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M410762200v1
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Papers In Press, published online ahead of print January 27, 2005
J. Biol. Chem, 10.1074/jbc.M410762200
Submitted on September 20, 2004
Revised on January 20, 2005
Accepted on January 27, 2005

Fibronectin regulates latent TGBbeta by controlling matrix assembly of latent TGFbeta binding protein 1

Sarah L. Dallas, Pitchumani Sivakumar, Carolyn J. P. Jones, Qian Chen, Donna M. Peters, Deane F. Mosher, Martin J. Humphries, and Cay M. Kielty

Department of Oral Biology, University of Missouri at Kansas City, Kansas City, Missouri 64108

Corresponding Author: dallass{at}umkc.edu

Latent transforming growth factor beta binding proteins (LTBPs) are extracellular matrix (ECM) glycoproteins that play a major role in storage of latent TGFbeta in the ECM and regulate its availability. Here we show that fibronectin is critical for incorporation of LTBP1 and TGFbeta into the ECM of osteoblasts and fibroblasts. Immunolocalization studies suggest that fibronectin provides an initial scaffold that precedes and patterns LTBP1 deposition but that LTBP1 and fibronectin are later localized in separate fibrillar networks, suggesting that the initial template is lost. Treatment of fetal rat calvarial osteoblasts with a 70kDa N-terminal fibronectin fragment that inhibits fibronectin assembly impaired incorporation of LTBP1 and TGFbeta into the ECM. Consistent with this, LTBP1 failed to assemble in embryonic fibroblasts that lack the gene for fibronectin. LTBP1 assembly was rescued by full length fibronectin and superfibronectin, which are capable of assembly into fibronectin fibrils but not by other fibronectin fragments, including a 160kDa RGD-containing fragment that activates alpha 5beta 1 integrins. This suggests that the critical event for LTBP1 assembly is the formation of a fibronectin fibrillar network and that integrin ligation by fibronectin molecules alone is not sufficient. Not only was fibronectin essential for the initial incorporation of LTBP1 into the ECM, but the continued presence of fibronectin was required for the continued assembly of LTBP1. These studies highlight a non-redundant role for fibronectin in LTBP1 assembly into the ECM and suggest a novel role for fibronectin in regulation of TGFbeta via LTBP1 interactions.


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