Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.36 (hyaluronidase)
 4,606 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A sandwich-binding protein assay to determine the concentration of hyaluronic acid (HA) in body fluids has been developed. In this method, a hyaluronic acid binding protein (HABP) was adsorbed to the surface of a solid phase, and HA bound to HABP on the solid phase was detected by biotin-conjugated HABP. The method could assay HA levels within 6 hours using precoated microwells with HABP. HA could be determined in the range of 2-500 micrograms/l by this method using 50 microliters of serum. Within-run precision (CV) was 5.2-10.2%. The specificity of HABP to HA was confirmed by the elimination of the reaction with treatment by hyaluronidase digestion. Serum HA levels (median; range) of patients with rheumatoid arthritis (34; 2-187 micrograms/l) were shown to be higher than those with osteoarthritis (1; 1-21 micrograms/ml) and healthy controls (2; 1-8 micrograms/ml). No correlation between levels of HA and rheumatoid factor was found. HA was demonstrated to be a potential diagnostic marker for rheumatoid arthritis, and this HABP assay could be useful for determination of HA in clinical laboratory tests.
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PMID:Assay of serum hyaluronic acid in clinical application. 247 93

A study was made of the possibilities of an individual approach to intraarticular administration of protease inhibitors, cytostatics and orgoteine in patients with rheumatoid arthritis (RA). The activity of hyaluronidase, superoxide dismutase, the level of rheumatoid factor and the phagocyte count in synovial fluid were examined. With regard to the results of synovial fluid analysis in 67 RA patients, contrykal, orgoteine or cyclophosphamide were administered intra-articularly (based on an individual approach) in addition to corticosteroid hormones. It has been shown that with the individual approach to intraarticular drug administration the number of repeated punctures of the joints decreased by 18.8% while the amount of glucocorticosteroid hormones administered was twice as reduced.
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PMID:[The possibilities of an individual approach to intra-articular drug administration in rheumatoid arthritis patients]. 262 40

Synovial fluid (SF) of 16 adult patients with rheumatoid arthritis (RA) and 9 children with juvenile rheumatoid arthritis (JRA) was investigated for the presence of hidden 19S IgM rheumatoid factor (RF). SF was incubated with 500 IU hyaluronidase/g of SF, dialyzed against acetate buffers at decreasing pH, centrifuged and subjected to chromatography on a Sephadex G-200 column. The resulting IgM-containing fraction of SF from 5 seropositive patients (3 adult RA, 2 JRA patients) demonstrated RF activity by the complement-dependent hemolytic assay. Hidden 19S IgM RF was not found in the IgM-containing fractions of SF from 13 adult seronegative RA patients. Hidden 19S IgM RF was shown in the IgM-containing fraction of SF in 4 of 7 children with seronegative JRA.
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PMID:Hidden 19S IgM rheumatoid factor in synovial fluid. 731 Jul 76

Spontaneous synovitis developed in the limb joints and rheumatoid factor-like component appeared in the sera of two rabbits from a pool 36 animals in the course of a long-term immunization with bovine nasal cartilage antigens. A single intra-articular injection of proteoglycan antigens regularly provoked a heavy synovitis and cartilage destruction irrespective of whether the booster injections were administered in physiological saline, or in Freund's complete adjuvant. The dose-dependent severity of arthritis suggested that the antibody titre against proteoglycan antigens played an important role in this mechanism. The synovial extract and synovial fluid of knee joints injected with proteoglycan antigens showed an increased enzyme activity concerning the four acid hydrolases (acid phosphatase, cathepsin D, hyaluronidase and beta-glucuronidase). The high activity of lysosomal acid hydrolases which persisted for several months can derange the molecular structure of proteoglycans of cartilage. The degraded proteoglycans may trigger autoimmune reactions, and the process eventually leads to chronic inflammation and joint destruction.
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PMID:Experimental arthritis produced by proteoglycan antigens in rabbits. 745 41