Abstract
Proteoglycans were extracted from the adult human meniscus under dissociative conditions and purified by CsCl-density-gradient centrifugation. The preparations of highest density contained proteoglycan that possessed the ability to interact with hyaluronic acid, was of large subunit size and was composed of chondroitin sulphate, keratan sulphate and sialic acid-containing oligosaccharides. This 'cartilage-like' proteoglycan also exhibited subunit and aggregate structures analogous to those of hyaline-cartilage proteoglycans when examined by electron microscopy. However, the composition of this proteoglycan was more comparable with proteoglycans from immature cartilage than from age-matched cartilage. The preparations from lower density, which were enriched in dermatan sulphate, contained smaller proteoglycan that was not able to interact with hyaluronic acid. This non-aggregating proteoglycan may be structurally distinct from the 'cartilage-like' proteoglycan, which does not contain dermatan sulphate.
MeSH Terms
Aged
Amino Acids/analysis
Borohydrides/pharmacology
Carbohydrates/analysis
Chromatography, Gel
Humans
Hyaluronic Acid/metabolism
Menisci, Tibial/metabolism,ultrastructure
Middle Aged
Papain/pharmacology
Proteoglycans/isolation & purification,metabolism
Chemicals
Amino Acids
Borohydrides
Carbohydrates
Proteoglycans
Hyaluronic Acid
Papain
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Roughley P J
McNicol D
Santer V
Buckwalter J
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