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LRP-1: A Checkpoint for the Extracellular Matrix Proteolysis

Low-density lipoprotein receptor-related protein-(LRP-1) is a large endocytic receptor that binds more than 35 ligands and exhibits signaling properties. Proteinases capable of degrading extracellular matrix (ECM), called matrix proteinases in this paper, are mainly serine proteinases: the activator...

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Detalles Bibliográficos
Autores principales: Etique, Nicolas, Verzeaux, Laurie, Dedieu, Stéphane, Emonard, Hervé
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3723059/
https://www.ncbi.nlm.nih.gov/pubmed/23936774
http://dx.doi.org/10.1155/2013/152163
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author Etique, Nicolas
Verzeaux, Laurie
Dedieu, Stéphane
Emonard, Hervé
author_facet Etique, Nicolas
Verzeaux, Laurie
Dedieu, Stéphane
Emonard, Hervé
author_sort Etique, Nicolas
collection PubMed
description Low-density lipoprotein receptor-related protein-(LRP-1) is a large endocytic receptor that binds more than 35 ligands and exhibits signaling properties. Proteinases capable of degrading extracellular matrix (ECM), called matrix proteinases in this paper, are mainly serine proteinases: the activators of plasminogen into plasmin, tissue-type (tPA) and urokinase-type (uPA) plasminogen activators, and the members of the matrix metalloproteinase (MMP) family. LRP-1 is responsible for clearing matrix proteinases, complexed or not with inhibitors. This paper attempts to summarize some aspects on the cellular and molecular bases of endocytic and signaling functions of LRP-1 that modulate extra- and pericellular levels of matrix proteinases.
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spelling pubmed-37230592013-08-09 LRP-1: A Checkpoint for the Extracellular Matrix Proteolysis Etique, Nicolas Verzeaux, Laurie Dedieu, Stéphane Emonard, Hervé Biomed Res Int Review Article Low-density lipoprotein receptor-related protein-(LRP-1) is a large endocytic receptor that binds more than 35 ligands and exhibits signaling properties. Proteinases capable of degrading extracellular matrix (ECM), called matrix proteinases in this paper, are mainly serine proteinases: the activators of plasminogen into plasmin, tissue-type (tPA) and urokinase-type (uPA) plasminogen activators, and the members of the matrix metalloproteinase (MMP) family. LRP-1 is responsible for clearing matrix proteinases, complexed or not with inhibitors. This paper attempts to summarize some aspects on the cellular and molecular bases of endocytic and signaling functions of LRP-1 that modulate extra- and pericellular levels of matrix proteinases. Hindawi Publishing Corporation 2013 2013-07-10 /pmc/articles/PMC3723059/ /pubmed/23936774 http://dx.doi.org/10.1155/2013/152163 Text en Copyright © 2013 Nicolas Etique et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review Article
Etique, Nicolas
Verzeaux, Laurie
Dedieu, Stéphane
Emonard, Hervé
LRP-1: A Checkpoint for the Extracellular Matrix Proteolysis
title LRP-1: A Checkpoint for the Extracellular Matrix Proteolysis
title_full LRP-1: A Checkpoint for the Extracellular Matrix Proteolysis
title_fullStr LRP-1: A Checkpoint for the Extracellular Matrix Proteolysis
title_full_unstemmed LRP-1: A Checkpoint for the Extracellular Matrix Proteolysis
title_short LRP-1: A Checkpoint for the Extracellular Matrix Proteolysis
title_sort lrp-1: a checkpoint for the extracellular matrix proteolysis
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3723059/
https://www.ncbi.nlm.nih.gov/pubmed/23936774
http://dx.doi.org/10.1155/2013/152163
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AT emonardherve lrp1acheckpointfortheextracellularmatrixproteolysis