Cartilage content of proteoglycans decreases early in induced degenerative hip joint disease. Remaining molecules show structural changes indicating fragmentation. Fragments lost from the articular cartilage are released to the synovial fluid, where they can be quantified by enzyme linked immunosorbent assay. Their amounts are related to the activity of the disease process.

The influence of synovial fluid and serum from patients with inflammatory joint disease on proteoglycan metabolism was studied in organ culture of bovine nasal cartilage. Proteoglycan biosynthesis, i.e. incorporation of [35S]-sulphate, was reduced after addition of synovial fluid from rheumatoid arthritis and reactive arthritis patients. Also some rheumatoid arthritis sera but no reactive arthriti

Synovial fluids from 6 of 12 patients with rheumatoid arthritis (RA) and from 3 of 11 patients with reactive arthritis contained measurable levels of tumor necrosis factor α (TNFα). Seven of 12 sera from RA patients contained TNFα, while only 1 of those from reactive arthritis patients was positive. Gamma-interferon was detected in the synovial fluids and sera of only the RA patients. Tumor necros

The concentrations of aminoterminal-type-III procollagen (procollagen N-) peptide, and of proteoglycans were measured in knee-joint synovial fluid and serum from patients with rheumatoid arthritis or reactive arthritis. All synovial fluids contained large amounts of intact propeptide. The synovial fluid: serum propeptide ratios were high, suggesting local propeptide liberation. A correlation was d

Analysis of human cartilage extracts by radioimmunoassay showed that the noncollagenous 148-kd cartilage matrix protein was present in extracts of tracheal cartilage but was undetectable in normal or arthritic joint cartilage, corroborating previous results with bovine cartilage samples. Concentrations of the protein in the circulation, as studied by radioimmunoassay, were greatly elevated in pati

We have previously shown synovial fluid (SF) proteoglycan concentrations to be sensitive markers of altered cartilage metabolism in arthritis. We determined the proteoglycan concentrations in sera and SF from 23 patients with juvenile chronic arthritis and in sera from 30 healthy children by a specific enzyme linked immunosorbent assay. In both groups of children, decreasing concentrations of prot

Asisted living (AL) technologies, enabled by technical advances such as the advent of the Internet of Things, are increasingly gaining importance in our aging society. This article discusses the potential of future high-accuracy localization systems as a key component of AL applications. Accurate location information can be tremendously useful to realize, e.g., behavioral monitoring, fall detectio

An early event in joint disease is a progressive destruction of the articular cartilage following degradation of matrix macromolecular constituents. The fragments thus formed are released into surrounding fluids by diffusion and can be detected and quantified by immunoassay. By using assays for macromolecules/fragments specific for cartilage, it is possible to monitor processes in a given articula

OBJECTIVE: To investigate whether fragmentation of proteoglycans in arthritis results in domains that have different levels of release from cartilage at different stages of the disease.METHODS: Two regions of the proteoglycan, the hyaluronan-binding region and the glycosaminoglycan-rich region of the core protein, were measured, by immunoassay, in knee joint synovial fluids of patients with rheuma

Cartilage oligomeric matrix protein (COMP) is a tissue specific non-collagenous matrix protein. We have developed an enzyme-linked immunosorbent assay for the detection of this protein in synovial fluid and serum. The protein has been quantified in these fluids in patients with rheumatoid arthritis (RA), reactive arthritis, juvenile chronic arthritis, osteoarthritis and in sera of control subjects