Secreted protein acidic and rich in cysteine (SPARC), also known as Osteonectin (ON), is a member of the SPARC family. SPARC contains a EF-hand domain, a follistatin-like domain and a Kazal-like domain. It is expressed at high levels in tissues undergoing morphogenesis, remodeling and wound repair. SPARC has two calcium binding sites; an acidic domain that binds 5 to 8 Ca2+ with a low affinity and an EF-hand loop that binds a Ca2+ ion with a high affinity. SPARC appears to regulate cell growth through interactions with the extracellular matrix and cytokines.It binds calcium and copper, several types of collagen, albumin, thrombospondin, PDGF and cell membranes. The activity of SPARC is context- and cell-type-dependent, which is highlighted by the fact that SPARC has shown seemingly contradictory effects on tumor progression in both clinical correlative studies and in animal models. SPARC enhances the Wnt/beta-catenin signaling pathway and regulates the expression and posttranslational modification of collagen. SPARC might drive preadipocytes away from the status of growth arrest and therefore prevent terminal differentiation. SPARC could also decrease WAT deposition through its negative effects on angiogenesis.
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