Synopsis
The mucosubstances embrace two types of molecule, the proteoglycans and the glycoproteins. These polymers have in common the existence of a single polypeptide chain to which is attached one or more polysaccharide structures. It is, however, possible to distinguish the two groups by means of several important structural characteristics of their carbohydrate components.
The presence of large amounts of carbohydrate in the molecules of many mucosubstances puts special difficulties in the way of their fixation for microscopical examination. The staining reactions used for the proteoglycans and glycoproteins depend entirely on the chemical properties of their carbohydrate components; in the past, these reactions have lacked specificity, but new, improved methods are becoming available.
In their biosynthesis, the mucosubstances seem to follow an intracellular pathway peculiar to those proteins destined for extracellular secretion, and distinct from that of the cytoplasmic proteins. The membrane systems of the endoplasmic reticulum and Golgi apparatus are of particular importance in the process.
Little is known of the biological role of many of the mucosubstances, and of their carbohydrate components in particular. A theory is put forward, proposing an essential role for the proteoglycans of cartilage in the maintenance of the mechanical function of the tissue. Work now in progress is giving strong indications that a lysosomal proteinase, cathepsin D, plays an important part in the pathological degeneration of cartilage, through its action on the proteoglycans. Lysosomes seem well equipped in their complement of hydrolytic enzymes to mediate the catabolism of mucosubstances in general.
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References
Barrett, A. J. (1967). Lysosomal acid proteinase of rabbit liver.Biochem. J. 104, 601.
Barrett, A. J. (1968). Cartilage. InComprehensive Biochemistry (eds. M. Florkin and E. H. Stotz), Vol. 26B, p. 425, Amsterdam: Elsevier.
Barrett, A. J. (1969). Properties of lysosomal enzymes. InLysosomes in Biology and Pathology (eds. J. T. Dingle and H. B. Fell), Vol. 2, p. 245, Amsterdam: North-Holland.
Barrett, A. J. (1970a). Cathepsin D. Purification of isoenzymes from human and chiken liver.Biochem. J. 117, 601.
Barrett, A. J. (1970b). The role of lysosomes in arthritis.Advanc. Sci. 27, 140.
Campbell, P. N. (1970). Functions of polyribosomes attached to membranes of animal cells.FEBS Lett. 7, 1.
Cook, G. M. W. (1968). Glycoproteins in membranes.Biol. Rev. 43, 363.
Dingle, J. T., Barrett, A. J. & Weston, P. D. (1971). Cathepsin D: immuno-inhibition by specific antisera.Biochem. J. In press.
Dingle, J. T. &Lucy, J. A. (1965). Vitamin A, carotinoids and cell function.Biol. Rev. 40, 422.
Disalvo, J. &Schubert, M. (1966). Interactions during fibril formation of soluble collagen with cartilage proteinpolysaccharide.Biopolymers 4, 247.
Dodgson, K. S. &Lloyd, A. G. (1968). Metabolism of acidic glycosaminoglycans (mucopolysaccharides). InCarbohydrate Metabolism and its Disorders (eds. F. Dickens, P. J. Randle and W. J. Whelan), p. 169, New York: Academic Press.
Fell, H. B. (1964). The role of organ cultures in the study of vitamins and hormones. InVitamins and Hormones (eds. R. S. Harris, I. G. Wool and J. A. Loraine), p. 81. New York: Academic Press.
Fewer, D., Threadgold, J. &Sheldon, H. (1964). Studies on cartilage 5. Electron microscopic observations on the autoradiographic localisation of S35 in cells and matrix.J. Ultrastruct. Res. 11, 166.
Godman, G. C. &Lane, N. (1964). On the site of sulfation in the chondrocyte.J. Cell Biol. 21, 353.
Gottschalk, A. (ed.) (1966). Glycoproteins. Amsterdam: Elsvier.
Hodson, S. &Meenan, A. (1969). The distribution of acidic mucopolysaccharides in corneal stroma.Experientia 25, 1305.
Horwitz, A. L. &Dorfman, A. (1968). Subcellular sites for synthesis of chondromucoprotein of cartilage.J. Cell Biol. 38, 358.
Meyer, K. (1969). Biochemistry and biology of mucopolysaccharides.Amer. J. Med. 47, 664.
Morré, D. J., Merlin, L. M. &Keenan, T. W. (1969). Localization of glycosyl transferase activities in a golgi appararus-rich fraction isolated from rat liver.Biochem. biophys. Res. Commun. 37, 813.
Morrison, R. I. G. (1970). The breakdown of proteoglycans by lysosomal enzymes and its specific inhibition by an antiserum to cathepsin D. InThe Chemistry and Molecular Biology of the Intercellular Matrix (ed. E. A. Balazs), Vol. 3, p. 1683 New York Academic Press.
Rambourg, A. &Leblond, C. P. (1967). Electron microscope observations on the carbohydrate-rich cell coat present at the surface of cells in the rat.J. Cell. Biol. 32, 27.
Rosenberg, L. (1971). Chemical basis for the histological use of Safranin O in the study of articular cartilage.J. Bone Jt Surg. 53A, 69.
Rosenberg, L., Hellmann, W. &Kleinschmidt, A. K. (1970). Macromolecular models of proteinpolysaccharides from bovine nasal cartilage based on electron microscope studies.J. biol. Chem. 245, 4123.
Scott, J. E. &Stockwell, R. A. (1967). On the use and abuse of the critical electrolyte concentration approach to the localisation of tissue polyanions.J. Histochem. Cytochem. 15, 111.
Spiro, R. G. (1970). Glycoproteins.Ann. Rev. Biochem. 38, 599.
Thomas, L. (1964). The effects of papain, vitamin A, and cortisone on cartilage matrixin vivo.Biophys. J. 4, No. 1, Pt 2, 207.
Weston, P. D. (1969). A specific antiserum to lysosomal cathepsin D.Immunology 17, 421.
Whur, P., Herscovics, A. &Leblond, C. P. (1969). Radioautographic visualization of the incorporation of galactose-3H and mannose-3H by rat thyroids in vitro in relation to the stages of thyroglobulin synthesis.J. Cell Biol. 43, 289.
Williams, D. J. &Rabin, B. R. (1969). The effects of aflatoxin Br and steroid hormones on polysome binding to microsomal membranes as measured by the activity of an enzyme catalysing disulphide interchange.FEBS Letters 4, 103.
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Barrett, A.J. The biochemistry and function of mucosubstances. Histochem J 3, 213–221 (1971). https://doi.org/10.1007/BF01005220
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DOI: https://doi.org/10.1007/BF01005220