The small leucine-rich proteoglycans (SLRPs) are a family of proteins that are present in extracellular matrix and that share in common multiple repeats of a leucine-rich structural motif, flanked by cysteine residues. These proteins appear to interact in many cases with collagen, modifying the deposition and arrangement of collagen fibers in the extracellular matrix, and also with cells and with soluble growth factors. The interaction of SLRPs with cells and with growth factors like TGF-beta may affect the proliferation of cells in addition to modifying the extracellular environment. Postranslational modification of SLRPs with carbohydrates and sulfate-containing groups appears to modify the function of SLRPs. Changes in SLRP expression and modification in cornea, atherosclerotic plaque, joints, bone, tendons, and kidney may be associated with disease progression in those tissues. Decorin is one SLRP expressed throughout the body that stabilizes collagen fibrils and that also antagonizes the action of the cytokine TGF-beta, blocking cell cycle progression, and potentially playing a role in cancer and wound healing. The SLRP biglycan is expressed in bone and other connective tissues and genetic disruption of biglycan in mice causes low bone mass similar to osteoporosis.
Contributor: Glenn Croston, PhD
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