LRP-1: A Checkpoint for the Extracellular Matrix Proteolysis

Joint Authors

Etique, Nicolas
Verzeaux, Laurie
Dedieu, Stéphane
Emonard, Hervé

Source

BioMed Research International

Issue

Vol. 2013, Issue 2013 (31 Dec. 2013), pp.1-7, 7 p.

Publisher

Hindawi Publishing Corporation

Publication Date

2013-07-09

Country of Publication

Egypt

No. of Pages

7

Main Subjects

Medicine

Abstract EN

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.

American Psychological Association (APA)

Etique, Nicolas& Verzeaux, Laurie& Dedieu, Stéphane& Emonard, Hervé. 2013. LRP-1: A Checkpoint for the Extracellular Matrix Proteolysis. BioMed Research International،Vol. 2013, no. 2013, pp.1-7.
https://search.emarefa.net/detail/BIM-1003456

Modern Language Association (MLA)

Etique, Nicolas…[et al.]. LRP-1: A Checkpoint for the Extracellular Matrix Proteolysis. BioMed Research International No. 2013 (2013), pp.1-7.
https://search.emarefa.net/detail/BIM-1003456

American Medical Association (AMA)

Etique, Nicolas& Verzeaux, Laurie& Dedieu, Stéphane& Emonard, Hervé. LRP-1: A Checkpoint for the Extracellular Matrix Proteolysis. BioMed Research International. 2013. Vol. 2013, no. 2013, pp.1-7.
https://search.emarefa.net/detail/BIM-1003456

Data Type

Journal Articles

Language

English

Notes

Includes bibliographical references

Record ID

BIM-1003456