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...
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todo:paper_09575235_v17_n3_p181_Lauricella2023-10-03T15:52:35Z Influence of homocysteine on fibrin network lysis Lauricella, A.M. Quintana, I. Castañon, M. Sassetti, B. Kordich, L. Fibrin networks Fibrinolysis Homocysteine fibrin homocysteine plasminogen tissue plasminogen activator urokinase amino acid analysis article binding kinetics controlled study electron microscopy fiber fibrin metabolism genetic resistance human human cell hyperhomocysteinemia lysis plasminogen activation priority journal regulatory mechanism thickness vascular disease Blood Coagulation Fibrin Fibrinolysis Homocysteine Humans Microscopy, Electron Plasma Plasmin Plasminogen Activator Inhibitor 1 Plasminogen Activators Plasminogen Inactivators 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. Fil:Lauricella, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Quintana, I. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Castañon, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Sassetti, B. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Kordich, L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_09575235_v17_n3_p181_Lauricella |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Fibrin networks Fibrinolysis Homocysteine fibrin homocysteine plasminogen tissue plasminogen activator urokinase amino acid analysis article binding kinetics controlled study electron microscopy fiber fibrin metabolism genetic resistance human human cell hyperhomocysteinemia lysis plasminogen activation priority journal regulatory mechanism thickness vascular disease Blood Coagulation Fibrin Fibrinolysis Homocysteine Humans Microscopy, Electron Plasma Plasmin Plasminogen Activator Inhibitor 1 Plasminogen Activators Plasminogen Inactivators |
| spellingShingle |
Fibrin networks Fibrinolysis Homocysteine fibrin homocysteine plasminogen tissue plasminogen activator urokinase amino acid analysis article binding kinetics controlled study electron microscopy fiber fibrin metabolism genetic resistance human human cell hyperhomocysteinemia lysis plasminogen activation priority journal regulatory mechanism thickness vascular disease Blood Coagulation Fibrin Fibrinolysis Homocysteine Humans Microscopy, Electron Plasma Plasmin Plasminogen Activator Inhibitor 1 Plasminogen Activators Plasminogen Inactivators Lauricella, A.M. Quintana, I. Castañon, M. Sassetti, B. Kordich, L. Influence of homocysteine on fibrin network lysis |
| topic_facet |
Fibrin networks Fibrinolysis Homocysteine fibrin homocysteine plasminogen tissue plasminogen activator urokinase amino acid analysis article binding kinetics controlled study electron microscopy fiber fibrin metabolism genetic resistance human human cell hyperhomocysteinemia lysis plasminogen activation priority journal regulatory mechanism thickness vascular disease Blood Coagulation Fibrin Fibrinolysis Homocysteine Humans Microscopy, Electron Plasma Plasmin Plasminogen Activator Inhibitor 1 Plasminogen Activators Plasminogen Inactivators |
| description |
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. |
| format |
JOUR |
| author |
Lauricella, A.M. Quintana, I. Castañon, M. Sassetti, B. Kordich, L. |
| author_facet |
Lauricella, A.M. Quintana, I. Castañon, M. Sassetti, B. Kordich, L. |
| author_sort |
Lauricella, A.M. |
| title |
Influence of homocysteine on fibrin network lysis |
| title_short |
Influence of homocysteine on fibrin network lysis |
| title_full |
Influence of homocysteine on fibrin network lysis |
| title_fullStr |
Influence of homocysteine on fibrin network lysis |
| title_full_unstemmed |
Influence of homocysteine on fibrin network lysis |
| title_sort |
influence of homocysteine on fibrin network lysis |
| url |
http://hdl.handle.net/20.500.12110/paper_09575235_v17_n3_p181_Lauricella |
| work_keys_str_mv |
AT lauricellaam influenceofhomocysteineonfibrinnetworklysis AT quintanai influenceofhomocysteineonfibrinnetworklysis AT castanonm influenceofhomocysteineonfibrinnetworklysis AT sassettib influenceofhomocysteineonfibrinnetworklysis AT kordichl influenceofhomocysteineonfibrinnetworklysis |
| _version_ |
1782024026237960192 |