinogen Canterbury (Aα20 Va→Asp). J Clin Invest 1995; 96: 2854-58.
  CrossrefPubMedGoogle Scholar
• 17 Okumura N, Furihata K, Terasawa F, Nakagoshi R, Ueno I, Katsuyama T. Fibrinogen Matsumoto I; a γ364 Asp→His (GAT→CAT) substitution associated with defective fibrin polymerization. Thromb Haemost 1996; 75: 887-91.
  Article in Thieme ConnectPubMedGoogle Scholar
• 18 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.
  CrossrefPubMedGoogle Scholar
• 19 Terasawa F, Okumura N, Higuchi Y, Ishikawa S, Tozuka M, Ishida F, Kitano K, Katsuyama T. Fibrinogen Matsumoto III: a variant with γ-275 Arg→Cys (CGC→TGC) -Comaparison of fibrin polymerization properties with those of Matsumoto I (γ364 Asp→His) and Matsumoto II (γ308 Asn→Lys). Thromb Haemost 1999; 81: 763-6.
  Article in Thieme ConnectPubMedGoogle Scholar
• 20 Takebe M, Soe G, Kohno I, Sugo T, Matsuda M. Calcium ion-dependent monoclonal antibody against human fibrinogen; preparation, characterization, and application to fibrinogen purification. Thromb Haemost 1995; 73: 662-7.
  Article in Thieme ConnectPubMedGoogle Scholar
• 21 Mihalyi E. Physiological studies of bovine fibrinogen. IV. ultraviolet absorption and its relation to the structure of the molecule. Biochemistry 1968; 7: 208-23.
  CrossrefPubMedGoogle Scholar
• 22 Terasawa F, Okumura N, Kitano K, Hayashida N, Shimosaka M, Okazaki M, Lord ST. 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.
  PubMedGoogle Scholar
• 23 Lord ST, Strickland E, Jayjock E. Strategy for recombinant multichain protein synthesis: Fibrinogen Bβ-chain variant as a thrombin substrates. Biochemistry 1996; 35: 2342-8.
  CrossrefPubMedGoogle Scholar
• 24 Ng AS, Lewis SD, Shafer JA. Quantifying thrombin-catalyzed release of fibrinopeptides from fibrinogen using high-performance liquid chromatography. Methods Enzymol 1993; 222: 341-58.
  PubMedGoogle Scholar
• 25 Chung DW, Harris JE, Davie EW. Nucleotide sequences of the three genes coding for human fibrinogen. In; Fibrinogen, thrombosis, coagulation and fibrinolysis. Liu CY, Chien S. eds Plenum Press; New York: 1990: 39-48.
  Google Scholar
• 26 Hessel B, Stenbjerg S, Dyr J, Kudryk B, Therkildsen L, Blombäck B. Fibrinogen Aarhus – A new case of dysfibrinogenemia. Thromb Res 1986; 42: 21-37.
  CrossrefPubMedGoogle Scholar
• 27 Blombäck B, Hessel B, Hogg D, Therkildsen L. A two-step fibrinogenfibrin transition in blood coagulation. Nature 1978; 275: 501-5.
  CrossrefPubMedGoogle Scholar
• 28 Higgins DL, Lewis SD, Shafer JA. Steady state kinetic parameters for the thrombin-catalyzed conversion of human fibrinogen to fibrin. J Biol Chem 1983; 258: 9276-82.
  PubMedGoogle Scholar
• 29 Nossel HL, Hurlet-Jensen A, Liu CY, Koehn JA, Canfield RE. Fibrinopeptide release from fibrinogen. Ann NY Acad Sci 1983; 408: 269-78.
  CrossrefPubMedGoogle Scholar
• 30 Weisel JW, Veklich Y, Gorkun O. The sequence of cleavage of fibrinopeptides from fibrinogen is important for protofibril formation and enhancement of lateral aggregation in fibrin clots. J Mol Biol 1993; 232: 285-97.
  CrossrefPubMedGoogle Scholar
• 31 Shainoff JR, Dardik BN. Fibrinopeptide B in fibrin assembly and metabolism; physiologic significance in delayed release of the peptide. Ann NY Acad Sci 1983; 408: 254-68.
  CrossrefPubMedGoogle Scholar
• 32 Hasegawa N, Sasaki S. Location of the binding site “b” for lateral polymerization of fibrin. Thromb Res 1990; 57: 183-95.
  CrossrefPubMedGoogle Scholar
• 33 Cierniewski CS, Budzynski AZ. Involvement of the a chain in fibrin clot formation. Effect of monoclonal antibodies. Biochemistry 1992; 31: 4248-53.
  CrossrefPubMedGoogle Scholar
• 34 Gorkun OV, Veklich YI, Medved LV, Henschen AH, Weisel JW. Role of the αC domains of fibrin in clot formation. Biochemistry 1994; 33: 6986-97.
  CrossrefPubMedGoogle Scholar
• 35 Gorkun OV, Henschen-Edman AH, Ping LF, Lord ST. Analysis of Aα251 fibrinogen: The αC domain has a role in polymerization, albeit more subtle than anticipated from the analogous proteolytic fragment X. Biochemistry 1998; 37: 15434-41.
  CrossrefPubMedGoogle Scholar
• 36 Okada M, Blombäck B. Calcium and fibrin gel structure. Thromb Res 1983; 29: 269-80.
  CrossrefPubMedGoogle Scholar
• 37 Carr ME, Gabriel DA, McDonagh J. Influence of Ca²⁺ on the structure of reptilase-derived and thrombin-derived fibrin gels. Biochem J 1986; 239: 513-6.
  CrossrefPubMedGoogle Scholar
• 38 Mihalyi E. Clotting of bovine fibrinogen. Kinetic analysis of the release of fibrinopeptides by thrombin and of the calcium uptake upon clotting at high fibrinogen concentrations. Biochemistry 1988; 7: 976-82.
  PubMedGoogle Scholar
• 39 Müller MF, Ris H, Ferry JD. Electron microscopy of fine fibrin clots and fine and corse fibrin films. J Mol Biol 1984; 174: 369-84.
  CrossrefPubMedGoogle Scholar
• 40 Bale MD, Müller MF, Ferry JD. Rheological studies of creep and creep recovery of unligated fibrin clots; Comparison of clots prepared with thrombin and ancrod. Biopolymers 1985; 24: 461-82.
  CrossrefPubMedGoogle Scholar
• 41 Müller MF, Ferry JD. Stress relaxation in fine fibrin films: Comparison of films prepared with thrombin and ancrod. Biopolymers 1984; 23: 2311-23.
  CrossrefPubMedGoogle Scholar
• 42 Everse SJ, Spraggon G, Veerapandian L, Riley M, Doolittle RF. Conformational changes in fragments D and double-D from human fibrin(ogen) upon binding the peptide ligand Gly-His-Arg-Pro-amide. Biochemistry 1999; 38: 2941-6.
  CrossrefPubMedGoogle Scholar
• 43 Furlan M, Rupp C, Beck EA, Svendsen L. Effect of calcium and synthetic peptides on fibrin polymerization. Thromb Haemost 1982; 47: 118-21.
  Article in Thieme ConnectPubMedGoogle Scholar