Because serum estrogen levels are associated with the presence of osteoarthritis, and cartilage tissue is known to contain estrogen receptors, it is of interest to determine the extent to which estrogen is biosynthesized and/or metabolized in cartilage tissue or isolated chondrocytes. In this preliminary study, using a sensitive assay method, estrogen synthetase (aromatase) was undetectable in articular cartilage or isolated chondrocytes in culture from immature female rabbits. However, estrogen metabolism, specifically estrogen 17 beta-hydroxysteroid dehydrogenase activity, was detected in homogenized cartilage tissue, and at substantially higher specific activities in freshly isolated chondrocytes. These fresh chondrocytes, assayed in culture without any exogenous cofactor, demonstrated a significantly higher activity for converting the weak estrogen, estrone, to the more potent estrogen, estradiol. Chondrocytes grown to confluence in culture had very low estrogen 17 beta-hydroxysteroid dehydrogenase specific activity. Homogenized cartilage tissue, tested only with added NADPH as cofactor, also showed a preference for estradiol as the principal product, but this may have been primarily due to the use of reduced cofactor. If subsequent experiments confirm the presence of estrogen 17 beta-hydroxysteroid dehydrogenase activity, and its preference for converting estrone into estradiol, in human cartilage tissue and chondrocytes, this could have substantial implications in the estrogen dependency of osteoarthritis.