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Modulation of alkaline phosphatase activity in KB cells by hyperosmolality and prednisolone: Effect on enzyme inhibition by phosphate

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Summary

A striking reduction in alkaline phosphatase activity occurs when KB cells (originally derived from a human nasopharyngeal carcinoma) are grown in hyperosmolar media and/or with prednisolone. This reduction is accompanied by the transition of the activity from predominantly heat-labile to heat-stable and by changes in susceptibility to inhibition by inorganic phosphate. Cell multiplication is required for these effects. The alkaline phosphatase of control cultures is significantly less sensitive to inhibition than the enzyme of KB cells with reduced activity. This quantitative difference is correlated with enzyme thermostability. To obtain the same degree of inhibition, greater amounts of phosphate are required for the heat-stable activity than for the heat-labile activity.

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Author notes

  1. Fritz Herz

    Present address: Department of Pathology, Montefiore Hospital and Medical Center, Albert Einstein College of Medicine, 111 East 210th Street, 10467, Bronx, New York

Authors and Affiliations

  1. Department of Pediatrics, Sinai Hospital, 21215, Baltimore, Maryland

    Fritz Herz

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  1. Fritz Herz
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This work was supported in part by Grant 5-SO1-RR05478-10 from the National Institutes of Health and was initiated at Sinai Hospital, Baltimore, Md

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Herz, F. Modulation of alkaline phosphatase activity in KB cells by hyperosmolality and prednisolone: Effect on enzyme inhibition by phosphate. In Vitro 10, 63–69 (1974). https://doi.org/10.1007/BF02615339

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