Proteoglycan degradation by the ADAMTS family of proteinases

Proteoglycans are key components of extracellular matrices, providing structural support as well as influencing cellular behaviour in physiological and pathological processes. The diversity of proteoglycan function reported in the literature is equally matched by diversity in proteoglycan structure. Members of the ADAMTS (A Disintegrin And Metalloproteinase with ThromboSpondin motifs) family of enzymes degrade proteoglycans and thereby have the potential to alter tissue architecture and regulate cellular function. In this review, we focus on ADAMTS enzymes that degrade the lectican and small leucine-rich repeat families of proteoglycans. We discuss the known ADAMTS cleavage sites and the consequences of cleavage at these sites. We illustrate our discussion with examples from the literature in which ADAMTS proteolysis of proteoglycans makes profound changes to tissue function.

► Lecticans and SLRPs are proteoglycans that can be degraded by ADAMTS proteinases in vivo.
► ADAMTS enzymes are members of the metzincin family of zinc-dependent proteinases.
► Lecticans bind hyaluronan to help hydrate tissues and confer biomechanical properties.
► SLRPs can act as co-receptors for signalling or depots for growth factor binding.
► ADAMTS cleavage of lecticans and SLRPs can be pathological or physiological.