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Alkaline phosphatase activity in cultured meningioma cells

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Summary

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 byl-homoarginine, levamisole, and l-bromotetramisole, but unaffected byl-phenylalanine andl-phenylalanylglycylglycine. 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.

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Takahara, N., Herz, F. & Hirano, A. Alkaline phosphatase activity in cultured meningioma cells. Acta Neuropathol 57, 45–50 (1982). https://doi.org/10.1007/BF00688876

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