Immunolocalisation of matrix metalloproteinase 3 (stromelysin) in rheumatoid synovioblasts (B cells): correlation with rheumatoid arthritis

Article Abstract:

Rheumatoid arthritis (RA) is an inflammatory joint disease characterized by stiffness, swelling, enlargement of the cartilage, and pain. In RA, inflammation of the synovial membrane which lines the joint causes destruction of the cartilage, bones, tendons, and ligaments, resulting in deformity and disability of the joints. Damage may result from mechanical factors, highly reactive molecules called free radicals, or enzymes that specifically break down proteins. Matrix metalloproteinases (MMPs) are enzymes manufactured by connective tissue; MMPs may play an important part in the joint destruction occurring in RA. This group of enzymes includes collagenase which breaks down the fiber-like protein collagen, MMP-2 or gelatinase, and MMP-3 or stromelysin. The production of these enzymes is activated by various factors released by lymphocytes, a type of immune cell. Stromelysin has been shown to degrade several proteins contained within the joint, including cartilage proteins and collagen, although its role in rheumatoid arthritis has not been demonstrated. Synovial tissue was obtained from nine patients with rheumatoid arthritis and was analyzed for the presence of stromelysin. The enzyme was detected in the synovial lining of RA patients but not in normal synovial membranes. Stromelysin is produced by cells that resemble synovioblasts or B cells. In addition, synovioblast production of stromelysin is stimulated by some unknown factor released by macrophages, cells that can ingest particles. (Consumer Summary produced by Reliance Medical Information, Inc.)

Causes of, Proteases

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Immunolocalisation studies on six matrix metalloproteinases and their inhibitors, TIMP-1 and TIMP-2, in synovia from patients with osteo- and rheumatoid arthritis

Article Abstract:

Stromelysin 1, an enzyme that can degrade several of the various proteins forming cartilage matrix, appears to be involved in arthritic diseases. Other families of connective tissue enzymes also appear to be involved. Samples were taken from the joint linings of diseased joints from seven rheumatoid arthritis patients and three osteoarthritis patients. Cells were cultured and assayed and slides were analyzed for the presence and location of stromelysin 1 and 2, matrilysin, gelatinases A and B, and enzyme inhibiting factors TIMP-1 and 2. Stromelysin 1 was found throughout the joint in all cases, both bound to connective tissue and within cells, but stromelysin 2 was not present. Collagenase, gelatinase A, and matrilysin were found only in rheumatic joints, and their regional distribution suggested that their synthesis was restricted in location and episodic in nature. TIMP-1, but not TIMP-2, was seen in five samples. All of these patients had been treated with anti-inflammatory drugs.

Protease inhibitors, Osteoarthritis

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Effects of induced mast cell activation on prostaglandin E and metalloproteinase production by rheumatoid synovial tissue in vitro

Article Abstract:

Mast cell activation in joint synovial tissue may be an important physiological component of rheumatoid arthritis. Mast cells store powerful substances which affect inflammation, blood vessel formation, tissue remodeling, and immune reactions. Researchers treated synovial tissue samples from rheumatoid arthritic joints with an antibody that induces mast cells to release their contents. Activated mast cells released significant amounts of tryptase and prostaglandin E2, but showed no consistent pattern of metalloproteinase release.

Prostaglandins E, Mast cells

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• Abstracts: Concentrations of glycosaminoglycans in synovial fluids and their relation with immunological and inflammatory mediators in rheumatoid arthritis

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