SLRP

Small leucine-rich proteoglycan (SLRP) refers to a family of secreted extracellular matrix proteoglycans characterized by their leucine-rich repeat (LRR) motifs. These molecules regulate collagen fibrillogenesis, ECM assembly, and growth factor signaling.

Most members possess a core protein with covalently attached glycosaminoglycan (GAG) chains, typically dermatan sulfate, chondroitin sulfate or keratan sulfate; others exist predominantly as core proteins with little or no GAG.

Notable members include decorin (DCN), biglycan (BGN), fibromodulin (FMOD), lumican (LUM), keratocan (KERA), epiphycan (EPYC), asporin (ASPN), opticin (OPTC) and osteoadherin (OSAD).

SLRPs influence collagen assembly and fibril organization in connective tissues and modulate signaling by transforming growth factor-beta and other growth factors. They are widely expressed in skin, tendon, cartilage, cornea and bone, and their functions contribute to tissue integrity, wound healing and transparency in the cornea.

Altered SLRP expression or function has been associated with fibrosis, osteoarthritis, cancer progression and impaired wound repair. In research and clinical contexts, SLRPs are explored for biomaterial design, regenerative medicine and as potential therapeutic targets.