LRP-1: a checkpoint for the extracellular matrix proteolysis
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Updated: May 8, 2026

High-throughput Measurement of Plasma Membrane Resealing Efficiency in Mammalian Cells
Published on: January 7, 2019
Nicolas Etique1, Laurie Verzeaux, Stéphane Dedieu
1CNRS FRE 3481 MEDyC (Matrice Extracellulaire et Dynamique Cellulaire), Laboratoire SiRMa (Signalisation et Récepteurs Matriciels), Université de Reims Champagne-Ardenne (URCA), Reims, France.
Abstract:
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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