The transforming growth factor-β-inducible matrix protein βig-h3 interacts with fibronectin

Document Type

Article

Publication Date

2002

Abstract

Proper growth and development require the orderly synthesis and deposition of individual components of the extracellular matrix (ECM) into well ordered networks. Once formed, the ECM maintains tissue structure and houses resident cells. One ECM component, βig-h3, is a highly conserved transforming growth factor-β-inducible protein that has been hypothesized to function as a bifunctional linker between individual matrix components and resident cells. To gain insights into its physiological function, full-length βig-h3 protein was produced using a baculovirus expression system and purified under native conditions. Human fibroblasts attached and spread on βig-h3-coated plates and developed actin stress fibers. Purified βig-h3 binds fibronectin (FN) and type I collagen (Col I) but does not bind gelatin. Using defined fragments of FN, we localized the βig-h3 recognition region to the gelatin/collagen binding domain present in the N-terminal region of the FN molecule. Our results identify FN and Col I as two ligands of βig.h3 in the ECM.

Publication Title

Journal of Biological Chemistry

Volume

277

Issue

31

First Page

28003

Last Page

28009

Comments

This article was published in Journal of Biological Chemistry, Volume 277, Issue 31, Pages 28003-28009.

The published version is available at http://dx.doi.org/10.1074/jbc.M106837200.

Copyright © 2002.

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