Decorin is a small secreted chondroitin/dermatan sulfate proteoglycan belonging to the class I small leucine-rich proteoglycan family (SLRP). All SLRP family members are characterized by the Nterminal and C terminal cysteine rich regions, which flank the central region containing 1012 tandem leucinerich repeats. In mouse Decorin, the glycosaminoglycan chain is Olinked to Ser34 in the Nterminal disulfide bridged loop. Decorin binds to fibronectin, TGFβ, type I and type II collagen. The binding of Decorin to these molecules is mediated via the core protein. Decorin plays a role in maintaining collagen fibrillogenesis. Depending on the cell context, Decorin can either block or augment the bioactivity of TGFβ Decorin induces growth suppression by activation of a signaling pathway that culminates in the blockade of the cell cycle machinery. Decorin can also induce fibroblast cytoskeletal and signalling changes that results in an increased cell migration (1, 2).