Impairment of proteoglycan-collagen interaction in early experimental osteoarthrosis.

McDevitt, C A; Muir, Helen; Gilbertson, E M

doi:10.1136/ard.34.6.541

Cited by 6 publications

(3 citation statements)

References 4 publications

(3 reference statements)

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“…11). McDevitt et al (35) similarly observed decreased glucosamine contents of A1 fractions isolated from articular cartilage of dogs after the cruciate ligament had been transsectioned. The changes in the glucosamine contents can be attributed to an altered content of keratan sulfate, because separate quantitation of hyaluronic acid using a specific radioligand assay showed essentially equal amounts of hyaluronic acid in the samples ( Table 2).…”

Section: Proteoglycan Compositionmentioning

confidence: 82%

Proteoglycan alterations during developing experimental osteoarthritis in a novel hip joint model

Inerot

Heinegård

Olsson³

et al. 1991

Journal Orthopaedic Research

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Degenerative hip joint disease was induced in dogs by extra-articular surgery that created a condition that mimics hip dysplasia. Decreased acetabular coverage of the femoral head gave altered mechanical load, with ensuing cartilage degeneration. For comparison, degenerative knee joint disease was induced in other dogs by transection of the anterior cruciate ligament of the knee. The femoral head articular cartilage showed macroscopic signs of degeneration within a month. No macroscopical changes of synovitis were present. Chemical analysis of cartilage samples showed loss of proteoglycans. Guanidine hydrochloride extracts of the cartilage contained proteoglycan fragments that could be separated by equilibrium density gradient centrifugation in cesium chloride. The data indicate that proteoglycans are fragmented by proteolytic cleavage and lost from the cartilage. The proteoglycans remaining in the tissue are smaller and have lost the ability to aggregate with hyaluronic acid. Similarly, in experimental knee joint osteoarthritis, the proteoglycan content of the cartilage decreased. The structural changes of those proteoglycans remaining were of a different nature, with no changes in proteoglycan size or aggregation properties, possibly indicating that both degradation and repair took place in the knee articular cartilage and/or that fragments were rapidly lost from the tissue. This may follow from different surgical procedures, only the one used for the hip joint being extra-articular, or from the different anatomy and physiology of the hip joint and the knee joint.

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Section: Proteoglycan Compositionmentioning

confidence: 82%

Proteoglycan alterations during developing experimental osteoarthritis in a novel hip joint model

Inerot

Heinegård

Olsson³

et al. 1991

Journal Orthopaedic Research

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“…Cleavage of the collagen triple helix and subsequent disruption of the fibril structure results in loss of aggrecan complexes from the tissue (31,32). Cleavage of the aggrecan backbone itself leads to loss of part or all of the chondroitin sulfate domain, with consequent loss of swelling pressure and increase in load on the collagen network (33).…”

mentioning

confidence: 99%

Structural Analysis of Cartilage Proteoglycans and Glycoproteins Using Matrix-Assisted Laser Desorption/Ionization Time-of-Flight Mass Spectrometry

Zaia

Liu

Boynton

et al. 2000

Analytical Biochemistry

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“…These extended aggregates are constrained within a network of collagen fibres. The breakdown of this hierarchy appears to be one of the biochemical changes directly associated with osteoarthrosis (McDevitt & Muir, 1975). This conclusion has been reached from the observations that this disorder is often accompanied by both an increase in the quantity of unassociated proteoglycan and a disordering of the collagen network in the cartilage.…”

Section: Study Of Hyaluronic Acid Flexibility By Electric Birefringencementioning

confidence: 96%

Study of hyaluronic acid flexibility by electric birefringence

Trimm¹,

Jennings²

1983

Biochemical Journal

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Transient-electric-birefringence experiments were conducted on four samples of hyaluronic acid over the molecular-mass (M) range 5 x 10-4 x 106 in dilute aqueous solution. The geometrical, optical and electrical characteristics were monitored via the rotary relaxation times, optical-polarizability antisotropies and electrical polarizabilities respectively. Each indicates the molecular conformation to be consistent with some degree of rigidity at low M but that this does not persist at high M. The molecules do not become true random coils, but are best characterized in terms of a persistence length of 20nm or 20 disaccharide units.

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Impairment of proteoglycan-collagen interaction in early experimental osteoarthrosis.

Cited by 6 publications

References 4 publications

Proteoglycan alterations during developing experimental osteoarthritis in a novel hip joint model

Proteoglycan alterations during developing experimental osteoarthritis in a novel hip joint model

Structural Analysis of Cartilage Proteoglycans and Glycoproteins Using Matrix-Assisted Laser Desorption/Ionization Time-of-Flight Mass Spectrometry

Study of hyaluronic acid flexibility by electric birefringence

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