JOINT DESTRUCTION IN ARTHRITIS: METALLOPROTEINASES IN THE SPOTLIGHT CONSTANCE E . BRINCKERHOFF The erosion of connective tissue (cartilage, tendon, and bone) that accompanies both rheumatoid arthritis (RA) and osteoarthritis (OA) is, unfortunately, well known to physicians and patients alike. This destruction is mediated largely by collagenase and stromelysin, enzymes that are produced by the synovial fibroblasts (1). Collagenase is rate limiting in collagen degradation, while stromelysin degrades noncollagen proteins, e.g., laminin, fibronectin, and proteoglycans. Both enzymes belong to the gene family of metalloproteinases, which comprises at least 10 members (2). All metalloproteinases are active at neutral pH, contain zinc as an integral part of their structure, require Ca++ for activity, and are inhibited by tissue inhibitor of metalloproteinases (TIMP). Thus, TIMP, also a product of synovial fibroblasts, provides a potential mechanism for controlling degradation of the extracellular matrix, but its actual role in modulating disease has been debated. Until now, most of our information on the biochemical and biologic features of these enzymes has been derived from in vitro studies utilizing either From the Department of Medicine and the Department of Biochemistry, Dartmouth Medical School, Hanover, New Hampshire. Supported by NIH grant AR-26599 and by grants from the
Arthritis & Rheumatology – Wiley
Published: Oct 7, 1991
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