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Volumn 89, Issue 1, 2003, Pages 48-52

The circulatory half-lives of α-profibrin and α-fibrin monomer, and comparisons with other fibrin(ogen) derivatives

Author keywords

Clearance; Fibrinogen; Fibrin; Profibrin

Indexed keywords

ALPHA FIBRIN MONOMER; ALPHA PROFIBRIN MONOMER; FIBRIN DERIVATIVE; FIBRIN MONOMER; FIBRINOGEN; FIBRINOPEPTIDE; UNCLASSIFIED DRUG;

EID: 0037250480     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1055/s-0037-1613542     Document Type: Article
Times cited : (12)

References (24)
  • 1
    • 0022000448 scopus 로고
    • Kinetic characterization of a saturable pathway for rapid clearance of circulating fibrin monomer
    • Dardik BN, Shainoff JR. Kinetic characterization of a saturable pathway for rapid clearance of circulating fibrin monomer. Blood 1985; 65: 680-8.
    • (1985) Blood , vol.65 , pp. 680-688
    • Dardik, B.N.1    Shainoff, J.R.2
  • 2
    • 0025240637 scopus 로고
    • Effects of cross-linking on clearance of circulating α-fibrin monomer and its complexes
    • Shainoff JR, Dardik BN. Effects of cross-linking on clearance of circulating α-fibrin monomer and its complexes. J Lab Clin Med 1990; 115: 314-23.
    • (1990) J Lab Clin Med , vol.115 , pp. 314-323
    • Shainoff, J.R.1    Dardik, B.N.2
  • 3
    • 0020171935 scopus 로고
    • Adsorptive endocytosis of fibrin monomer by macrophages: Evidence of a receptor for the amino terminus of the fibrin α-chain
    • Shainoff JR, Gonda SR. Adsorptive endocytosis of fibrin monomer by macrophages: Evidence of a receptor for the amino terminus of the fibrin α-chain. Proc Natl Acad Sci USA 1982; 79: 4565-9.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 4565-4569
    • Shainoff, J.R.1    Gonda, S.R.2
  • 4
    • 0025236602 scopus 로고
    • Characterization of a mode of specific binding of fibrin monomer through its amino-terminal domain by macrophages and macrophage cell-lines
    • Shainoff JR, Stearns DJ, DiBello PM, Hishikawa-Itoh Y. Characterization of a mode of specific binding of fibrin monomer through its amino-terminal domain by macrophages and macrophage cell-lines. Thromb Haemost 1990; 60: 193-203.
    • (1990) Thromb Haemost , vol.63 , pp. 193-203
    • Shainoff, J.R.1    Stearns, D.J.2    DiBello, P.M.3    Hishikawa-Itoh, Y.4
  • 6
    • 0036180151 scopus 로고    scopus 로고
    • Fibrin precursors, intermediaries for hemostasis in the clot war
    • Shainoff JR, DiBello PM. Fibrin precursors, intermediaries for hemostasis in the clot war. Thromb Res 2002; 105: 3-13.
    • (2002) Thromb Res , vol.105 , pp. 3-13
    • Shainoff, J.R.1    DiBello, P.M.2
  • 7
    • 0001156062 scopus 로고
    • Cofibrins and fibrin intermediates as indicators of thrombin activity in vivo
    • Shainoff JR, Page IH. Cofibrins and fibrin intermediates as indicators of thrombin activity in vivo. Circ Res 1960; 8: 1013-22.
    • (1960) Circ Res , vol.8 , pp. 1013-1022
    • Shainoff, J.R.1    Page, I.H.2
  • 8
    • 0001211464 scopus 로고
    • Significance of cryoprofibrin in fibrinogen-fibrin conversion
    • Shainoff JR, Page IH. Significance of cryoprofibrin in fibrinogen-fibrin conversion. J Exp Med 1962; 116: 687-707.
    • (1962) J Exp Med , vol.116 , pp. 687-707
    • Shainoff, J.R.1    Page, I.H.2
  • 9
    • 0037205396 scopus 로고    scopus 로고
    • Allosteric effects potentiating the release of the second fibrinopeptide A from fibrinogen by thrombin
    • Shainoff JR, Smejkal GB, DiBello PM, Sung SS, Bush LA, DiCera E. Allosteric effects potentiating the release of the second fibrinopeptide A from fibrinogen by thrombin. J Biol Chem 2002; 277: 19367-73.
    • (2002) J Biol Chem , vol.277 , pp. 19367-19373
    • Shainoff, J.R.1    Smejkal, G.B.2    DiBello, P.M.3    Sung, S.S.4    Bush, L.A.5    DiCera, E.6
  • 10
    • 0027439793 scopus 로고
    • GPR-phoresis, a novel approach to determining fibrin monomer and other macromolecular derivatives of fibrinogen and fibrin in blood
    • Shainoff JR, Urbanic DA, DiBello PM, Valenzuela V. GPR-phoresis, a novel approach to determining fibrin monomer and other macromolecular derivatives of fibrinogen and fibrin in blood. Blood Coagul Fibrinolysis 1993; 4: 87-92.
    • (1993) Blood Coagul Fibrinolysis , vol.4 , pp. 87-92
    • Shainoff, J.R.1    Urbanic, D.A.2    DiBello, P.M.3    Valenzuela, V.4
  • 11
    • 0029793535 scopus 로고    scopus 로고
    • Isolation and characterization of the fibrin-intermediate arising from cleavage of one fibrinopeptide A from fibrinogen
    • Shainoff JR, Smejkal GB, DiBello PM, Mitkevich OV, Levy PJ, Lill H et al. Isolation and characterization of the fibrin-intermediate arising from cleavage of one fibrinopeptide A from fibrinogen. J Biol Chem 1996; 271: 24129-37.
    • (1996) J Biol Chem , vol.271 , pp. 24129-24137
    • Shainoff, J.R.1    Smejkal, G.B.2    DiBello, P.M.3    Mitkevich, O.V.4    Levy, P.J.5    Lill, H.6
  • 12
    • 0016759666 scopus 로고
    • Cross-linking of fibrinogen and fibrin by fibrin-stabilizing factor
    • Kanaide H, Shainoff JR. Cross-linking of fibrinogen and fibrin by fibrin-stabilizing factor. J Lab Clin Med 1975; 85: 574-97.
    • (1975) J Lab Clin Med , vol.85 , pp. 574-597
    • Kanaide, H.1    Shainoff, J.R.2
  • 13
    • 0002273971 scopus 로고
    • Studies on the metabolism and distribution of fibrinogen in young and older rabbit. II. Results
    • Atencio AC, Reeve EB. Studies on the metabolism and distribution of fibrinogen in young and older rabbit. II. Results. J Lab Clin Med 1965; 66: 20-33.
    • (1965) J Lab Clin Med , vol.66 , pp. 20-33
    • Atencio, A.C.1    Reeve, E.B.2
  • 14
    • 0035940439 scopus 로고    scopus 로고
    • Crystal structure of native chicken fibrinogen at 2.7 A resolution
    • Yang Z, Kollman JM, Pandi L, Doolittle RF. Crystal structure of native chicken fibrinogen at 2.7 A resolution. Biochem 2001, 40: 12515-23.
    • (2001) Biochem , vol.40 , pp. 12515-12523
    • Yang, Z.1    Kollman, J.M.2    Pandi, L.3    Doolittle, R.F.4
  • 15
    • 0032699170 scopus 로고    scopus 로고
    • The use of soluble fibrin in evaluating the acute and chronic hypercoagulable state
    • Dempfle CE. The use of soluble fibrin in evaluating the acute and chronic hypercoagulable state. Thromb Haemost 1999; 82: 673-83.
    • (1999) Thromb Haemost , vol.82 , pp. 673-683
    • Dempfle, C.E.1
  • 16
    • 0027497737 scopus 로고
    • Soluble fibrin as a molecular marker for a pre-thrombotic state: A mini-review
    • Nieuwenhuizen W. Soluble fibrin as a molecular marker for a pre-thrombotic state: A mini-review. Blood Coagul Fibrinolysis 1993; 4: 93-6.
    • (1993) Blood Coagul Fibrinolysis , vol.4 , pp. 93-96
    • Nieuwenhuizen, W.1
  • 17
    • 0015092656 scopus 로고
    • The effect of fibrin-stabilizing factor on the subunit structure of human fibrin
    • Schwartz ML, Pizzo SV, Hill RL, McKee PA. The effect of fibrin-stabilizing factor on the subunit structure of human fibrin. J Clin Invest 1971; 50: 1506-13.
    • (1971) J Clin Invest , vol.50 , pp. 1506-1513
    • Schwartz, M.L.1    Pizzo, S.V.2    Hill, R.L.3    McKee, P.A.4
  • 18
    • 0022481026 scopus 로고
    • Characterization of murine peritoneal macrophage receptors for fibrino(oge) degradation products
    • Rjagopalan S, Pizzo SV. Characterization of murine peritoneal macrophage receptors for fibrino(oge) degradation products. Blood 1986; 67: 1224-8.
    • (1986) Blood , vol.67 , pp. 1224-1228
    • Rjagopalan, S.1    Pizzo, S.V.2
  • 19
    • 0020531697 scopus 로고
    • The clearance of human fibrinogen fragments X and Y in mice: A process mediated by the fragment D receptor
    • Pasqua JJ, Pizzo SV. The clearance of human fibrinogen fragments X and Y in mice: A process mediated by the fragment D receptor. Thromb Haemost 1983; 49: 78-80.
    • (1983) Thromb Haemost , vol.49 , pp. 78-80
    • Pasqua, J.J.1    Pizzo, S.V.2
  • 20
    • 0020585451 scopus 로고
    • The role of ligand-ligand interactions in competition by fibrinogen and fibrin degradation products for fibrinogen binding to human platelets
    • Pasqua JJ, Pizzo SV. The role of ligand-ligand interactions in competition by fibrinogen and fibrin degradation products for fibrinogen binding to human platelets. Biochim Biophys Acta 1983; 757: 282-7.
    • (1983) Biochim Biophys Acta , vol.757 , pp. 282-287
    • Pasqua, J.J.1    Pizzo, S.V.2
  • 21
    • 0020396960 scopus 로고
    • The clearance of human fibrinogen fragments D1, D2, D3 and fibrin fragment D1 dimer in mice
    • Pizzo SV, Pasqua JJ. The clearance of human fibrinogen fragments D1, D2, D3 and fibrin fragment D1 dimer in mice. Biochim Biophys Acta 1982; 718: 177-84.
    • (1982) Biochim Biophys Acta , vol.718 , pp. 177-184
    • Pizzo, S.V.1    Pasqua, J.J.2
  • 22
    • 0016365949 scopus 로고
    • The in vivo behavior of the terminal derivatives of fibrinogen and fibrin cleaved by plasmin
    • Catanzaro A, Edgington TS. The in vivo behavior of the terminal derivatives of fibrinogen and fibrin cleaved by plasmin. J Lab Clin Med 1974; 83: 458-66.
    • (1974) J Lab Clin Med , vol.83 , pp. 458-466
    • Catanzaro, A.1    Edgington, T.S.2
  • 23
    • 0012787713 scopus 로고
    • Survival of fibrinogen degradation products in the circulation after thrombolytic therapy for acute myocardial infarction
    • Brommer EJP, Engbers J, Laarse AVd, Nieuwenhuizen W. Survival of fibrinogen degradation products in the circulation after thrombolytic therapy for acute myocardial infarction. Fibrinolysis 1988; 1: 149-53.
    • (1988) Fibrinolysis , vol.1 , pp. 149-153
    • Brommer, E.J.P.1    Engbers, J.2    Laarse, A.V.3    Nieuwenhuizen, W.4
  • 24
    • 0018357032 scopus 로고
    • Binding phenomena of isolated unique plasmic degradation products of human cross-linked fibrin
    • Olexa SA, Budzynski AZ. Binding phenomena of isolated unique plasmic degradation products of human cross-linked fibrin. J Biol Chem 1979; 254: 4925-32.
    • (1979) J Biol Chem , vol.254 , pp. 4925-4932
    • Olexa, S.A.1    Budzynski, A.Z.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.