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A more recent version of this article appeared on July 29, 2005
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Papers In Press, published online ahead of print June 1, 2005
J. Biol. Chem, 10.1074/jbc.M504270200
Submitted on April 19, 2005
Revised on May 24, 2005
Accepted on June 1, 2005

The prodomain of BMP-7 targets the BMP-7 complex to the extracellular matrix

Kate E. Gregory, Robert N. Ono, Noe L. Charbonneau, Chiu-Liang Kuo, Douglas R. Keene, Hans Peter Bachinger, and Lynn Y. Sakai

Department of Biochemistry and Molecular Biology, Oregon Health & Science University and Shriners Hospital for Children, Portland, OR 97239

Corresponding Author: lys{at}shcc.org

Biochemical and biophysical methods are used to show that BMP-7 is secreted as a stable complex consisting of the processed growth factor dimer noncovalently associated with its two prodomain propeptide chains and that the BMP-7 complex is structurally similar to the small TGFb complex. Since the prodomain of TGFb interacts with Latent TGFb Binding Proteins, a family of molecules homologous to the fibrillins, the prodomain of BMP-7 was tested for binding to fibrillin-1 or to LTBP-1. The BMP-7 prodomain and BMP-7 complex, but not the separated growth factor dimer, interact with N-terminal regions of fibrillin-1. This interaction may target the BMP-7 complex to fibrillin microfibrils in the extracellular matrix. Immunolocalization of BMP-7 in tissues like the kidney capsule and skin reveals co-localization with fibrillin. However, BMP-7 immunolocalization in other tissues known to be active sites for BMP-7 signaling is not apparent, suggesting that immunolocalization of BMP-7 in certain tissues represents specific extracellular storage sites. These studies suggest that the prodomains of TGFb-like growth factors are important for positioning and concentrating growth factors in the extracellular matrix. In addition, they raise the possibility that prodomains of other TGFb-like growth factors interact with fibrillins and/or LTBPs and are also targeted to the extracellular matrix.


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