The Heterogeneity and Polydispersity of Articular Cartilage Proteoglycans

Swann, David A.; Powell, Susan B.; Sotman, S L

doi:10.1016/b978-0-12-301301-9.50062-1

Cited by 8 publications

(19 citation statements)

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“…The detailed chemical composition and properties of this PG and the analytical methods used in this study are given in Ref. 22. IR analysis indicated that the CS-6 contained 6-sulfated residues, that the DS contained 4-sulfated residues, and that PG-I was primarily 6 -s~l f a t e d .~~…”

Section: Materials a N D Methodsmentioning

confidence: 99%

Effects of glycosaminoglycans and proteoglycan on the in vitro assembly and thermal stability of collagen fibrils

Snowden

Swann

1980

Biopolymers

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SynopsisThe effects of three glycosaminoglycans (chondroitin 6-sulfate, dermatan sulfate, and hyaluronate) and a proteoglycan on the kinetics of fibril formation and on the thermal stability of the i n uitro assembled collagen fibrils, under physiological conditions of ionic strength and pH, have been examined. The glycosaminoglycans were found to influence the kinetics of collagen precipitation but not the thermal stability of the i n uitro assembled fibrils. The proteoglycan was found to influence the kinetics of collagen precipitation and to reduce the thermal stability of the i n uitro assembled fibrils. Comparison of the interaction occurring between chondroitin 6-sulfate and collagen under acidic conditions (0.05M acetic acid) and that occurring under physiological conditions showed that markedly different interaction products were formed under the different conditions.

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Section: Materials a N D Methodsmentioning

confidence: 99%

Effects of glycosaminoglycans and proteoglycan on the in vitro assembly and thermal stability of collagen fibrils

Snowden

Swann

1980

Biopolymers

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“…Amino acids, hexosamines, neutral sugars, Nacetylneuraminic acid, uronic acid and sulphate were measured by previously described methods (Swann et al, 1979). A manual resorcinol method (Jourdian et al, 1971) was used to determine the sialic acid content of column fractions (Fig.…”

Section: General Analytical Methodsmentioning

confidence: 99%

“…Proteoglycans were extracted from metacarpalphalangeal joints of foetal, calf and adult cattle feet with guanidinium chloride containing proteinase inhibitors (1 mM-phenylmethanesulphonyl fluoride, 1 mM-p-chloromercuribenzoic acid and lOmM-disodium EDTA) and fractionated by two dissociative density gradients by using the procedure described by Swann et al (1979).…”

Section: Extraction Andfractionationmentioning

confidence: 99%

“…

Proteoglycans were extracted from the articular cartilage of foetal, calf and adult bovine metacarpal-phalangeal joints with 4 M-guanidinium chloride. After extraction, the high-density proteoglycans (PG-I fractions) were prepared by sedimentation in two sequential CsCl-density-gradient procedures [Swann, Powell & Sotman (1979) Chem. 254,[945][946][947][948][949][950][951][952][953][954].

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mentioning

confidence: 99%

“…Cartilage proteo-1959;Anderson et al, 1964;Mathews & Glasgov, glycans are complex polydisperse macromolecules 1966; Hjertquist & Engfeldt, 1967, and references consisting of chondroitin sulphate, keratan sulphate cited therein; Greiling & Stuhlsatz, 1969; Bjelle et (Rosenberg et al, 1975(Rosenberg et al, , 1976Hardingham et al, al., 1972;Hjertquist & Lemperg, 1972;Hjertquist & 1976;Heinegard & Axelsson, 1977; Heinegird, Wasteson, 1972;Lemperg et al, 1974;Mankin & 1977; Hascall & Heinegard, 1979) and oligo-saccharide side chains covalently linked to a protein core . Several studies (Hoffman et al, 1975;Hopwood & Robinson, 1975;Roughley & Mason, 1976;Stanescu et al, 1977;Swann et al, 1979) have also shown that articular cartilage contains different types of proteoglycans and significant quantities of protein and glycoprotein constituents. There is therefore the possibility that the gross chemical changes may reflect alterations in the structure and/or the proportions of the different types of macromolecular components.…”

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Age-related changes in the chemical composition of bovine articular cartilage. The structure of high-density proteoglycans

Garg

Swann

1981

Biochemical Journal

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Proteoglycans were extracted from the articular cartilage of foetal, calf and adult bovine metacarpal-phalangeal joints with 4m-guanidinium chloride. After extraction, the high-density proteoglycans (PG-I fractions) were prepared by sedimentation in two sequential CsCl-density-gradient procedures [Swann, Powell & Sotman (1979) J. Biol. Chem.254, 945-954]. The PG-I fractions from foetal, calf and adult tissues accounted for 75%, 52% and 46% respectively of the extracted components. The glucosamine, galactose, N-acetylneuraminic acid and protein contents increased with age. The overall amino acid compositions of PG-I fractions were similar. Fractionation of PG-I-fraction samples on a Bio-Gel A-50m column indicated that the molecular weight decreased with age. The PG-I fractions were specifically (3)H-labelled by treatment with galactose oxidase followed by reduction with NaB(3)H(4). The (3)H radioactivity was incorporated into both galactose and galactosamine residues of different carbohydrate side chains. The elution profiles of alkaline borohydride-treated foetal, calf and adult PG-I-fraction samples on a Sepharose 6B column showed that the molecular weights of chondroitin sulphate chains were 13500, 12000 and 10500 in foetal, calf and adult tissues respectively. Fractionation of the alkaline borohydride-treated foetal, calf and adult PG-I-fraction samples and (3)H-labelled calf and adult PG-I-fraction samples on a Bio-Gel P-10 column showed that there was an inverse relationship between the low-molecular-weight O-linked oligosaccharides and the higher-molecular-weight sialic acid-containing constituents at different ages. The oligosaccharide components of foetal, calf and adult PG-I-fraction samples represented 79%, 69% and 36% respectively of the total sialic acid content of the proteoglycans. Similarly in the (3)H-labelled calf and adult samples 75% and 30% of the total radioactivity were present in the oligosaccharide components respectively. Digestion with chondroitinase AC-II and infrared analyses showed that the PG-I-fraction F and C samples contained primarily chondroitin 4-sulphate chains whereas PG-I-fraction sample A was 6-sulphated. These studies show that the major proteoglycans (PG-I fractions) in the articular cartilage of foetal, calf and adult animals differ in the content, types and structure of the chondroitin sulphate, keratan sulphate and oligosaccharide constituents. These changes in proteoglycan structure reflect the gross age-related changes in the chemical composition of the tissue.

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The chemical composition of bovine vitreous-humour collagen fibres

Swann¹,

Sotman²

1980

Biochemical Journal

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The insoluble protein fraction was prepared from the central and posterior peripheral fraction of bovine vitreous humour. The collagen present in this fraction was solubilized by pepsin and fractionated by gel chromatography. Analysis of the solubilized collagen fractions showed that the alpha-chain component had an amino acid composition and yielded a series of CNBr-cleavage peptides that showed it was very similar to type II collagen obtained from articular cartilage. Bovine vitreous-humour collagen alpha-chains differed, however, from those of cartilage collagen in that they had a lower alanine content and differed in their susceptibility to cleavage by CNBr. Satisfactory cleavage was obtained after two CNBr treatments involving reduction and alkylation. In addition, significant quantities of other peptides constituents were present in the vitreous-humour collagen fractions, and the galactose and glucose content of the alpha-chain fraction was more than double that of the same fraction obtained from articular cartilage. Although the origin of the additional peptide constituents in the vitreous-humour collagen preparations is not known, the results obtained indicate that they are probably not derived from a distinct type of alpha-chain component but may be terminal peptides covalently linked to the alpha 1 type-II helical portions of the collagen. The differences in the chemical composition of the vitreous-humour collagen indicate that vitreous-humour fibres are composed of a special type-II collagen.

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The Heterogeneity and Polydispersity of Articular Cartilage Proteoglycans

Cited by 8 publications

References 5 publications

Effects of glycosaminoglycans and proteoglycan on the in vitro assembly and thermal stability of collagen fibrils

Effects of glycosaminoglycans and proteoglycan on the in vitro assembly and thermal stability of collagen fibrils

Age-related changes in the chemical composition of bovine articular cartilage. The structure of high-density proteoglycans

The chemical composition of bovine vitreous-humour collagen fibres

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