메뉴 건너뛰기




Volumn 46, Issue 5, 2009, Pages 379-387

Homocysteine modifies fibrin clot deformability: Another possible explanation of harm

Author keywords

Dynamic rheometry; Homocysteine; Loss modulus; Storage modulus; Viscoelastic properties

Indexed keywords

AMINO ACID; HOMOCYSTEINE;

EID: 72949106293     PISSN: 0006355X     EISSN: None     Source Type: Journal    
DOI: 10.3233/BIR-2009-0459     Document Type: Article
Times cited : (11)

References (29)
  • 1
    • 0037418247 scopus 로고    scopus 로고
    • Atherosclerosis, thrombosis and vascular biology Italian study group, No evidence of association between prothrombotic gene polymorphisms and the development of acute myocardial infarction at a young age
    • Atherosclerosis, thrombosis and vascular biology Italian study group, No evidence of association between prothrombotic gene polymorphisms and the development of acute myocardial infarction at a young age, Circulation 107 (2003), 1117-1122.
    • (2003) Circulation , vol.107 , pp. 1117-1122
  • 2
    • 0032725352 scopus 로고    scopus 로고
    • Molecular risk factor for thrombosis
    • R.M. Bertina, Molecular risk factor for thrombosis, Thromb. Haemost. 82 (1999), 601-609.
    • (1999) Thromb. Haemost. , vol.82 , pp. 601-609
    • Bertina, R.M.1
  • 3
    • 11144242551 scopus 로고    scopus 로고
    • Endothelial dysfunction in patients with recent myocardial infarction and hyperhomocysteinaemia: Effects of vitamin supplementation
    • London
    • S. Chia, R. Wilson, C.A. Ludlam, D.J. Webb, A.D. Flapan and D.E. Newby, Endothelial dysfunction in patients with recent myocardial infarction and hyperhomocysteinaemia: Effects of vitamin supplementation, Clin. Sci. (London) 108 (2005), 65-72.
    • (2005) Clin. Sci. , vol.108 , pp. 65-72
    • Chia, S.1    Wilson, R.2    Ludlam, C.A.3    Webb, D.J.4    Flapan, A.D.5    Newby, D.E.6
  • 4
    • 0002281292 scopus 로고
    • Structural and mechanical properties of biopolymer gels
    • A.H. Clark and S.B. Ross-Murphy, Structural and mechanical properties of biopolymer gels, Adv. Polym. Sci. 83 (1987), 57-192.
    • (1987) Adv. Polym. Sci. , vol.83 , pp. 57-192
    • Clark, A.H.1    Ross-Murphy, S.B.2
  • 6
    • 0030971062 scopus 로고    scopus 로고
    • Homocysteine and thrombotic disease
    • A. D'Angelo and J. Selhub, Homocysteine and thrombotic disease, Blood 90 (1997), 1-11.
    • (1997) Blood , vol.90 , pp. 1-11
    • D'Angelo, A.1    Selhub, J.2
  • 7
    • 0001843265 scopus 로고
    • Viscoelastic properties of food gels
    • M.A. Rao and J.F. Steffe, eds, Elsevier, Oxford
    • J.L. Doublier, B. Launay and G. Cuvelier, Viscoelastic properties of food gels, in: Viscoelastic Properties of Foods, M.A. Rao and J.F. Steffe, eds, Elsevier, Oxford, 1992, pp. 371-434.
    • (1992) Viscoelastic Properties of Foods , pp. 371-434
    • Doublier, J.L.1    Launay, B.2    Cuvelier, G.3
  • 8
    • 22244460811 scopus 로고    scopus 로고
    • Hyperhomocysteinemia, thrombosis and vascular biology
    • L.S. Ebsen, Hyperhomocysteinemia, thrombosis and vascular biology, Cell. Mol. Biol. 50 (2004), 917-930.
    • (2004) Cell. Mol. Biol. , vol.50 , pp. 917-930
    • Ebsen, L.S.1
  • 9
    • 0026645829 scopus 로고
    • Fibrin gel network characteristics and coronary heart disease; Relationship to plasma fibrinogen concentration, acute phase protein, serum lipoproteins and coronary atherosclerosis
    • K. Fatah, A. Hamsten, B. Blombäck and M. Blombäck, Fibrin gel network characteristics and coronary heart disease; relationship to plasma fibrinogen concentration, acute phase protein, serum lipoproteins and coronary atherosclerosis, Thromb. Haemost. 68 (1992), 130-135.
    • (1992) Thromb. Haemost. , vol.68 , pp. 130-135
    • Fatah, K.1    Hamsten, A.2    Blombäck, B.3    Blombäck, M.4
  • 11
    • 0001386179 scopus 로고    scopus 로고
    • Analysis of aggregate structure in food protein gels with the concept of fractal
    • T. Hagiwara, H. Kumagai, T. Matsunaga and K. Nakamura, Analysis of aggregate structure in food protein gels with the concept of fractal, Biosci. Biotech. Biochem. 61 (1997), 1663-1667.
    • (1997) Biosci. Biotech. Biochem. , vol.61 , pp. 1663-1667
    • Hagiwara, T.1    Kumagai, H.2    Matsunaga, T.3    Nakamura, K.4
  • 13
    • 0037101570 scopus 로고    scopus 로고
    • Effects of Homocysteine thiol group on fibrin networks: Another possible mechanism of harm
    • A.M. Lauricella, I. Quintana and L. Kordich, Effects of Homocysteine thiol group on fibrin networks: Another possible mechanism of harm, Thromb. Res. 107 (2002), 75-79.
    • (2002) Thromb. Res. , vol.107 , pp. 75-79
    • Lauricella, A.M.1    Quintana, I.2    Kordich, L.3
  • 14
    • 0042666891 scopus 로고    scopus 로고
    • Effects of homocysteine on L-arginine transport and nitric oxide formation in human platelets
    • DOI 10.1046/j.1365-2362.2003.01203.x
    • G. Leoncini, R. Pascale and M.G. Signorello, Effects of homocysteine on l-arginine transport and nitric oxide formation in human platelets, Eur. J. Clin. Invest. 33 (2003), 713-719. (Pubitemid 36918635)
    • (2003) European Journal of Clinical Investigation , vol.33 , Issue.8 , pp. 713-719
    • Leoncini, G.1    Pascale, R.2    Signorello, M.G.3
  • 15
    • 0022131749 scopus 로고
    • Large deformation and ultimate properties of biopolymer gels: 1. Single biopolymer component systems
    • H. Mc Evoy, S.B. Ross-Murphy and A.H. Clark, Large deformation and ultimate properties of biopolymer gels: 1. Single biopolymer component systems, Polymer 26 (1985), 1483-1492.
    • (1985) Polymer , vol.26 , pp. 1483-1492
    • Mc Evoy, H.1    Ross-Murphy, S.B.2    Clark, A.H.3
  • 16
    • 0034910719 scopus 로고    scopus 로고
    • Induction of oxidative stress by homocyst(e)ine impairs endothelial function
    • V. Mujumdar, G. Aru and S. Tgagi, Induction of oxidative stress by homocyst(e)ine impairs endothelial function, J. Cell Biochem. 82 (2001), 491-500.
    • (2001) J. Cell Biochem. , vol.82 , pp. 491-500
    • Mujumdar, V.1    Aru, G.2    Tgagi, S.3
  • 17
    • 10744223660 scopus 로고    scopus 로고
    • Rheology-structure properties of gellan systems: Evidence of network formation at low gellan concentrations
    • A.I. Rodríguez-Hernández, S. Durand, C. Garnier, A. Tecante and J.L. Doublier, Rheology-structure properties of gellan systems: Evidence of network formation at low gellan concentrations, Food Hydrocoll. 17 (2003), 621-628.
    • (2003) Food Hydrocoll. , vol.17 , pp. 621-628
    • Rodríguez-Hernández, A.I.1    Durand, S.2    Garnier, C.3    Tecante, A.4    Doublier, J.L.5
  • 20
    • 33644553466 scopus 로고    scopus 로고
    • Modification of fibrinogen by homocysteine thiolactone increases resistance to fibrinolysis: A potential mechanism of the thrombotic tendency in hyperhomocysteinemia
    • D.L. Sauls, E. Lockhart, M.E. Warren, A. Lenkowski, S.E. Wilhelm and M. Hoffman, Modification of fibrinogen by homocysteine thiolactone increases resistance to fibrinolysis: A potential mechanism of the thrombotic tendency in hyperhomocysteinemia, Biochemistry 45 (2006), 2480-2487.
    • (2006) Biochemistry , vol.45 , pp. 2480-2487
    • Sauls, D.L.1    Lockhart, E.2    Warren, M.E.3    Lenkowski, A.4    Wilhelm, S.E.5    Hoffman, M.6
  • 21
    • 0141450396 scopus 로고    scopus 로고
    • Elevated plasma Homocysteine leads to alterations in fibrin clot structure and stability: Implications for the mechanism of thrombosis in Hyperhomocysteinemia
    • D.L. Sauls, A.S. Wolberg and M. Hoffman, Elevated plasma Homocysteine leads to alterations in fibrin clot structure and stability: Implications for the mechanism of thrombosis in Hyperhomocysteinemia, J. Thromb. Haemost. 1 (2003), 300-306.
    • (2003) J. Thromb. Haemost. , vol.1 , pp. 300-306
    • Sauls, D.L.1    Wolberg, A.S.2    Hoffman, M.3
  • 22
    • 0027970345 scopus 로고
    • Changes in clot deformability, A possible explanation for the epidemiological association between plasma fibrinogen concentration and myocardial infarction
    • M.C. Scrutton, S.B. Ross-Murphy, G.M. Bennet, Y. Stirling and T.W. Meade, Changes in clot deformability, A possible explanation for the epidemiological association between plasma fibrinogen concentration and myocardial infarction, Blood Coagul. Fibrinol. 5 (1994), 719-723.
    • (1994) Blood Coagul. Fibrinol. , vol.5 , pp. 719-723
    • Scrutton, M.C.1    Ross-Murphy, S.B.2    Bennet, G.M.3    Stirling, Y.4    Meade, T.W.5
  • 23
    • 0001024684 scopus 로고
    • Scaling behavior of the elastic properties of colloidal gels
    • W.H. Shih, W.Y. Shih, K. Seong-Il, L. Jun and I.A. Aksay, Scaling behavior of the elastic properties of colloidal gels, Phys. Rev. A 42 (1990), 4772-4779.
    • (1990) Phys. Rev. A , vol.42 , pp. 4772-4779
    • Shih, W.H.1    Shih, W.Y.2    Seong-Il, K.3    Jun, L.4    Aksay, I.A.5
  • 24
    • 0029257541 scopus 로고
    • Homocysteine species as components of plasma redox thiol status
    • M. Ueland, Homocysteine species as components of plasma redox thiol status, Clin. Chem. 41 (1995), 340-342.
    • (1995) Clin. Chem. , vol.41 , pp. 340-342
    • Ueland, M.1
  • 26
    • 0033817681 scopus 로고    scopus 로고
    • Hyperhomocysteinemia, vascular pathology and endothelial dysfunction
    • C. Van Guldener and C. Stehouwer, Hyperhomocysteinemia, vascular pathology and endothelial dysfunction, Semin. Thromb. Hemost. 26 (2000), 313-324.
    • (2000) Semin. Thromb. Hemost. , vol.26 , pp. 313-324
    • Van Guldener, C.1    Stehouwer, C.2
  • 27
    • 9644260704 scopus 로고    scopus 로고
    • The mechanical properties of fibrin for basic scientists and clinicians
    • J.W. Weisel, The mechanical properties of fibrin for basic scientists and clinicians, Biophys. Chem. 112(2,3) (2004), 267-276.
    • (2004) Biophys. Chem. , vol.112 , Issue.2-3 , pp. 267-276
    • Weisel, J.W.1
  • 28
    • 34250692159 scopus 로고    scopus 로고
    • Structure of fibrin: Impact on clot stability
    • J.W. Weisel, Structure of fibrin: Impact on clot stability, J. Thromb. Haemost. 5(Suppl. 1) (2007), 116-124.
    • (2007) J. Thromb. Haemost. , vol.5 , Issue.SUPPL. 1 , pp. 116-124
    • Weisel, J.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.