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Volume 52 (6): 723-733, 2004
Copyright ©The Histochemical Society, Inc.
Functional Analysis of the Matricellular Protein SPARC with Novel Monoclonal Antibodies
Department of Vascular Biology, The Hope Heart Institute, Seattle, Washington
Correspondence to: Dr. E. Helene Sage, Hope Heart Program, Benaroya Research Institute at Virginia Mason, 1201 9th Avenue, Seattle, WA 98101-2795. E-mail: hsageBRI{at}hopeheart.org
SPARC (osteonectin, BM-40) is a matricellular glycoprotein that is expressed in many embryogenic and adult tissues undergoing remodeling or repair. SPARC modulates cellular interaction with the extracellular matrix (ECM), inhibits cell adhesion and proliferation, and regulates growth factor activity. To explore further the function and activity of this protein in tissue homeostasis, we have developed several monoclonal antibodies (MAbs) that recognize distinct epitopes on SPARC. The MAbs bind to SPARC with high affinity and identify SPARC by ELISA, Western blotting, immunoprecipitation, immunocytochemistry, and/or immunohistochemistry. The MAbs were also characterized in functional assays for potential alteration of SPARC activity. SPARC binds to collagen I and laminin-1 through an epitope defined by MAb 293; this epitope is not involved in the binding of SPARC to collagen III. The other MAbs did not interfere with the binding of SPARC to collagen I or III or laminin-1. Inhibition of the anti-adhesive effect of SPARC on endothelial cells by MAb 236 was also observed. Functional analysis of SPARC in the presence of these novel MAbs now confirms that the activities ascribed to this matricellular protein can be assigned to discrete subdomains. (J Histochem Cytochem 52:723–733, 2004)
Key Words: SPARC • collagen • matricellular • monoclonal antibody • extracellular matrix
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