Abstract
Proteoglycans are a complex family of macromolecules that consist of a protein core to which at least one glycosaminoglycan is covalently attached through the neutral trisaccharide, Galßl→3Galßl→4Xylß→Ser (for review, see Rodén, 1980). The heparin/heparan sulfate family of glycosaminoglycans is formed in the Golgi by the sequential addition of alternating GlcA and GlcNAc onto this trisaccharide, whereas the chondroitin sulfate family of glycosaminoglycans is formed by the sequential addition of alternating GlcA and GalNAc. After addition of the precursor saccharides, the polymer undergoes a number of enzymatic modifications including N- and O-sulfation and epimerization of GlcA to IdoA to yield mature glycosaminoglycans. The combination of different core proteins, varied numbers, types, and sizes of glycosaminoglycans, and possible N- and O-linked oligosaccharides results in a diverse family of proteoglycans. This diversity probably reflects the proteoglycans’ numerous functions in different cells and tissues. Proteoglycans are major constituents of the extracellular matrix where they help to determine both the physical properties and function of connective tissues. Proteoglycans are also important components of plasma membranes where they bind growth factors and often participate in intercellular binding and cell/matrix interactions.
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Humphries, D.E., Stevens, R.L. (1992). Regulation of the Gene that Encodes the Peptide Core of Heparin Proteoglycan and Other Proteoglycans that are Stored in the Secretory Granules of Hematopoietic Cells. In: Lane, D.A., Björk, I., Lindahl, U. (eds) Heparin and Related Polysaccharides. Advances in Experimental Medicine and Biology, vol 313. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-2444-5_6
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DOI: https://doi.org/10.1007/978-1-4899-2444-5_6
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