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J. Biol. Chem., Vol. 282, Issue 30, 22062-22071, July 27, 2007

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SPARC Regulates Processing of Procollagen I and Collagen Fibrillogenesis in Dermal Fibroblasts^*

Tyler J. Rentz, Felicitta Poobalarahi, Paul Bornstein, E. Helene Sage^¶, and Amy D. Bradshaw¹

From the Department of Medicine, Medical University of South Carolina, Charleston, South Carolina 29412, the Department of Biochemistry, University of Washington, Seattle, Washington 98195, and the ^¶Hope Heart Program, Benaroya Research Institute at Virginia Mason, Seattle, Washington 98101

A characterization of the factors that control collagen fibril formation is critical for an understanding of tissue organization and the mechanisms that lead to fibrosis. SPARC (secreted protein acidic and rich in cysteine) is a counter-adhesive protein that binds collagens. Herein we show that collagen fibrils in SPARC-null skin from mice 1 month of age were inefficient in fibril aggregation and accumulated in the diameter range of 60-70 nm, a proposed intermediate in collagen fibril growth. In vitro, procollagen I produced by SPARC-null dermal fibroblasts demonstrated an initial preferential association with cell layers, in comparison to that produced by wild-type fibroblasts. However, the collagen I produced by SPARC-null cells was not efficiently incorporated into detergent-insoluble fractions. Coincident with an initial increase in cell association, greater amounts of total collagen I were present as processed forms in SPARC-null versus wild-type cells. Addition of recombinant SPARC reversed collagen I association with cell layers and decreased the processing of procollagen I in SPARC-null cells. Although collagen fibers formed on the surface of SPARC-null fibroblasts earlier than those on wild-type cells, fibers on SPARC-null fibroblasts did not persist. We conclude that SPARC mediates the association of procollagen I with cells, as well as its processing and incorporation into the extracellular matrix.

Received for publication, January 8, 2007 , and in revised form, April 13, 2007.

^* This work was supported by National Institutes of Health Grants KO1 (to A. D. B.), GM-40711 (to E. H. S.), and AR 11248 (to P. B.) and a Veteran Affairs Career Development Award (to A. D. B.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed: Gazes Cardiac Research Institute, 114 Doughty St., Medical University of South Carolina, Charleston, SC 29425. Tel.: 843-792-4959; Fax: 843-876-5068; E-mail: bradshad{at}musc.edu.

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