Temporomandibular joint syndrome
The expression of a chondroitin-sulfate epitope (epitope 846) in OA cartilage, that is otherwise only present in fetal and neonatal cartilage, provides further evidence that OA is a distinct pathologic process. temporomandibular joint syndrome Evaluation of psoriatic arthritis. A final but important distinction is that degradative enzyme activity is increased in OA, but not in normal aging cartilage. (top of page) What molecules are responsible for degrading cartilage matrix? The primary enzymes responsible for the degradation of cartilage are the matrix metalloproteinases (MMPs) (slide). These enzymes are secreted by both synovial cells and chondrocytes and are categorized into three general categories: a) collagenases; b) stromelysins; and, c) gelatinases. temporomandibular joint syndrome Finger pain. Under normal conditions, MMP synthesis and activation are tightly regulated at several levels. They are secreted as inactive proenzymes that require enzymatic cleavage in order to become activated. Once activated, MMPs become susceptible to the plasma-derived MMP inhibitor, alpha-2-macroglobulin, and to tissue inhibitors of MMPs (TIMPs) that are also secreted by synovial cells and chondrocytes. temporomandibular joint syndrome Temporomandibular joint syndrome. In OA, synthesis of MMPs is greatly enhanced and the available inhibitors are overwhelmed, resulting in net degradation. Interestingly, stromelysin can serve as an activator for its own proenzyme, as well as for procollagenase and prostromelysin, thus creating a positive feedback loop of proMMP activation in cartilage. (top of page) What factor(s) is responsible for inducing metalloprotease synthesis? One candidate is interleukin-1 (IL-1).
Temporomandibular joint syndrome
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