ADAMTS proteoglycanases in the physiological and pathological central nervous system

ADAMTS-1, -4, -5 and -9 belong to ‘a disintegrin and metalloproteinase with thrombospondin motifs (ADAMTS)’ family and more precisely to the proteoglycanases subgroup based on their common ability to degrade chondroitin sulfate proteoglycans. They have been extensively investigated for their involve...

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Autores: Lemarchant, Sighild, Pruvost, Mathilde, Montaner, Joan, Emery, Evelyne, Vivien, Denis, Kanninen, Katja, Koistinaho, Jari
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2013
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/142783
Acceso en línea:http://hdl.handle.net/10261/142783
Access Level:acceso abierto
Palabra clave:A disintegrin and metalloproteinase with thrombospondin motifs
Stroke
Spinal cord injury
Angiogenesis Neurorepair
Synaptic plasticity Inflammation
Chondroitin sulfate proteoglycans
Proteoglycanases
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spelling ADAMTS proteoglycanases in the physiological and pathological central nervous systemLemarchant, SighildPruvost, MathildeMontaner, JoanEmery, EvelyneVivien, DenisKanninen, KatjaKoistinaho, JariA disintegrin and metalloproteinase with thrombospondin motifsStrokeSpinal cord injuryAngiogenesis NeurorepairSynaptic plasticity InflammationChondroitin sulfate proteoglycansProteoglycanasesADAMTS-1, -4, -5 and -9 belong to ‘a disintegrin and metalloproteinase with thrombospondin motifs (ADAMTS)’ family and more precisely to the proteoglycanases subgroup based on their common ability to degrade chondroitin sulfate proteoglycans. They have been extensively investigated for their involvement in inflammation-induced osteoarthritis, and a growing body of evidence indicates that they may be of key importance in the physiological and pathological central nervous system (CNS). In this review, we discuss the deregulated expression of ADAMTS proteoglycanases during acute CNS injuries, such as stroke and spinal cord injury. Then, we provide new insights on ADAMTS proteoglycanases mediating synaptic plasticity, neurorepair, angiogenesis and inflammation mechanisms. Altogether, this review allows us to propose that ADAMTS proteoglycanases may be original therapeutic targets for CNS injuries.This work was supported by the University of Eastern Finland and the ERANET-Neuron research program ‘ProteA: Proteases before, during and after stroke’, 2012–2015.Peer ReviewedBioMed CentralEuropean CommissionUniversity of Eastern Finland2017201720132017info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionhttp://hdl.handle.net/10261/142783reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Ingléshttp://doi.org/10.1186/1742-2094-10-133Noinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/1427832026-05-22T06:33:51Z
dc.title.none.fl_str_mv ADAMTS proteoglycanases in the physiological and pathological central nervous system
title ADAMTS proteoglycanases in the physiological and pathological central nervous system
spellingShingle ADAMTS proteoglycanases in the physiological and pathological central nervous system
Lemarchant, Sighild
A disintegrin and metalloproteinase with thrombospondin motifs
Stroke
Spinal cord injury
Angiogenesis Neurorepair
Synaptic plasticity Inflammation
Chondroitin sulfate proteoglycans
Proteoglycanases
title_short ADAMTS proteoglycanases in the physiological and pathological central nervous system
title_full ADAMTS proteoglycanases in the physiological and pathological central nervous system
title_fullStr ADAMTS proteoglycanases in the physiological and pathological central nervous system
title_full_unstemmed ADAMTS proteoglycanases in the physiological and pathological central nervous system
title_sort ADAMTS proteoglycanases in the physiological and pathological central nervous system
dc.creator.none.fl_str_mv Lemarchant, Sighild
Pruvost, Mathilde
Montaner, Joan
Emery, Evelyne
Vivien, Denis
Kanninen, Katja
Koistinaho, Jari
author Lemarchant, Sighild
author_facet Lemarchant, Sighild
Pruvost, Mathilde
Montaner, Joan
Emery, Evelyne
Vivien, Denis
Kanninen, Katja
Koistinaho, Jari
author_role author
author2 Pruvost, Mathilde
Montaner, Joan
Emery, Evelyne
Vivien, Denis
Kanninen, Katja
Koistinaho, Jari
author2_role author
author
author
author
author
author
dc.contributor.none.fl_str_mv European Commission
University of Eastern Finland
dc.subject.none.fl_str_mv A disintegrin and metalloproteinase with thrombospondin motifs
Stroke
Spinal cord injury
Angiogenesis Neurorepair
Synaptic plasticity Inflammation
Chondroitin sulfate proteoglycans
Proteoglycanases
topic A disintegrin and metalloproteinase with thrombospondin motifs
Stroke
Spinal cord injury
Angiogenesis Neurorepair
Synaptic plasticity Inflammation
Chondroitin sulfate proteoglycans
Proteoglycanases
description ADAMTS-1, -4, -5 and -9 belong to ‘a disintegrin and metalloproteinase with thrombospondin motifs (ADAMTS)’ family and more precisely to the proteoglycanases subgroup based on their common ability to degrade chondroitin sulfate proteoglycans. They have been extensively investigated for their involvement in inflammation-induced osteoarthritis, and a growing body of evidence indicates that they may be of key importance in the physiological and pathological central nervous system (CNS). In this review, we discuss the deregulated expression of ADAMTS proteoglycanases during acute CNS injuries, such as stroke and spinal cord injury. Then, we provide new insights on ADAMTS proteoglycanases mediating synaptic plasticity, neurorepair, angiogenesis and inflammation mechanisms. Altogether, this review allows us to propose that ADAMTS proteoglycanases may be original therapeutic targets for CNS injuries.
publishDate 2013
dc.date.none.fl_str_mv 2013
2017
2017
2017
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Publisher's version
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/142783
url http://hdl.handle.net/10261/142783
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv http://doi.org/10.1186/1742-2094-10-133
No
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv BioMed Central
publisher.none.fl_str_mv BioMed Central
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15.812429

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