Influence of homocysteine on fibrin network lysis

To elucidate some of the links between homocysteine and vascular disease, we have evaluated the effect of the amino acid on the formation (by kinetics studies), structure (by electron microscopy) and lysis of the fibrin network, using tissue-type plasminogen activator (t-PA) and urokinase-type plasm...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autor principal: Lauricella, A.M
Otros Autores: Quintana, I., Castañon, M., Sassetti, B., Kordich, L.
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: 2006
Acceso en línea:Registro en Scopus
DOI
Handle
Registro en la Biblioteca Digital
Aporte de:Registro referencial: Solicitar el recurso aquí
LEADER 11020caa a22011657a 4500
001 PAPER-7227
003 AR-BaUEN
005 20230518203658.0
008 190411s2006 xx ||||fo|||| 00| 0 eng|d
024 7 |2 scopus  |a 2-s2.0-33645533315 
024 7 |2 cas  |a fibrin, 9001-31-4; homocysteine, 454-28-4, 6027-13-0; plasminogen, 9001-91-6; tissue plasminogen activator, 105913-11-9; urokinase, 139639-24-0; Fibrin, 9001-31-4; Homocysteine, 454-28-4; Plasmin, EC 3.4.21.7; Plasminogen Activator Inhibitor 1; Plasminogen Activators, EC 3.4.21.-; Plasminogen Inactivators 
040 |a Scopus  |b spa  |c AR-BaUEN  |d AR-BaUEN 
030 |a BLFIE 
100 1 |a Lauricella, A.M. 
245 1 0 |a Influence of homocysteine on fibrin network lysis 
260 |c 2006 
270 1 0 |m Lauricella, A.M.; Departamento de Química Biológica, Facultad de Ciencias Exactas Y Naturales, Ciudad Universitaria, (C1428EHA) Buenos Aires, Argentina; email: lht@qb.fcen.uba.ar 
506 |2 openaire  |e Política editorial 
504 |a Bertina, R.M., Molecular risk factor for thrombosis (1999) Thromb Haemost, 82, pp. 601-609 
504 |a Guba, S., Fonseca, V., Fink, L., Hyperhomocysteinemia and thrombosis (1999) Semin Thromb Hemost, 25, pp. 291-309 
504 |a D'Angelo, A., Selhub, J., Homocysteine and thrombotic disease (1997) Blood, 90, pp. 1-11 
504 |a Van Guldener, C., Stehouwer, C., Hyperhomocysteinemia, vascular pathology and endothelial dysfunction (2000) Semin Thromb Hemost, 26, pp. 313-324 
504 |a Welch, G.N., Loscalzo, J., Homocysteine and atherothrombosis (1998) N Engl J Med, 338, pp. 1042-1050 
504 |a Mujumdar, V., Aru, G., Tgagi, S., Induction of oxidative stress by homocyst(e)ine impairs endothelial function (2001) J Cell Biochem, 82, pp. 491-500 
504 |a Coppola, A., Giovanni, D., De Stefano, V., Mancini, F., Cerbone, A., Di Minno, G., Homocysteine, coagulation, platelet function, and thrombosis (2000) Semin Thromb Hemost, 26, pp. 243-254 
504 |a Ueland, M., Homocysteine species as components of plasma redox thiol status (1995) Clin Chem, 41, pp. 340-342 
504 |a Lauricella, A.M., Quintana, I., Kordich, L., Effects of homocysteine thiol group on fibrin networks: Another possible mechanism of harm (2002) Thromb Res, 107, pp. 75-79 
504 |a Sauls, D.L., Wolberg, A.S., Hoffman, M., Elevated plasma homocysteine leads to alterations in fibrin clot structure and stability: Implications for the mechanism of thrombosis in hyperhomocysteinemia (2003) J Thromb Haemost, 1, pp. 300-306 
504 |a Graham, I.M., Daly, L.E., Refsum, H.M., Robinson, K., Brattstrom, L.E., Ueland, P.M., Plasma homocysteine as a risk factor for vascular disease: The European Concerted Action Project (1997) JAMA, 277, pp. 1775-1781 
504 |a Vollset, S.E., Refsum, H., Irgens, L.M., Emblem, B.M., Tverdal, A., Gjessing, H.K., Plasma total homocysteine, pregnancy complications, and adverse pregnancy outcomes: The Hordaland Homocysteine study (2000) Am J Clin Nutr, 71, pp. 962-968 
504 |a Miller, J.W., Homocysteine and Alzheimer's disease (1999) Nutr Rev, 57, pp. 126-129 
504 |a Boushey, C.J., Beresford, S.A.A., Omenn, G.S., Motulsky, A.G., A quantitative assessment of plasma homocysteine as a risk for vascular disease: Probable benefits of increasing folic acid intake (1995) JAMA, 274, pp. 1049-1057 
504 |a Clarke, R., Armitage, J., Vitamin supplements and cardiovascular risk: Review of the randomised trials and homocysteine-lowering vitamin supplements (2000) Semin Thromb Hemost, 26, pp. 341-348 
504 |a Smilde, T., Van Den Berkmortel, F., Boerts, G.H., Wollersheim, H., De Boo, T., Van Langen, Carotid and femoral artery wall thickness in patients at risk for cardiovascular disease, with emphasis on hyperhomocysteinemia (1998) Arterioscler Thromb Vasc Biol, 18, pp. 1958-1963 
504 |a Lambert, J., Van Der Berg, M., Steyn, M., Rauwerda, J.A., Donker, A.J., Stehouwer, C.D., Familial hyperhomocysteinaemia and endothelium-dependent vasodilation and arterial distensibility of large arteries (1999) Cardiovasc Res, 42, pp. 743-751 
504 |a Poddar, R., Sivasubramanian, N., Di Bello, P.M., Robinson, K., Jacobsen, D.W., Homocysteine induces expression and secretion of monocyte chemottractant protein-1 and interleukin-8 in human aortic endothelial cells: Implications for vascular disease (2001) Circulation, 103, pp. 2717-2723 
504 |a Weiss, N., Mechanisms of increased vascular oxidant stress in hiperhomocysteinemia and its impact on endothelial function (2005) Curr Drug Metab, 6, pp. 27-36 
504 |a Weisel, J., Veklich, Y., Collet, J., Francis, C., Structural studies of fibrinolysis by electron and light microscopy (1999) Thromb Haemost, 82, pp. 277-282 
504 |a Meh, D.A., Mosesson, M.W., DiOrio, J.P., Siebenlist, K.R., Hernandez, I., Amrani, D.L., Stojanovich, L., Desintegration and reorganization of fibrin networks during tissue-type plaminogen activator-induced clot lysis (2001) Blood Coagul Fibrinolysis, 12, pp. 627-637 
504 |a Collet, J.P., Park, D., Lesty, C., Soria, J., Soria, C., Montalescot, G., Influence of fibrin network conformation and fibrin fiber diameter on fibrinolysis speed. Dynamic and structural approaches by confocal microscopy (2000) Arterioscler Thromb Vasc Biol, 20, pp. 1354-1361 
504 |a Wu, J.H., Siddiqui, K., Diamond, S., Transport phenomena and clot dissolving therapy: An experimental investigation of diffusion-controlled and permeation-enheanced fibrinolysis (1994) Thromb Haemost, 72, pp. 105-112 
504 |a Kolev, K., Machovich, R., Molecular and cellular modulation of fibrinolysis (2003) Thromb Haemost, 89, pp. 610-621 
504 |a Carr, M.E., Alving, B.M., Effect of fibrin structure on plasmin-mediated dissolution of plasma clots (1995) Blood Coagul Fibrinolysis, 6, pp. 567-573 
504 |a Gabriel, D.A., Muga, K., Boothroyd, E.M., The effect of fibrin structure in fibrinolysis (1992) J Biol Chem, 267, pp. 24259-24263 
504 |a Collet, J.P., Nagaswami, C., Farrell, D.H., Montalescot, G., Weisel, J.W., Influence of gamma' fibrinogen splice variant on fibrin physical properties and fibrinolysis rate (2004) Arterioscler Thromb Vasc Biol, 24, pp. 382-386 
504 |a Siebenlist, K.R., Mosesson, M.W., Hernandez, I., Bush, L.A., Di Cera, E., Shainoff, J.R., Studies on the basis for the properties of fibrin produced from fibrinogen containing gamma' chains (2005) Blood, 106, pp. 2730-2736 
504 |a Siebenlist, K., Meh, D., Mosesson, M., Protransglutaminase (factor XIII) mediated crosslinking of fibrinogen and fibrin (2001) Thromb Haemost, 86, pp. 1221-1228 
504 |a Tofler, G.H., D'Agostino, R.B., Jacques, P.F., Bostom, A.G., Wilson, P.W.F., Lipinska, I., Association between increased homocysteine levels and impaired fibrinolytic potencial: Potencial mechanism for cardiovascular risk (2002) Thromb Haemost, 88, pp. 799-804 
504 |a Hajjar, K.A., Homocysteine induced modulation of tissue of plasminogen activator binding to its endothelial cell membrane receptor (1993) J Clin Invest, 91, pp. 2873-2879 
520 3 |a To elucidate some of the links between homocysteine and vascular disease, we have evaluated the effect of the amino acid on the formation (by kinetics studies), structure (by electron microscopy) and lysis of the fibrin network, using tissue-type plasminogen activator (t-PA) and urokinase-type plasminogen activator (u-PA). We have studied whether homocysteine could alter the activity of the components involved in fibrinolysis (by amidolytic and thrombolytic methods). The results showed that homocysteine-associated networks were more compact and branched than controls (52 ± 6 vs 44 ± 5 fibers/field, P = 0.008), and were formed by shorter and thicker fibers. This clot proved to be more resistant to fibrinolysis with u-PA than control [lysis time 50%: 257 ± 16 (homocysteine) vs 187 ± 6 min (control); P < 0.004], but there were no differences with t-PA. Homocysteine did not affect the biological activities of plasmin, or plasminogen activation by t-PA and u-PA. Defective fibrinolysis with u-PA was therefore associated with homocysteine-fibrin structural alterations rather than the homocysteine effect on the biological activities of the fibrinolytic components evaluated. Results suggest that hyperhomocysteinemic patients could produce tight clots, were more resistant to lysis, and generated a procoagulant environment in situ. We believe that our findings may contribute to understanding the mechanisms involved in the homocysteine harmful effect. © 2006 Lippincott Williams & Wilkins.  |l eng 
593 |a Department of Biological Chemistry, School of Exact and Natural Sciences, Buenos Aires University, Argentina 
593 |a Departamento de Química Biológica, Facultad de Ciencias Exactas Y Naturales, Ciudad Universitaria, (C1428EHA) Buenos Aires, Argentina 
690 1 0 |a FIBRIN NETWORKS 
690 1 0 |a FIBRINOLYSIS 
690 1 0 |a HOMOCYSTEINE 
690 1 0 |a FIBRIN 
690 1 0 |a HOMOCYSTEINE 
690 1 0 |a PLASMINOGEN 
690 1 0 |a TISSUE PLASMINOGEN ACTIVATOR 
690 1 0 |a UROKINASE 
690 1 0 |a AMINO ACID ANALYSIS 
690 1 0 |a ARTICLE 
690 1 0 |a BINDING KINETICS 
690 1 0 |a CONTROLLED STUDY 
690 1 0 |a ELECTRON MICROSCOPY 
690 1 0 |a FIBER 
690 1 0 |a FIBRIN METABOLISM 
690 1 0 |a GENETIC RESISTANCE 
690 1 0 |a HUMAN 
690 1 0 |a HUMAN CELL 
690 1 0 |a HYPERHOMOCYSTEINEMIA 
690 1 0 |a LYSIS 
690 1 0 |a PLASMINOGEN ACTIVATION 
690 1 0 |a PRIORITY JOURNAL 
690 1 0 |a REGULATORY MECHANISM 
690 1 0 |a THICKNESS 
690 1 0 |a VASCULAR DISEASE 
690 1 0 |a BLOOD COAGULATION 
690 1 0 |a FIBRIN 
690 1 0 |a FIBRINOLYSIS 
690 1 0 |a HOMOCYSTEINE 
690 1 0 |a HUMANS 
690 1 0 |a MICROSCOPY, ELECTRON 
690 1 0 |a PLASMA 
690 1 0 |a PLASMIN 
690 1 0 |a PLASMINOGEN ACTIVATOR INHIBITOR 1 
690 1 0 |a PLASMINOGEN ACTIVATORS 
690 1 0 |a PLASMINOGEN INACTIVATORS 
700 1 |a Quintana, I. 
700 1 |a Castañon, M. 
700 1 |a Sassetti, B. 
700 1 |a Kordich, L. 
773 0 |d 2006  |g v. 17  |h pp. 181-186  |k n. 3  |p Blood Coagul. Fibrinolysis  |x 09575235  |t Blood Coagulation and Fibrinolysis 
856 4 1 |u https://www.scopus.com/inward/record.uri?eid=2-s2.0-33645533315&doi=10.1097%2f01.mbc.0000220238.99843.45&partnerID=40&md5=5b236e112db3f6cadf38479da14d38df  |y Registro en Scopus 
856 4 0 |u https://doi.org/10.1097/01.mbc.0000220238.99843.45  |y DOI 
856 4 0 |u https://hdl.handle.net/20.500.12110/paper_09575235_v17_n3_p181_Lauricella  |y Handle 
856 4 0 |u https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09575235_v17_n3_p181_Lauricella  |y Registro en la Biblioteca Digital 
961 |a paper_09575235_v17_n3_p181_Lauricella  |b paper  |c PE 
962 |a info:eu-repo/semantics/article  |a info:ar-repo/semantics/artículo  |b info:eu-repo/semantics/publishedVersion 
999 |c 68180