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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Autores principales:	Lauricella, Ana María, Castañon, María Mercedes, Kordich, Lucía Clelia, Quintana, Irene Luisa
Publicado:	2013
Materias:	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
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09295305_v35_n2_p257_Lauricella http://hdl.handle.net/20.500.12110/paper_09295305_v35_n2_p257_Lauricella
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_09295305_v35_n2_p257_Lauricella
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spelling	paper:paper_09295305_v35_n2_p257_Lauricella2023-06-08T15:52:23Z Alterations of fibrin network structure mediated by dermatan sulfate Lauricella, Ana María Castañon, María Mercedes Kordich, Lucía Clelia Quintana, Irene Luisa 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. 2013 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09295305_v35_n2_p257_Lauricella 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, Ana María Castañon, María Mercedes Kordich, Lucía Clelia Quintana, Irene Luisa 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.
author	Lauricella, Ana María Castañon, María Mercedes Kordich, Lucía Clelia Quintana, Irene Luisa
author_facet	Lauricella, Ana María Castañon, María Mercedes Kordich, Lucía Clelia Quintana, Irene Luisa
author_sort	Lauricella, Ana María
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
publishDate	2013
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09295305_v35_n2_p257_Lauricella http://hdl.handle.net/20.500.12110/paper_09295305_v35_n2_p257_Lauricella
work_keys_str_mv	AT lauricellaanamaria alterationsoffibrinnetworkstructuremediatedbydermatansulfate AT castanonmariamercedes alterationsoffibrinnetworkstructuremediatedbydermatansulfate AT kordichluciaclelia alterationsoffibrinnetworkstructuremediatedbydermatansulfate AT quintanaireneluisa alterationsoffibrinnetworkstructuremediatedbydermatansulfate
_version_	1768544784351232000

Alterations of fibrin network structure mediated by dermatan sulfate

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