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Proteolytic Remodeling of the Synaptic Cell Adhesion Molecules (CAMs) by Metzincins in Synaptic Plasticity

Cell adhesion molecules participate in the formation, maturation, function and plasticity of synaptic connections. The growing body of evidence indicates that in the regulation of the synaptic plasticity, in which these molecules play pivotal role, also the proteolytic processes are involved. This r...

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Detalles Bibliográficos
Autores principales: Bajor, Malgorzata, Kaczmarek, Leszek
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer US 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3653053/
https://www.ncbi.nlm.nih.gov/pubmed/23124395
http://dx.doi.org/10.1007/s11064-012-0919-6
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author Bajor, Malgorzata
Kaczmarek, Leszek
author_facet Bajor, Malgorzata
Kaczmarek, Leszek
author_sort Bajor, Malgorzata
collection PubMed
description Cell adhesion molecules participate in the formation, maturation, function and plasticity of synaptic connections. The growing body of evidence indicates that in the regulation of the synaptic plasticity, in which these molecules play pivotal role, also the proteolytic processes are involved. This review focuses on extracellular proteolysis of the cell adhesion molecules by specific subgroup of the matrix metalloproteinases, a disintegrin and metalloproteases and a disintegrin and metalloproteinase with thrombospondin motifs, jointly referred to as metzincins, in driving coordinated synaptic structural and functional modifications underlying synaptic plasticity in the adult brain.
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spelling pubmed-36530532013-05-16 Proteolytic Remodeling of the Synaptic Cell Adhesion Molecules (CAMs) by Metzincins in Synaptic Plasticity Bajor, Malgorzata Kaczmarek, Leszek Neurochem Res Review Cell adhesion molecules participate in the formation, maturation, function and plasticity of synaptic connections. The growing body of evidence indicates that in the regulation of the synaptic plasticity, in which these molecules play pivotal role, also the proteolytic processes are involved. This review focuses on extracellular proteolysis of the cell adhesion molecules by specific subgroup of the matrix metalloproteinases, a disintegrin and metalloproteases and a disintegrin and metalloproteinase with thrombospondin motifs, jointly referred to as metzincins, in driving coordinated synaptic structural and functional modifications underlying synaptic plasticity in the adult brain. Springer US 2012-11-04 2013 /pmc/articles/PMC3653053/ /pubmed/23124395 http://dx.doi.org/10.1007/s11064-012-0919-6 Text en © The Author(s) 2012 https://creativecommons.org/licenses/by/4.0/ This article is distributed under the terms of the Creative Commons Attribution License which permits any use, distribution, and reproduction in any medium, provided the original author(s) and the source are credited.
spellingShingle Review
Bajor, Malgorzata
Kaczmarek, Leszek
Proteolytic Remodeling of the Synaptic Cell Adhesion Molecules (CAMs) by Metzincins in Synaptic Plasticity
title Proteolytic Remodeling of the Synaptic Cell Adhesion Molecules (CAMs) by Metzincins in Synaptic Plasticity
title_full Proteolytic Remodeling of the Synaptic Cell Adhesion Molecules (CAMs) by Metzincins in Synaptic Plasticity
title_fullStr Proteolytic Remodeling of the Synaptic Cell Adhesion Molecules (CAMs) by Metzincins in Synaptic Plasticity
title_full_unstemmed Proteolytic Remodeling of the Synaptic Cell Adhesion Molecules (CAMs) by Metzincins in Synaptic Plasticity
title_short Proteolytic Remodeling of the Synaptic Cell Adhesion Molecules (CAMs) by Metzincins in Synaptic Plasticity
title_sort proteolytic remodeling of the synaptic cell adhesion molecules (cams) by metzincins in synaptic plasticity
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3653053/
https://www.ncbi.nlm.nih.gov/pubmed/23124395
http://dx.doi.org/10.1007/s11064-012-0919-6
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