The specific activity of alkaline phosphatase in cultured human meningioma cells varies over a relatively wide range. There is no correlation between the levels of activity and the histological type of meningioma from which the cultures were derived. The enzyme is heat-labile and is strongly inhibited by L-homoarginine, levamisole, and 1-bromotetramisole, but unaffected by L-phenylalanine and L-phenylalanyl-glycylglycine. These findings indicate that meningioma cells synthesize the liver/bone/kidney form of alkaline phosphatase. In contrast to cultures derived from pituitary adenomas, glioblastomas, and astrocytomas in which prednisolone and/or sodium butyrate elicit a manifold increase of alkaline phosphatase activity, with meningioma cells the hormone causes only a slight augmentation in specific activity, and the fatty acid is ineffective. As with other cells producing the liver/bone/kidney enzyme form, no increase in activity occurs in meningioma cells growing in hyperosmolar medium.