Abstract
Proteoglycans are important components of the extracellular matrix of articular cartilage and other soft tissues. The structural organization of these macromolecules is believed to be significant for maintaining the cohesion of the extracellular matrix, and thus influences the material properties of the tissue as a whole (Pottenger et al. 1982; Muir 1983). Recent studies have shown that the structure of proteoglycans varies with cartilage age and pathology (Hjertquist and Wasteson 1972; Bayliss and Ali 1979; Muir 1977, 1980, 1983; Roughley and White 1980; Pal et al. 1981; Buckwalter et al. 1983; Buckwalter and Rosenberg 1985). In general, as cartilage ages and degenerates, proteoglycan size decreases (i.e. lower molecular weight) and the percentage of non- aggregated forms increases. The decrease in proteoglycan size and percentage aggregation has been shown to be important factors in increased mobility of the proteoglycan within the collagen meshwork (Pottenger et al. 1982; Muir 1983). Link proteins serve to stabilize proteoglycan aggregates by joining the proteoglycan monomers to a linear hyaluronate chain (Hardingham 1979,1981). Changes in proteoglycan aggregation may involve abnormalities in the hyaluronate binding region of the monomer or the link protein (Muir 1977, 1983; Hardingham 1979,1981; Plaas and Sandy 1984; Poole 1986; Ratcliffe et al. 1986). These changes tend to alter the collagen-proteoglycan and proteoglycan-proteoglycan interactions (Obrink 1973; Myers et al. 1984b; Mow et al. 1989), causing possible migration of proteoglycan fragments through, and loss from, the extracellular matrix (Brandt 1974; Muir 1977; Bayliss and Ali 1979; Ratcliffe et al. 1986).
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Zhu, W.B., Mow, V.C. (1990). Viscometric Properties of Proteoglycan Solutions at Physiological Concentrations. In: Ratcliffe, A., Woo, S.LY., Mow, V.C. (eds) Biomechanics of Diarthrodial Joints. Springer, New York, NY. https://doi.org/10.1007/978-1-4612-3448-7_11
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