Alterations of fibrin network structure mediated by dermatan sulfate
Dermatan sulfate (DS) is well-known for its anticoagulant activity through binding to heparin cofactor II (HCII) to enhance thrombin inhibition. It has also been reported that DS has a profibrinolytic effect. We have evaluated the effects of DS solutions (4-20 μg/mL) on the formation (by kinetic stu...
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todo:paper_09295305_v35_n2_p257_Lauricella2023-10-03T15:47:34Z Alterations of fibrin network structure mediated by dermatan sulfate Lauricella, A.M. Castañon, M.M. Kordich, L.C. Quintana, I.L. Compaction Dermatan sulfate Fibrin formation Fibrin network structure Fibrinolysis dermatan sulfate fibrin fibrinogen urokinase article centrifugation controlled study drug determination drug effect fibrin clot human in vitro study lysis optical density priority journal protein blood level protein polymerization protein structure scanning electron microscopy structure activity relation Animals Anticoagulants Cattle Dermatan Sulfate Fibrin Protein Binding Dermatan sulfate (DS) is well-known for its anticoagulant activity through binding to heparin cofactor II (HCII) to enhance thrombin inhibition. It has also been reported that DS has a profibrinolytic effect. We have evaluated the effects of DS solutions (4-20 μg/mL) on the formation (by kinetic studies), structure (by electron microscopy and compaction assays) and lysis (with urokinase-type plasminogen activator) of plasma fibrin networks. The results showed that DS significantly prolonged the lag phase and decreased the fibrin formation rate and the optical density of the final networks versus control, in a concentration dependent way. DS-associated networks presented a minor network percentage compared with control, composed of lower number of fibers per field, which resulted significantly thinner and longer. Moreover, DS rendered gels more sensible to rupture by centrifugal force and more susceptible to lysis. When fibrin formation kinetic assays were performed with purified fibrinogen instead of plasma, in the absence of HCII, the optical density of final DS-associated networks was statistically lower than control. Therefore, a direct effect of DS on the thickness of fibers was observed. Since in all in vitro assays low DS concentrations were used, it could be postulated that the fibrin features described above are plausible to be found in in vivo thrombi and therefore, DS would contribute to the formation of less thrombogenic clots. © 2012 Springer Science+Business Media, LLC. Fil:Lauricella, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Castañon, M.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Kordich, L.C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Quintana, I.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_09295305_v35_n2_p257_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 |
Compaction Dermatan sulfate Fibrin formation Fibrin network structure Fibrinolysis dermatan sulfate fibrin fibrinogen urokinase article centrifugation controlled study drug determination drug effect fibrin clot human in vitro study lysis optical density priority journal protein blood level protein polymerization protein structure scanning electron microscopy structure activity relation Animals Anticoagulants Cattle Dermatan Sulfate Fibrin Protein Binding |
| spellingShingle |
Compaction Dermatan sulfate Fibrin formation Fibrin network structure Fibrinolysis dermatan sulfate fibrin fibrinogen urokinase article centrifugation controlled study drug determination drug effect fibrin clot human in vitro study lysis optical density priority journal protein blood level protein polymerization protein structure scanning electron microscopy structure activity relation Animals Anticoagulants Cattle Dermatan Sulfate Fibrin Protein Binding Lauricella, A.M. Castañon, M.M. Kordich, L.C. Quintana, I.L. Alterations of fibrin network structure mediated by dermatan sulfate |
| topic_facet |
Compaction Dermatan sulfate Fibrin formation Fibrin network structure Fibrinolysis dermatan sulfate fibrin fibrinogen urokinase article centrifugation controlled study drug determination drug effect fibrin clot human in vitro study lysis optical density priority journal protein blood level protein polymerization protein structure scanning electron microscopy structure activity relation Animals Anticoagulants Cattle Dermatan Sulfate Fibrin Protein Binding |
| description |
Dermatan sulfate (DS) is well-known for its anticoagulant activity through binding to heparin cofactor II (HCII) to enhance thrombin inhibition. It has also been reported that DS has a profibrinolytic effect. We have evaluated the effects of DS solutions (4-20 μg/mL) on the formation (by kinetic studies), structure (by electron microscopy and compaction assays) and lysis (with urokinase-type plasminogen activator) of plasma fibrin networks. The results showed that DS significantly prolonged the lag phase and decreased the fibrin formation rate and the optical density of the final networks versus control, in a concentration dependent way. DS-associated networks presented a minor network percentage compared with control, composed of lower number of fibers per field, which resulted significantly thinner and longer. Moreover, DS rendered gels more sensible to rupture by centrifugal force and more susceptible to lysis. When fibrin formation kinetic assays were performed with purified fibrinogen instead of plasma, in the absence of HCII, the optical density of final DS-associated networks was statistically lower than control. Therefore, a direct effect of DS on the thickness of fibers was observed. Since in all in vitro assays low DS concentrations were used, it could be postulated that the fibrin features described above are plausible to be found in in vivo thrombi and therefore, DS would contribute to the formation of less thrombogenic clots. © 2012 Springer Science+Business Media, LLC. |
| format |
JOUR |
| author |
Lauricella, A.M. Castañon, M.M. Kordich, L.C. Quintana, I.L. |
| author_facet |
Lauricella, A.M. Castañon, M.M. Kordich, L.C. Quintana, I.L. |
| author_sort |
Lauricella, A.M. |
| title |
Alterations of fibrin network structure mediated by dermatan sulfate |
| title_short |
Alterations of fibrin network structure mediated by dermatan sulfate |
| title_full |
Alterations of fibrin network structure mediated by dermatan sulfate |
| title_fullStr |
Alterations of fibrin network structure mediated by dermatan sulfate |
| title_full_unstemmed |
Alterations of fibrin network structure mediated by dermatan sulfate |
| title_sort |
alterations of fibrin network structure mediated by dermatan sulfate |
| url |
http://hdl.handle.net/20.500.12110/paper_09295305_v35_n2_p257_Lauricella |
| work_keys_str_mv |
AT lauricellaam alterationsoffibrinnetworkstructuremediatedbydermatansulfate AT castanonmm alterationsoffibrinnetworkstructuremediatedbydermatansulfate AT kordichlc alterationsoffibrinnetworkstructuremediatedbydermatansulfate AT quintanail alterationsoffibrinnetworkstructuremediatedbydermatansulfate |
| _version_ |
1807315667971473408 |