Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.31 (beta-glucuronidase)
 7,680 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The levels of six lysosomal enzymes (acid phosphatase, beta-acetylglucosaminidase, cathepsin D, beta-galactosidase, arylsulfatase A, and beta-glucuronidase) and four neutral and alkaline hydrolases (esterase, inorganic phyrophosphatase, alkaline phosphatase, and 5'-nucleotidase) were measured in osteoarthritic, rheumatoid and control synovia. All enzyme levels in diseased synovium except esterase values in osteoarthritis were significantly elevated compared with controls. The mean values of the group of acid hydrolases and the group of neutral and alkaline hydrolases in osteoarthritic synovia were 1.9- and 2.0-fold greater than those of control specimens. In rheumatoid synovia, the values were 4.2- and 4.5 fold greater than control for the same enzymes. Levels in rheumatoid synovia were significantly higher than those in osteoarthritic synovia with the exception of 5'-nucleotidase. Only a limited correlation between the extents of inflammation present in the synovia and the levels of a lysosomal marker enzyme (cathepsin D) was observed. These results demonstrate that whatever the mechanism, increased levels of acid hydrolases as well as certain neutral and alkaline hydrolases are present in osteoarthritic and rheumatoid synovia, and these enzymes are probably contained in the synovial lining cells.
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PMID:Acid, neutral, and alkaline hydrolases in arthritic synovium. 0 9

Lysozyme and lactoferrin levels were measured in 71 synovial fluids (SF) of patients with traumatic effusions, osteoarthritis, rheumatoid arthritis, pseudogout, septic arthritis, and gout, as well as in 91 synovial fluids graded according to their neutrophil count. Elevated lysozyme levels were found in all the inflammatory arthritides and also in osteoarthritis. Lactoferrin levels were not increased in osteoarthritis but displayed a close correlation to the extent of the inflammatory response as judged by SF neutrophilia. The ratio of lysozyme to lactoferrin decreased progressively with increasing SF neutrophilia. In vitro experiments showed that lactoferrin is released from neutrophils isochronously with lysozyme and beta-glucuronidase. Lactoferrin was not found in hyaline cartilage, a tissue known to contain lysozyme. These results are consistent with belief that SF lysozyme has a major derivation from both cartilage and neutrophils, and that lactoferrin arises only from neutrophils. These findings indicate that the simultaneous measurement of lysozyme and lactoferrin provides a potentially useful index of both joint inflammation and cartilage degradation.
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PMID:Lactoferrin and lysozyme levels in synovial fluid: differential indices of articular inflammation and degradation. 83 40

Tissue kallikrein is an enzyme that forms the vasoactive peptide kallidin from an endogenous substrate L-kininogen. Tissue kallikrein has been identified in joint fluids and in inflammatory infiltrates within synovial membranes. It is suggested that tissue kallikrein and kinins have an important role in synovitis and joint damage. Immunoreactive tissue kallikrein and amidase activity were both measured in the synovial fluid of 24 patients with rheumatoid arthritis (RA) and 12 with osteoarthritis (OA). Active enzyme concentrations were higher in RA than in OA and correlated well with the lysosomal enzymes beta-glucuronidase and lactate dehydrogenase. Both total immunoreactive tissue kallikrein and the proenzyme values were similar in RA and OA. Tissue kallikrein was localised by immunocytochemistry to the polymorphonuclear leucocytes present in the synovial fluid and membranes of patients with RA.
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PMID:A tissue kallikrein in the synovial fluid of patients with rheumatoid arthritis. 264 23

Phospholipase A2 (PLA2) activity was found in the sera and synovial fluids (SF) in rheumatoid arthritis (RA) and osteoarthritis (OA). PLA2 activity in RA SF was 6158 +/- 549 (SEM) U/ml (n = 48) and in RA sera 554 +/- 175 U/ml (normal sera-115 +/- 12 U/ml). In OA SF PLA2 activity was 5069 +/- 542 U/ml (n = 28), and in OA sera 268 +/- 55 U/ml. There was no significant difference between SF PLA2 activity in RA and OA. PLA2 activity in SF did not correlate with muramidase (lysozyme), beta-glucuronidase, total protein or white cell count, which were all significantly higher in RA SF than OA. A positive correlation between PLA2 in SF and matched sera was found in both RA and OA. It may be concluded that significant elevation of extracellular PLA2 occurs in both RA and OA, especially in the SF. The fact that high PLA2 did not correlate with other enzymes such as lysozyme and beta-glucuronidase, which are usually high in RA and low in OA SF, may mean that the handling of PLA2 in the joint space is different from other enzymes.
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PMID:Phospholipase A2 activity in sera and synovial fluids in rheumatoid arthritis and osteoarthritis. Its possible role as a proinflammatory enzyme. 403

Chondrocytes from adult and immature articular cartilage were separated on the basis of size by rate-zonal centrifugation in a Ficoll density gradient. Lysozomal enzyme activity (acid phosphatase and beta-glucuronidase) was determined in gradient fractions containing chondrocytes of different sizes. Acid phosphatase and beta-glucuronidase activity in mature articular cartilage was greatly increased in small sized cells, located in the superficial tangential zone. In cells from immature calf articular cartilage, there were two peaks of increased activity, on in the superficial tangential zone, the other in the deep radial zone, close to the cartilage bone junction. It is speculated that the small surface cells, with thier high degradative enzyme levels, may explain why the osteoarthritis process starts at the surface.
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PMID:Degradative enzyme activity in isolated chondrocyte populations. 706

Severance of the anterior cruciate ligament in the knees of mature beagles caused instability and resulted in the slow onset of changes comparable to those present in human osteoarthritis (OA). Heightened cellular activities were reflected in increased levels of arylsulfatase, acid phosphatase, and beta-glucuronidase in the articular cartilage. Similar increases in these lysosomal enzyme activities were found in the synovial fluid of the operated joints. Dietary supplementation with vitamin C resulted in increased serum protein content and increased cartilage formation, although ascorbate had no effect on enzyme activities. The early stages of OA in mature beagles, therefore, were characterized by interference with normal chondrocyte metabolism which resulted in staggered elevation of different lysosomal enzymes.
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PMID:Metabolic response during early stages of surgically-induced osteoarthritis in mature beagles. 720 21

beta-Glycosidases (N-acetyl-beta-glucosaminidase, N-acetyl-beta-galactosaminidase, beta-glucuronidase) were assayed in temporomandibular joint (TMJ) synovial fluid obtained from 23 patients with closed lock TMJ internal derangement (ID), four with closed-lock TMJ osteoarthritis (OA), and 13 with normal controls (N). Synovial fluid was collected from the upper joint space after injecting 1.5 ml of 1% lidocaine three times. The specific activity of N-acetyl-beta-glucosaminidase increased significantly both with ID (p < 0.01) and with OA (p < 0.001), along with increases in the activity of N-acetyl-beta-galactosaminidase (p < 0.05 with ID and p < 0.01 with OA) and in beta-glucuronidase (p < 0.05 both with ID and OA). The N-acetyl-beta-glucosaminidase activity with OA was also significantly higher (p < 0.001) than with ID. These findings suggest that N-acetyl-beta-glucosaminidase activity in the TMJ synovial fluid reflects the degree of TMJ dysfunction.
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PMID:Changes in synovial fluid N-acetyl-beta-glucosaminidase activity in the human temporomandibular joint with dysfunction. 818 2