Abstract
Connective tissue is composed of scattered cells embedded in an extracellular matrix consisting of abundant collagen fibers, elastin, and an amorphous ground substance dominated by proteoglycans. Proteoglycans contain a central protein core that is substituted with glycosaminoglycans. With the possible exception of hyaluronate all of the known glycosaminoglycans (Table 1) occur as proteoglycans. The various proteoglycans of the interfibrillar space are considered to control the architecture of the fibrillar network (Muir and Hardingham, 1975). A general observation is that the type of proteoglycan found in a tissue varies with the biomechanical properties of the tissue. The cartilage proteoglycan is especially designed for resisting compression and deformation by virtue of its aggregation with hyaluronate (carbohydrate—protein interaction) to form large, highly expanded supramolecular aggregates (Muir and Hardingham, 1975).
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© 1984 The Humana Press Inc.
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Fransson, LÅ., Cöster, L., Nieduszynski, I.A., Phelps, C.F., Sheehan, J.K. (1984). Self-Association of Copolymeric Glycosaminoglycans (Proteoglycans). In: Arnott, S., Rees, D.A., Morris, E.R. (eds) Molecular Biophysics of the Extracellular Matrix. Humana Press. https://doi.org/10.1007/978-1-4612-5166-8_5
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DOI: https://doi.org/10.1007/978-1-4612-5166-8_5
Publisher Name: Humana Press
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