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J Witter

Publications and source records attributed to J Witter.

4 recordsLinked to original sources
PubMed1990

Inflammation and cartilage metabolism in rheumatoid arthritis. Studies of the blood markers hyaluronic acid, orosomucoid, and keratan sulfate.

Single analyses of peripheral blood of rheumatoid arthritis (RA) patients showed a significant reduction in the mean value for keratan sulfate (KS) compared with that in control subjects, but the mean value for orosomucoid (OM) was elevated compared with that in control subjects. Some RA patients displayed highly elevated levels of hyaluronic acid (HA), while others exhibited normal levels. There was a significant inverse correlation between OM and KS content in RA patients, as well as a direct correlation between HA and OM. In longitudinal studies of RA patients, parallel changes in OM and HA and inverse changes between KS and OM or HA were commonly observed. Clinical analyses revealed that there was an inverse correlation between KS and morning stiffness, and direct correlations between the number of tender joints and HA, and between HA or the erythrocyte sedimentation rate and the number of joints with effusions. The reason(s) for the inverse correlation between KS and OM as an index of systemic inflammation remains to be established. Circulating HA represents an index of joint inflammation, for which a marker has not been previously available.

Adult↗
PubMed1987

The immunologic detection and characterization of cartilage proteoglycan degradation products in synovial fluids of patients with arthritis.

Antibodies were used in radioimmunoassays with gel chromatography to detect the hyaluronic acid-binding region, core protein, and keratan sulfate of human cartilage proteoglycan in the synovial fluids of patients with rheumatoid arthritis, juvenile rheumatoid arthritis, and osteoarthritis. All fluids contained proteoglycan that was mainly included on Sepharose CL-4B; this result indicates cleavage of proteoglycan (which is normally excluded). The hyaluronic acid-binding region was the smallest and most commonly detected fragment. It was relatively free of keratan sulfate and core protein, and it could sometimes bind to hyaluronic acid. Other larger fragments containing core protein and/or keratan sulfate were detected in every fluid.

Aggrecans↗
PubMed1987

Immunodetection and characterization of the degradation of cartilage proteoglycans in vitro and in vivo.

The large aggregating cartilage proteoglycans can be detected immunologically using antibodies directed against the hyaluronic acid-binding region, core protein, keratan sulfate, chondroitin sulfate, and hyaluronic acid. With radioimmunoassays we have detected proteoglycans released from adult human articular cartilage in vitro and in vivo. In vitro cleavage appears to occur mainly adjacent to the hyaluronic acid binding region with the release of the rest of the molecule. Two distinct populations have been observed, the larger of which is chondroitin sulfate-rich and the smaller keratan sulfate-rich. Although they are a little smaller and probably aggregate less with hyaluronic acid, these populations correspond in size and composition to two similar populations detected in situ in healthy adult human articular cartilage. In vivo studies of synovial fluid have revealed that the proteoglycan fragments are smaller and the most commonly detected fragment is the hyaluronic acid binding region. This suggests that in vivo further degradation occurs, probably due to degradation mediated by the inflamed synovium and polymorphonuclear leucocytes present in the synovial fluid of inflamed joints.

Binding Sites↗