Proteoglycans from Human Articular Cartilage: The Effect of Joint Location on the Structure

Abstract

Proteoglycan monomers from the articular cartilages of the knee, hip and shoulder of 3 subjects (21, 26 and 45 years old) were isolated and analysed. The proteoglycan monomers from the high weightbearing knee and hip joints were smaller than those from the low weight-bearing shoulder joints and both had a lower chondroitin sulphate content. The proteoglycan monomers from knee joint cartilage had the lowest intra-individual chondroitin-4rsulphate content in each case. Hyaluronate binding capacity was not found to be dependent on joint location. Der Einfluß der Gelenklokalisation auf die Struktur menschlicher KnorpelproteoglykaneZusammenfassung: Pröteoglykanmonomere aus den Gelenkknorpeln der Knie, Hüfte und Schulter wurden bei 3 Probanden (21, 25 und 45 Jahre alt) isoliert und analysiert. Die Pröteoglykanmonomere der hoch gewichtsbelä$teten Knie-und Hüftgelenke erwiesen sich als kleiner als die der weniger gewichtsbelasteten Schultergelenke und hatten jeweils einen niedrigeren Chondroitinsulfatgehalt. Die Pröteoglykanmonomere der Kniegelenkknorpel zeigten intraindividuell jeweils den niedrigsten Anteil Chondroitin-4-sulfat. Eine Abhängigkeit der Hyalüronatbindungsfähigkeit von der Gelenklokalisation wurde nicht festgestellt. *) TÄs work contains parts of the doctoral thesis of sulphate-rich region and one-third to the keratan G. Pallasch.sulphate-rich region. The remaming one-third is de-

Unilateral hindpaw amputation causes bilateral articular cartilage remodeling of the rat hip joint

“…The foveal region of the Norm rats and the I-limb of the AmpCont rats had a more densely staining matrix than their corresponding edge regions. This finding correlates with previous biochemical findings that cartilage from regions habitually exposed to high loading possesses a higher PG content per unit area than cartilage from less stressed sites [Gurr et al, 1985;Slowman and Brandt, 19861. In contrast, the A-limb of the AmpCont animals had statistically identical PG staining in both the foveal and edge region because of increases in the edge region PG content (Fig. 5).…”

Increased interleukin 1β production of macrophages by proteoglycan fragments deriving from articular cartilagein vitro

“…The experiments were done with the adherent cell fraction (Uhlin-Hansen and Kolset, 1988) by incubation (3 days) in the presence and absence of proteoglycans, proteoglycan fragments, glycosaminoglycans and endotoxine. Proteoglycans were isolated from different pools of human articular cartilage (about 70 g/pool) by extraction with a 4 tool/1 guanidinium hydrochloride solution followed by density gradient ultracentrifugation under associative and dissociative conditions according to Hascall and Kimura (1982) as reported earlier (Gurr et al, 1985). Characterisation by agarose/polyacrylamide gel electrophoresis of the isolated proteoglycans demonstrated one band in the position of large aggregating proteoglycans (PG LA 1/2, according to Heinegard's nomenclature).…”

“…This procedure resulted in a 23% decrease of the protein content and an increased mobility in gel electrophoresis. Pure fractions of glycosaminoglycans (chondroitin sulphate, dermatan sulphate, keratan sulphate and hyaluronate) were prepared from different sources as described elsewhere (Gurr et al, 1985). Endotoxine was purchased by Sigma Biochemicals (Miinchen, FRG).…”

Cartilage destruction mechanisms: initial changes in the proteoglycan pattern in Erysipelas arthritis of pigsin vivo and chondrocyte repair reactionin vitro

“…Isolation and analysis of proteoglycans and glycosaminoglycans was performed as described earlier [3]. Chondrocytes were isolated from healthy human articular cartilage (age of donor: 1,4 and 19 years) and cultivated in agarose gel as described elsewhere [4].…”