Core proteoglycans, small leucine-rich

Neame PJ, Choi HU, Rosenberg LC. The primary structure of the core protein of the small, leucine-rich proteoglycan (PG I) from bovine articular cartilage. J Biol Chem 1989 264 8653-8661. 

Scott PG, McEwan PA, Dodd CM, Bergmann EM, Bishop PN, Bella J. Crystal structure of the dimeric protein core of decorin, the archetypal small leucine-rich repeat proteoglycan. Proc Natl Acad Sci USA 2004 101 15633-15638. 

The proteoglycans in this family, which includes decorin, biglycan, lumican, and fibromodulin, are major components of the interstitial matrix produced by fibroblasts and other cells. The core proteins are small (37-45 kDa) and have several leucine-rich motifs [112] with similarity to the LH-CG receptor, thyrotropin receptor, and Drosophila proteins chaoptin and toll. Core proteins of this family characteristically undergo proteolytic processing following synthesis, with removal of an additional small peptide from the N-terminus. 

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