The role of link protein in mediating the interaction between hyaluronic acid and newly secreted proteoglycan subunits from adult human articular cartilage.

Abstract

Normal adult human articular cartilage in organ culture secretes proteoglycan subunits that cannot initially interact in a normal manner with hyaluronic acid unless the latter is present at high concentrations and a neutral pH is employed. However, if the newly secreted subunit is allowed to mature in the cartilage matrix for up to 12 h, then its ability to interact is indistinguishable from that of its more mature counterparts. This conversion does not take place if the proteoglycan subunits are incubated in dilute solutions in the absence of the cartilage, and it is prevented by culturing at low temperature. The newly secreted proteoglycan subunits can, however, be induced to interact with hyaluronic acid by the presence of link proteins. The complex formed by these three components cannot be dissociated in the presence of hyaluronic acid oligosaccharides, suggesting a normal aggregate configuration. It is thus possible that proteoglycan aggregate formation within the cartilage is initially mediated by the presence of link proteins, which induce a conformational change with the hyaluronic acid-binding region of the proteoglycan subunits, although additional modification may be necessary to render any such change irreversible.