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BioMed Research International
Volume 2013 (2013), Article ID 152163, 7 pages
Review Article

LRP-1: A Checkpoint for the Extracellular Matrix Proteolysis

CNRS FRE 3481 MEDyC (Matrice Extracellulaire et Dynamique Cellulaire), Laboratoire SiRMa (Signalisation et Récepteurs Matriciels), Université de Reims Champagne-Ardenne (URCA), Moulin de la Housse, Bât. 18, Chemin des Rouliers, BP 1039, 51687 Reims Cedex 2, France

Received 15 May 2013; Accepted 20 June 2013

Academic Editor: Davide Vigetti

Copyright © 2013 Nicolas Etique et al. 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.


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.