Regulation of the composition of the extracellular matrix by low density lipoprotein receptor-related protein-1

doi:10.1074/jbc.M511857200

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Papers In Press, published online ahead of print January 6, 2006
J. Biol. Chem, 10.1074/jbc.M511857200
Submitted on November 3, 2005
Accepted on January 6, 2006

Regulation of the composition of the extracellular matrix by low density lipoprotein receptor-related protein-1

Alban Gaultier, Ana Maria Salicioni, Sanja Arandjelovic, and Steven L. Gonias

Pathology Dept., University of California San Diego, La Jolla, CA 92093

Corresponding Author: sgonias{at}ucsd.edu

Low density lipoprotein receptor-related protein (LRP-1) is a catabolic receptor for extracellular matrix (ECM) structural proteins and for proteins that bind to ECM. LRP-1 also is implicated in integrin maturation. In this study, we applied a proteomics strategy to identify novel proteins involved in ECM modeling that are regulated by LRP-1. We show that LRP-1-deficiency in murine embryonic fibroblasts (MEFs) is associated with increased levels of type III collagen and pigment epithelium-derived factor, which accumulate in the substratum surrounding cells. The collagen receptor, uPAR-AP/Endo-180, is also increased in LRP-1-deficient MEFs. Human LRP-1 reversed the changes in protein expression associated with LRP-1 deficiency; however, the endocytic activity of LRP-1 was not involved. Instead, regulation occurred at the mRNA level. Inhibition of c-Jun amino-terminal kinase (JNK) blocked type III collagen expression in LRP-1-deficient MEFs, suggesting regulation of JNK activity as a mechanism by which LRP-1 controls mRNA expression. The ability of LRP-1 to regulate expression of the factors identified here suggests a role for LRP-1 in determining blood vessel structure and in angiogenesis.

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