Proteoglycan leucine-rich

Leucine-rich repeats represent binding motifs found in a wide variety of both plant and mammalian proteins (Kobe and Kajava, 2001). These are involved in a multitude of protein-protein interactions. The sequence of porcine ribonuclease inhibitor, for example, displays a leucine-rich repeat (LRR) of length 27-29 residues that occurs 15 times in tandem (Fig. 9). Likewise, the family of small leucine-rich proteoglycans that includes biglycan, decorin, epiphycan, fibromodulin, keratocan, and lumican... 

Decorin is a small, leucine-rich proteoglycan and one of the many extracellular matrix (ECM) compounds. It interacts closely with the D and E bands of type 1 collagen and increases collagen s tensile strength.39,40 In rats with subcutaneously implanted devices, we found that the decorin was highly expressed at the middle and later stages of the foreign body reaction.17... 

R.V. lozzo. 1999. The biology of small leucine-rich proteoglycans Functional network of interactive proteins J. Biol. Chem. 274 18843-18846. (PubMed)... 

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. 

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. 

Monfort J, Tardif G, Reboul P, Mineau F, Roughley P, Pelletier JP, Martel-Pelletier J. Degradation of small leucine-rich repeat proteoglycans by matrix metalloprotease-13 identification of a new biglycan cleavage site. Arthritis Res Ther 2006 8 R26-R34. 

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. 

Scott PG, Dodd CM, Bergmann EM, Sheehan JK, Bishop PN. Crystal structure of the biglycan dimer and evidence that dimerization is essential for folding and stability of class I small leucine-rich repeat proteoglycans. J Biol Chem 2006 281 13324-13332. 

Small Leucine-Rich Repeat Proteoglycans of Skin... 

Small LeucIne-RIch Repeat Protelns/Proteoglycans... 

Figure 1 Dendrogram to illustrate the relationships between the different small leucine-rich repeat proteins/proteoglycans (SLRPs). SLRPs belonging to Classes I and II have 12 leucine-rich repeats while those in Class III have 7. The spacing of N-terminal cysteines differs in each class. ECM2 is considered to be Class I related, while nyctalopin and chondroadherin each have distinct sequence and structural characteristics.

Matsushima N, Ohyanagi T, Tanaka T, Kretsinger RH. Super-motifs and evolution of tandem leucine-rich repeats within the small proteoglycans-bigly-can, decorin, lumican, fibromodulin, PRELP, keratocan, osteoadherin, epiphycan, and osteoglycin. Proteins 2000 38 210-225. 

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