Proteoglycans in normal and severely osteoarthritic human cartilage

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Abstract
Proteoglycans from osteoarthritic cartilage were compared to those from normal articular cartilage. Normal proteoglycan aggregates are larger in size and more homogeneous than those in osteoarthritis. Proteoglycan monomers from both sources gave 2 peaks on controlled pore glass bead chromatography. Although the retarded material from normal cartilage showed an affinity for hyaluronate, the same material from osteoarthritic cartilage did not. Hyaluronate-binding capacity of the material which is partly in the void volume and partly retarded was similar in both types of cartilage. Apparently in osteoarthritic cartilage the proteoglycan aggregates are smaller and more heterogeneous, and the chondroitin sulfate side chains are shorter. Apparently there are 2 populations of proteoglycan, one with its hyaluronate-binding-protein region of core protein intact and the other possessing an inactive binding region or totally lacking it.