Regulation of alkaline phosphatase expression in human choriocarcinoma cell lines.

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Abstract
The coincident expression of 2 structurally distinct isoenzymes of human alkaline phosphatase was demonstrated in 2 independently derived gestational choriocarcinoma cell lines [BeWo and JEG-3]. These proteins have enzymatic, antigenic and physical-chemical properties resembling those of isoenzymes from term placenta and adult liver. The regulation of these isoenzymes was studied during the exposure of both cell lines to 5-bromodeoxyuridine and dibutyryl cyclic AMP. The responses of the alkaline phosphatase isoenzymes to these agents were compared with the response of another protein phenotypic to placenta, the .alpha. subunit of chorionic gonadotropin. The separate structural genes coding for placental and liver alkaline phosphatases apparently are regulated in a noncoordinate fashion. Both alkaline phosphatase genes respond independently of the .alpha. subunit. The induction of the placental type isoenzyme occurs via at least 2 independent pathways.

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