A small fraction of dermatan sulfate with significantly increased anticoagulant activity was selected by interaction with the first complement protein

Dermatan sulfate (DS) is a member of the family of structurally complex, sulfated, linear heteropolysaccharides called glycosaminoglycans (GAGs). It has a similar structure to heparin and heparan sulfate (HS), but with acetylgalactosamine replacing glucosamine, and the uronic acid moiety, mainly idu...

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Detalles Bibliográficos
Autor principal: Recondo, Eduardo Francisco
Publicado: 2004
Materias:
AT
C1
DS
GAG
HS
rat
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00493848_v113_n3-4_p243_Calabrese
http://hdl.handle.net/20.500.12110/paper_00493848_v113_n3-4_p243_Calabrese
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spelling paper:paper_00493848_v113_n3-4_p243_Calabrese2023-06-08T15:05:47Z A small fraction of dermatan sulfate with significantly increased anticoagulant activity was selected by interaction with the first complement protein Recondo, Eduardo Francisco antithrombin AT C1 Complement system Con A Concanavalin A Dermatan sulfate DS free Dermatan sulfate free DS GAG glycosaminoglycan Heparin cofactor II HS Molecular interactions the first protein complex of the complement system calcium ion dermatan sulfate fibrinolytic agent heparin cofactor II plasma protein protein complex c1 unclassified drug animal experiment animal model animal tissue anticoagulation article complement system dissolution drug activity drug structure human ionic strength male nonhuman normal human precipitation priority journal rat thrombosis Acetylgalactosamine Animals Anticoagulants Calcium Complement C1 Dermatan Sulfate Fibrinolytic Agents Hexosamines Iduronic Acid Male Osmolar Concentration Precipitation Rats Rats, Wistar Structure-Activity Relationship Sulfates Dermatan sulfate (DS) is a member of the family of structurally complex, sulfated, linear heteropolysaccharides called glycosaminoglycans (GAGs). It has a similar structure to heparin and heparan sulfate (HS), but with acetylgalactosamine replacing glucosamine, and the uronic acid moiety, mainly iduronic, joined 1→3 to the hexosamine. We are studying the relationships between structure and activities of dermatan sulfate, in particular those associated with the thrombin inhibition mediated by heparin cofactor II (HCII). As we have demonstrated with heparin, a small fraction of dermatan sulfate was isolated by precipitation with the first component of the complement system, under very specific conditions of low ionic strength, and the presence of calcium ions. The sulfate content and the anticoagulant activity of the dermatan sulfate fraction isolated in the precipitate were three and four times greater respectively than the starting material. Our in vivo studies showed that this fraction has threefold higher thrombolytic activity than the DS. All these results suggest that this fraction could be used as a therapeutic agent for thrombi dissolution. © 2004 Elsevier Ltd. All rights reserved. Fil:Recondo, E.F. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2004 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00493848_v113_n3-4_p243_Calabrese http://hdl.handle.net/20.500.12110/paper_00493848_v113_n3-4_p243_Calabrese
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic antithrombin
AT
C1
Complement system
Con A
Concanavalin A
Dermatan sulfate
DS
free Dermatan sulfate
free DS
GAG
glycosaminoglycan
Heparin cofactor II
HS
Molecular interactions
the first protein complex of the complement system
calcium ion
dermatan sulfate
fibrinolytic agent
heparin cofactor II
plasma protein
protein complex c1
unclassified drug
animal experiment
animal model
animal tissue
anticoagulation
article
complement system
dissolution
drug activity
drug structure
human
ionic strength
male
nonhuman
normal human
precipitation
priority journal
rat
thrombosis
Acetylgalactosamine
Animals
Anticoagulants
Calcium
Complement C1
Dermatan Sulfate
Fibrinolytic Agents
Hexosamines
Iduronic Acid
Male
Osmolar Concentration
Precipitation
Rats
Rats, Wistar
Structure-Activity Relationship
Sulfates
spellingShingle antithrombin
AT
C1
Complement system
Con A
Concanavalin A
Dermatan sulfate
DS
free Dermatan sulfate
free DS
GAG
glycosaminoglycan
Heparin cofactor II
HS
Molecular interactions
the first protein complex of the complement system
calcium ion
dermatan sulfate
fibrinolytic agent
heparin cofactor II
plasma protein
protein complex c1
unclassified drug
animal experiment
animal model
animal tissue
anticoagulation
article
complement system
dissolution
drug activity
drug structure
human
ionic strength
male
nonhuman
normal human
precipitation
priority journal
rat
thrombosis
Acetylgalactosamine
Animals
Anticoagulants
Calcium
Complement C1
Dermatan Sulfate
Fibrinolytic Agents
Hexosamines
Iduronic Acid
Male
Osmolar Concentration
Precipitation
Rats
Rats, Wistar
Structure-Activity Relationship
Sulfates
Recondo, Eduardo Francisco
A small fraction of dermatan sulfate with significantly increased anticoagulant activity was selected by interaction with the first complement protein
topic_facet antithrombin
AT
C1
Complement system
Con A
Concanavalin A
Dermatan sulfate
DS
free Dermatan sulfate
free DS
GAG
glycosaminoglycan
Heparin cofactor II
HS
Molecular interactions
the first protein complex of the complement system
calcium ion
dermatan sulfate
fibrinolytic agent
heparin cofactor II
plasma protein
protein complex c1
unclassified drug
animal experiment
animal model
animal tissue
anticoagulation
article
complement system
dissolution
drug activity
drug structure
human
ionic strength
male
nonhuman
normal human
precipitation
priority journal
rat
thrombosis
Acetylgalactosamine
Animals
Anticoagulants
Calcium
Complement C1
Dermatan Sulfate
Fibrinolytic Agents
Hexosamines
Iduronic Acid
Male
Osmolar Concentration
Precipitation
Rats
Rats, Wistar
Structure-Activity Relationship
Sulfates
description Dermatan sulfate (DS) is a member of the family of structurally complex, sulfated, linear heteropolysaccharides called glycosaminoglycans (GAGs). It has a similar structure to heparin and heparan sulfate (HS), but with acetylgalactosamine replacing glucosamine, and the uronic acid moiety, mainly iduronic, joined 1→3 to the hexosamine. We are studying the relationships between structure and activities of dermatan sulfate, in particular those associated with the thrombin inhibition mediated by heparin cofactor II (HCII). As we have demonstrated with heparin, a small fraction of dermatan sulfate was isolated by precipitation with the first component of the complement system, under very specific conditions of low ionic strength, and the presence of calcium ions. The sulfate content and the anticoagulant activity of the dermatan sulfate fraction isolated in the precipitate were three and four times greater respectively than the starting material. Our in vivo studies showed that this fraction has threefold higher thrombolytic activity than the DS. All these results suggest that this fraction could be used as a therapeutic agent for thrombi dissolution. © 2004 Elsevier Ltd. All rights reserved.
author Recondo, Eduardo Francisco
author_facet Recondo, Eduardo Francisco
author_sort Recondo, Eduardo Francisco
title A small fraction of dermatan sulfate with significantly increased anticoagulant activity was selected by interaction with the first complement protein
title_short A small fraction of dermatan sulfate with significantly increased anticoagulant activity was selected by interaction with the first complement protein
title_full A small fraction of dermatan sulfate with significantly increased anticoagulant activity was selected by interaction with the first complement protein
title_fullStr A small fraction of dermatan sulfate with significantly increased anticoagulant activity was selected by interaction with the first complement protein
title_full_unstemmed A small fraction of dermatan sulfate with significantly increased anticoagulant activity was selected by interaction with the first complement protein
title_sort small fraction of dermatan sulfate with significantly increased anticoagulant activity was selected by interaction with the first complement protein
publishDate 2004
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00493848_v113_n3-4_p243_Calabrese
http://hdl.handle.net/20.500.12110/paper_00493848_v113_n3-4_p243_Calabrese
work_keys_str_mv AT recondoeduardofrancisco asmallfractionofdermatansulfatewithsignificantlyincreasedanticoagulantactivitywasselectedbyinteractionwiththefirstcomplementprotein
AT recondoeduardofrancisco smallfractionofdermatansulfatewithsignificantlyincreasedanticoagulantactivitywasselectedbyinteractionwiththefirstcomplementprotein
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