Abstract
Cartilage ultrastructure is based on collagen fibrils tied together by proteoglycans (PGs). Interfibrillar orthogonal PG bridges ('shape modules') were located by electron histochemistry using Cupromeronic blue methodology. Their frequency and size, similar to those in tendon, cornea, etc., were compatible with biochemical estimates of tissue decoran (formerly decorin), the PG component of shape module bridges. Digestion by hyaluronanase and chondroitinase AC helped to identify aggrecan and decoran and exemplified the destruction of shape modular organization by glycan-splitting agents. The anionic glycosaminoglycan (AGAG) of decoran, dermochondan sulphate (DS, formerly dermatan sulphate), contains L-iduronate, an elastic sugar unit. Chondroitan, keratan (present in aggrecan) and hyaluronan are not similarly elastic but can participate in sliding-filament reversible deformability. Mechanical properties predicted for the interfibrillar bridges accord with anisotropic stress/strain responses of articular cartilage to compressive or tensile stresses. We propose that fluid from pericellular aggrecan-rich domains moves under pressure into the interterritorial fibrillar arrays against the elastic resistance of the shape modules, which return the fluid, post-compression, to its original position. Cartilage is tendon-like, with the addition of expansile aggrecan-rich reservoirs of aqueous shock absorber fluid. Rupture or loss of interfibrillar ties would allow expansile PG to force the collagenous matrix apart, imbibing water, increasing swelling and fissuring--characteristic manifestations of osteoarthrosis (OA), a joint disease of major economic importance. Decoran may be a primary target of the OA disease process.