Calcitonin inhibits phospholipase A2 and collagenase activity of human osteoarthritic chondrocytes

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Calcitonin (CT) is a known potent inhibitor of bone resorption but its effect on cartilage enzymatic degradation has been incompletely studied. Salmon CT, at a concentration of 0, 0.1, 0.25, 0.5, 2.5 and 50 ng/ml, was added at 24 or 72 h to the culture medium of chondrocytes from human osteoarthritic hips and knees. The spontaneous collagenolytic activity, measured using a radiolabeled type II collagen, was inhibited by CT in a dose-dependent manner. However, CT had no effect on the total collagenolytic activity assayed after APMA activation. Stromelysin and plasmin activity, measured by degradation of casein and a synthetic substrate, were also unaffected by CT. Chondrocyte phospholipase A2 activity, assayed using a labeled specific substrate, was decreased by CT. Chondrocyte pre-incubation with CT significantly decreased the cell binding of labeled TNFα, but did not affect IL-1β cell binding. Attachment of chondrocytes on fibronectin was markedly stimulated by CT, while attachment to type II collagen was not. Significant effects were obtained using at least 2 or 5 ng/ml of CT. CT appears to decrease collagenolytic activity by decreasing its activation and/or increasing its inhibition by tissue inhibitors of metalloproteinases (TIMP). CT might act on osteoarthritic chondrocyte activation via mechanisms such as phospholipase A2 activity, human necrosis factor-α or fibronectin receptor expression.




Hellio, M. P., Peschard, M. J., Cohen, C., Richard, M., & Vignon, E. (1997). Calcitonin inhibits phospholipase A2 and collagenase activity of human osteoarthritic chondrocytes. Osteoarthritis and Cartilage, 5(2), 121–128.

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