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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
We present here a family with a clinical phenotype resembling Marfan syndrome (MFS), and displaying joint contracture and episodes of knee joint effusions, but lacking the cardiovascular features of the syndrome. The phenotype of this family represents a unique mixture of connective tissue symptoms, some of which are found in classical MFS and some of which are typical of dominant ectopia lentis.
Objective. Bone sialoprotein (BSP) was quantified in synovial fluids and sera from rheumatoid arthritis (RA) patients to elucidate whether its release from bone relates to the degree of joint tissue destruction. Osteocalcin was assayed for comparison. Methods. BSP and osteocalcin levels were determined by immunoassays of knee synovial fluids and of sera from RA patients who were selected on the
