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Proteoglycans of Cartilage

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Proteoglycans of Cartilage J Clin Pathol: first published as 10.1136/jcp.s3-12.1.67 on 1 January 1978. Downloaded from J. clin. Path., 31, Suppl. (Roy. Coll. Path.), 12, 67-81 Proteoglycans of cartilage HELEN MUIR From the Kennedy Institute of Rheumatology, Hammersmith, London Proteoglycans are probably the most important non- accounts for about half the dry weight of full- fibrillar constituents of connective tissue although thickness articular cartilage, but the amount little is known about the proteoglycans of connective decreases with depth from the articular surface tissue other than cartilage. Hence this paper is (Maroudas et al., 1969; Muir et al., 1970). Con- mainly concerned with cartilage proteoglycans. versely the proteoglycan content varies approxi- Proteoglycans are found throughout connective mately inversely with the collagen content and there tissue, but those of cartilage have certain features is a topographical variation in the overall composi- that distinguish them from proteoglycans of other tion of articular cartilage that appears to be charac- connective tissues. Cartilage is an avascular tissue in teristic of the individual (Maroudas et al., 1969; which the cells are sparsely distributed in a stiff Muir et al., 1970; Kempson et al., 1973). The matrix. Although the content of water is high-about inverse relationship of proteoglycan and collagen 70% in the cartilage of human femoral condyles contents is also clearly seen in human intervertebral (Maroudas et al., 1969)-it is precisely the presence discs (Adams et al., 1977). of water in conjunction with proteoglycans and col- lagen that makes cartilage resilient and elastic. General structure of proteoglycans Cartilage may be regarded as a reinforced fibre net- work which in load-bearing joints has to withstand The sulphated glycosaminoglycans such as chon- copyright. very high repetitive loads (Freeman and Kempson, droitin sulphate, keratan sulphate, or dermatan 1973). sulphate are present throughout connective tissue as As was first pointed out by Fessler (1960), a proteoglycans in which the glycosaminoglycan chains random macromolecular mesh (represented by pro- teoglycans in this instance) placed within a fibrous network (such as collagen) so that the macromole- Kgf/cm2 N/mm2 cules cannot move will impede the flow of interstitial http://jcp.bmj.com/ water within the tissue when an external force is 150 151 o 0 applied. Fluid pressure within cartilage rises im- 0 0 mediately a load is applied, but as the water is driven 0 out from the loaded area cartilage deforms only Q 0 CD (9 0 gradually because the proteoglycans entrapped in the E 0 1 10 0 collagen network impede the flow of interstitial a. 100 0 - Co/O~~~~0000 water. Hence the compressive stiffness of cartilage 10 0 o~~~~.o~~~ on September 28, 2021 by guest. Protected over short intervals is directly correlated with the V /0 00O proteoglycan content measured as glycosamino- 10 0 0 0 glycan (Kempson et al., 1970) (Fig. 1). Proteo- 0 00 cone glycans exert a swelling pressure that is constantly I~ 5 0,/d 0 5Q. 0 0 restrained by the collagen network in which they are 0 o entrapped. Maroudas (1975) has calculated the 00 0 internal osmotic pressure of cartilage of human femoral heads to be about 3-4-3-6 atmospheres. Sorption isotherms also indicate that swelling pres- C- 0 sure is mainly attributable to the proteoglycan 60 80 100 120 component ofcartilage (Mathews and Decker, 1977). Total glycosaminog lycans content The relative proportion of collagen to proteo- (pgImg dry weight) glycan and other constituents varies in different types Fig. 1 Variation of creep modulus (that is, stiffness of of connective tissue and largely determines the cartilage) with total glycosaminoglycan content (from physical characteristics of the tissue. Collagen Kempson et al., 1970). 67 J Clin Pathol: first published as 10.1136/jcp.s3-12.1.67 on 1 January 1978. Downloaded from 68 Helen Muir are attached at one end to a protein core. In cartilage sulphate are attached to protein via a trisaccharide proteoglycans as many as 50-100 chondroitin sequence of neutral sugars (Fig. 3) in which xylose sulphate chains are attached laterally to a protein is glycosidically attached to the hydroxyl group of backbone which comprises about 10-15% of the serine residues on the core protein. The complete weight of the molecule. Since the average chain structure of the linkage region was established by the weight of chondroitin sulphate is 15-20 000, cartilage work of Roden (Roden and Armand, 1966; Roden proteoglycans have molecular weights of about and Smith, 1966; Helting and Roden, 1968). Xylose, 1-3 x 106 daltons (Eyring and Yang, 1968; which had not previously been found in animal poly- Luscombe and Phelps, 1967; Pasternack et al., 1974). saccharides, is important in co-ordinating the The general structure, shown diagrammatically in synthesis of glycosaminoglycan chains with the Fig. 2, was proposed by Mathews and Lozaityte synthesis of core protein. (1958) and by Partridge et al. (1961). It is consistent with the effects of proteolytic enzymes, to which CHONDROITIN SULPHATE proteoglycans are particularly vulnerable (Muir, Chondroitin sulphate consists of repeating disac- 1958), because when even a few peptide bonds are charide units of glucuronic acid and N-acetylgalacto- cleaved the whole molecule falls apart. The electron samine (Fig. 4). There are about 25-30 such units in microscopical appearance of single molecules, spread the average chain of chondroitin sulphate with and visualised by a special technique (Rosenberg et almost one sulphate group per disaccharide in one al., 1970a) also agrees with this general structure. of two isomeric positions. The distribution of sul- phate residues along the chains is not uniform, however, as there are fewer in the vicinity of the cs linkage of carbohydrate to protein (Wasteson and the HA binOding KS Core protein / Lindahl, 1971). In chondroitin 4-sulphate sulphate is attached to C4 and in chondroitin 6-sulphate to C6 of the galactosamine residues forms occur in articular cartilage and (Fig. 4). Both copyright. chondroitin 6-sulphate gradually increases with age Wasteson, 1972) in adult human IIII]6,i N t 1 (Hjertquist and II articular cartilage (Mankin and Lippiello, 1971; ..1C11Ivl i p :\II\\\ll l Lust and Pronsky, 1972; Hjertquist and Lemperg, 1972; Lemperg et al., 1974). The proportions of each Constant region Variable region isomer may be deduced from the effects of specific Fig. 2 Diagram ofproteoglycan molecule. HA = degradative enzymes, known as chondroitinases. The hyaluronic acid. CS = chondroitin sulphate. results suggest that the chondroitin sulphate isomers http://jcp.bmj.com/ KS = keratan sulphate. are not present as separate chains but that the sulphate groups occuipy one or other isomeric In addition to chondroitin sulphate cartilage position along the same chain (Mourao and Dietrich, proteoglycans contain fewer but variable numbers 1973; Seno et al., 1975; Murata and Bjelle, 1977). of keratan sulphate chains attached to the same core The biological significance of the position of the protein (Seno et al., 1965; Tsiganos and Muir, 1967; sulphate group is not known. Both chondroitin isomers display highly ordered helical con- Heinegard and Gardell, 1967; Hoffman et al., 1967; sulphate on September 28, 2021 by guest. Protected Hascall and Riolo, 1972; HeinegArd, 1972). In any formations when stretched films of these compounds given cartilage proteoglycans are heterogeneous and are examined by x-ray fibre analysis. In chondroitin exhibit a range of chemical composition and mole- 6-sulphate, however, the sulphate groups project cular size. Chondroitin sulphate and all sulphated further from the chain than in chondroitin 4-sulphate glycosaminoglycans with the exception of keratan (Isaac and Atkins, 1973; Atkins, 1977). Chondroitin COOH CH20H CH20H H H \s0 \ ro\ O\rO-CH2to -Oi H>HY HHNH2 H OH H OH H OH H OH COOH Fig. 3 Trisaccharide sequence ofneutral sugars that link glycosaminoglycan chains such as chondroitin sulphate to serine residues of the core protein. J Clin Pathol: first published as 10.1136/jcp.s3-12.1.67 on 1 January 1978. Downloaded from Proteoglycans of cartilage 69 COOH HO3S CH20H CH20HC HO3SOCH2 0 ' HO "~ ~ 01 H~ HH HH HH LH NHCOCH3@n H OH H NHCOCH3I L ndi t Fig. 5 Repeating disaccharide unit of keratan sulphate. COOH HO3S O CH2 over glucosamine (Gregory and Roden, 1961; ~ 0HO 0 Bhavanandan and Meyer, 1967) and there are branch 0 H HH H points along the chain where extra galactose is attached. Small amounts of fucose (Bhavanandan I H OH H NHCOCH3I and Meyer, 1968) and sialic acid (Toda and Seno, L .n 1970; Hascall and Riolo, 1972) are also present in b terminal positions. Fig. 4 Repeating disaccharide units of(a) chondroitin 4-sulphate, and (b) chondroitin 6-sulphate. Extraction and heterogeneity of proteoglycans 6-sulphate may therefore interact more strongly than Extraction procedures developed for one kind of chondroitin 4-sulphate with the basic groups of cartilage are not necessarily applicable to all kinds collagen and other proteins. and proteoglycans are much more difficult to extract from other types of connective tissue. Much of the KERATAN SULPHATE earlier work on proteoglycans was initiated by Keratan sulphate is found only in proteoglycans of Schubert and his associates (Gerber et al., 1960; Pal cartilage, intervertebral discs, and cornea. It con- and Schubert, 1965; Pal et al., 1966), who employed copyright. tains no uronic acid. It consists essentially of disac- high-speed homogenisation to achieve efficient charide repeating units of N-acetylglucosamine and extraction when about 65 % of the proteoglycan was galactose (Fig. 5), and hence molar ratios of extracted from bovine nasal cartilage. glucosamine:galactosamine may be used to deter- High shearing forces degrade polymers of large mine the relative proportions ofkeratan sulphate and molecular weight (Harrington and Zimm, 1965) and chondroitin sulphate in isolated proteoglucans and, hence methods employing high-speed homogenisa- less precisely, in whole cartilage.
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