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PubMedDate not supplied

The effect of synovial tissue on the breakdown of articular cartilage in organ culture.

UNLABELLED: Living (pig) cartilage in contact with synovium lost both proteoglycan and collagen and sometimes became reduced to a mass of fibroblast-like chondrocytes without matrix; dead cartilage lost proteoglycan but less collagen. Similar changes appeared in living cartilage grown at a distance from the synovium but in the same dish; dead cartilage was unaffected. CONCLUSION: the synovium has a) a direct, presumably enzymatic action on cartilage matrix and b) an indirect effect mediated through the chondrocytes.

Animals↗
PubMedDate not supplied

Antigen-induced arthritis. Decreased proteoglycan content and inhibition of proteoglycan synthesis in articular cartilage.

An arthritis was induced in rabbits immunized with human serum albumin by injection of antigen into the hind knee joint. Histological changes in the synovial membrane and an increase in polymorphonuclear granulocytes in the synovial fluid indicated an inflammatory response similar to that described with fibrin as antigen (1). The arthritis was accompanied by no significant change in the collagen content, but a marked decrease in the proteoglycan content of the cartilage was noted. Cartilage from inflamed joints generally exhibited a decreased ability to synthesize proteoglycan in vitro.

Animals↗
PubMedDate not supplied

Effects of diphosphonates on glycosaminoglycan synthesis and proteoglycan aggregation in normal adult articular cartilage.

The effects of disodium ethane-1-hydroxy-1,1-diphosphonate (EHDP) and disodium dichloromethylene diphosphonate (Cl2MDP) on glycosaminoglycan synthesis and macromolecular organization of proteoglycans have been examined in normal adult canine cartilage. One to 500 micron of either compound produced reversible inhibition of glycosaminoglycan synthesis to about 70% of control levels, whereas lower concentrations had no effect. Based on Sephadex G-200 chromatography, the average hydrodynamic size of glycosaminoglycans in diphosphonate-treated cartilage was similar to that of those in control cartilage. In most cases proteoglycan aggregates from diphosphonate-treated cartilage were smaller in hydrodynamic size than those from control cartilage, as judged by Sepharose 2B elution profiles. The size of purified proteoglycan subunits, obtained after dissociation of the aggregates with 4 M guanidinium chloride or after incubation of the aggregates with hyaluronic acid beta1 leads to 3 hydrolase, was not affected by the diphosphonates. Furthermore, proteoglycans from diphosphonate-treated cartilage did not interact in vitro with hyaluronic acid, suggesting that diminished proteoglycan aggregation may have resulted from an abnormality in the hyaluronate-binding region of the proteoglycan core protein.

Animals↗
PubMed1980

Antigen-induced arthritis. Studies on the inhibition of proteoglycan synthesis observed in articular cartilage during short-term joint inflammation.

During the acute phase of antigen-induced arthritis, cartilage was obtained from five different sites within the joint, and chondrocyte activity was assessed by autoradiography of sections labeled with 35S-sulfate. There was a marked inhibition of chondrocyte proteoglycan synthesis in all weight-bearing areas; in addition, the complete superficial layer of cells and many mid-zone cells in these areas were completely inactive. Electron microscopy showed that the inactive surface cells had degenerated completely, and that many mid-zone cells contained an accumulation of intracytoplasmic filaments and were depleted in biosynthetic organelles. A biochemical study of the inhibition showed that: 1) the incorporation of 35S-sulfate and 3H-acetate into glycosaminoglycans was inhibited to a similar extent; 2) the inhibition of glycosaminoglycan synthesis could not be reversed either by the addition of benzyl-beta-D-xyloside to incubations or by maintenance of the cartilage in organ culture for 6 days; 3) the inhibited chondrocytes exhibited a decreased ability to secrete proteoglycans into the extracellular fraction of the cartilage.

Animals↗
PubMed1982

Articular cartilage atrophy in lower limb amputees.

A retrospective and radiologic survey of the hips of 53 above-knee amputees showed that none of these hips was normal. Osteoporosis was present in all subjects, and cartilage thickness was reduced in 27 cases. This reduced thickness was inversely correlated with stump length, since it occurred in 11 of 13 upper-third amputees, but in none of 10 lower-third amputees. The mechanisms of cartilage atrophy are discussed.

Adult↗
PubMed1983

Collagenolytic activity and collagen matrix breakdown of the articular cartilage in the Pond-Nuki dog model of osteoarthritis.

Recent reports on the Pond-Nuki model of osteoarthritis in the dog have provided evidence for partial disruption of the collagen network. The possibility of collagenase involvement in these localized changes was studied. Animals were killed 2, 4, 8, and 12 weeks after surgery. The left knee served as a sham-operated control. Cartilages from femoral condyles were processed for light and electron microscopy and assayed for collagenolytic activity by a direct tissue assay, based on the measurement of digestion of endogenous cartilage collagen. Animals killed at 2 and 4 weeks showed fibrillation and mild erosion of femoral condyles, which usually progressed to ulceration by 8 and 12 weeks. Electron microscopy demonstrated fiber disruption of the mid-zone perilacunar collagen as early as 2 weeks after the operation. Total collagenolytic activity, measured after activation by aminophenylmercuric acetate, was significantly higher in decreased cartilage than in controls of 2, 4, and 8 weeks; the peak value was at 4 weeks. Collagenase was shown, by its specific action on type I collagen, to be present at 2 and 4 weeks; however, other metalloproteases may also contribute to the digestion. The correlation between increased collagenolytic activity and the early osteoarthritic changes in cartilage suggests a role of this enzyme activity in the disease process.

Animals↗
PubMed1984

Neutral proteases capable of proteoglycan digesting activity in osteoarthritic and normal human articular cartilage.

Proteases have been postulated to account for the progressive disappearance of matrix proteoglycans in osteoarthritic (OA) cartilage. The digestion of endogenous proteoglycans by neutral proteases in human OA cartilage homogenates has been measured and compared with that of normal age-matched controls. Cartilage was obtained from 16 patients at the time of knee arthroplasty and from 7 accident victims. Tissue blocks were cut from the tibial plateau; part was used for histologic grading of the severity of OA and part was homogenized for the quantification of neutral metallo- and serine protease activities, based on the release of digested products from endogenous proteoglycans. Total metalloprotease activity (latent plus active forms) was elevated 3- to 10-fold in all diseased cartilage. This elevation was already significant in mild disease, but was greatest in samples of moderate to severe disease. The active form of the enzyme was highest at the center of erosions and decreased in the margins of the plateau. The digestion of proteoglycans, as distinct from their mere release from the tissue, was demonstrated by chromatography on Sepharose-CL2B and by large pore electrophoresis. Serine protease activity on proteoglycans was much lower than that of metalloprotease. The mean activity was highest in mild disease and declined in the severe disease samples, but the difference between these 2 groups and the controls was not statistically significant. The results of this study are consistent with the hypothesis that the neutral metalloproteases of cartilage are involved in the degradation of proteoglycans in osteoarthritis.

Adult↗
PubMed1988

An enzymatically induced structural transformation in articular cartilage. Its significance with respect to matrix breakdown.

It was demonstrated in this study that the 3-dimensional, "pseudo-random" architecture of collagen in the general matrix of normal cartilage can be transformed enzymatically into a radial array of fibril aggregates or fibers. By first degrading the proteoglycans and then attacking the collagen, it is possible to produce a collagenous structure almost identical to that observed in matrices exhibiting both nonprogressive softening and osteoarthritic changes, and in matrices subjected to dynamic overloading. This structural transformation is explained as a breakdown in the fibril interlinking system.

Animals↗
PubMed1990

Osteoarthritis-related changes in human articular cartilage. An immunologic study.

We report the use of immunologic methods for detecting specific alterations in human osteoarthritic cartilage. Monoclonal antibodies with specificities for proteoglycans and link proteins have been used to define immunogenic sites in these molecules. We have identified 1 site in the protein core, 1 site in the link proteins, and another site that is common to both proteoglycan and link proteins, which are not modified in osteoarthritic cartilage. In addition, an antigenic determinant in link proteins that is altered in osteoarthritic cartilage has been identified. These results suggest that the structure of the ternary complex (hyaluronic acid binding region-link proteins-hyaluronic acid) could be altered in osteoarthritic cartilage. These modifications may be due to a genetic defect or to partial enzymatic degradation of these sites.

Aged↗
PubMed1990

Interleukin-1-induced interleukin-6 is required for the inhibition of proteoglycan synthesis by interleukin-1 in human articular cartilage.

Cartilage from normal controls, patients with osteoarthritis, and patients with rheumatoid arthritis produced no interleukin-6 (IL-6) in culture. However, IL-1 induced massive production of IL-6 (up to 135 ng/ml) in cartilage from all 3 sources, in a dose-dependent manner (in some cases, a peak value was reached). The levels of induced IL-6 were similar to those found in rheumatoid arthritis synovial fluid. At IL-1 concentrations that induced almost complete inhibition of proteoglycan (PG) synthesis, IL-6 production could still be increased considerably. Exogenous IL-6 inhibited PG synthesis by up to 25%. IL-1-induced inhibition of PG synthesis was reversed by antibodies against recombinant human IL-6. These results suggest that IL-6 is required for the IL-1-induced inhibition of PG synthesis.

Adult↗
PubMed1991

Chondrons from articular cartilage. III. Morphologic changes in the cellular microenvironment of chondrons isolated from osteoarthritic cartilage.

Chondrons were isolated from human and canine osteoarthritic cartilage using low-speed homogenization techniques. Changes in chondron morphology were evaluated using differential interference-contrast microscopy, phase-contrast microscopy, and histochemical and ultrastructural methods. Chondrocyte viability was assessed using fluorescein diacetate staining, and chondron metabolism was investigated using autoradiography. The results suggest that initial changes in the collagen and proteoglycan distribution within the chondron are followed by chondrocyte proliferation to form clusters. These techniques offer the potential to study cell matrix interactions in degenerative osteoarthritis.

Aged↗