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Progestin Regulation of Alkaline Phosphatase in the Human Breast Cancer Cell Line T47D¹

Institute of Chemistry, School of Medicine, University of Brescia, Brescia, Italy [D. D. L., A. A.], and Peralta Cancer Research Institute and Aeron Biotechnology, San Leandro, California 94578 [D. Z.]

In T47D breast cancer cell line, progestin (R5020) induces de novo synthesis of an alkaline phosphatase enzyme. Based on inhibitor profiles and antigenic specificity, it is apparent that this enzyme belongs to the class of membrane-associated tissue-unspecific alkaline phosphatases. Enzyme induction was uniquely specific to progestins and not altered by other steroid hormones or synthetic analogues. The progestin induction of the tissue-unspecific alkaline phosphatase was time and dose dependent. The protein synthesis inhibitor cycloheximide blocks the enzyme synthesis and tunicamycin blocks the enzyme activity, showing that the induction was new synthesis of protein in its complete glycosylated form and not activation of a preexisting enzyme. To our knowledge this is the first report of progesterone-induced expression of a tissue-unspecific alkaline phosphatase gene of such magnitude (about 30- to 100-fold) in a progesterone-responsive tissue.

¹ This work was partially supported by a contract (Proposal No. PL 910009) in framework of the Bridge Program, T-Projection Animal Cell Biology, of the Commission of the European Communities.

² To whom requests for reprints should be addressed.

Received 3/27/91. Accepted 6/ 4/91.

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