Abstract
Proteoglycans (PGs) occur in virtually almost all mammalian tissues and are especially prominent in cartilage. They are characterized by their core proteins and have at least one covalently bound glycosaminoglycan (GAG) chain. These macromolecules and type II collagen are major components of the extracellular matrix of cartilage, where the former exists predominantly as aggregates, resulting from the specific interaction of PG monomers and hyaluronate. This interaction is stabilized by oligosaccharide-containing link proteins. The monomers consist of a core protein, to which are attached a large number of chondroitin sulfate chains, keratan sulfate chains, and both O-linked and N-linked oligosaccharides (Figs. 6-1–6-3).
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Takagi, M. (1990). Ultrastructural cytochemistry of cartilage proteoglycans and their relation to the calcification process. In: Bonucci, E., Motta, P.M. (eds) Ultrastructure of Skeletal Tissues. Electron Microscopy in Biology and Medicine, vol 7. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-1487-5_6
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DOI: https://doi.org/10.1007/978-1-4613-1487-5_6
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