Placental Alkaline Phosphatase Isoenzyme Expression by the Non-HeLa DoT Cervical-carcinoma Cell Line

Overview

Journal Biochem J

Specialty Biochemistry

Date 1981 Dec 15

PMID 7342975

Citations 2

Authors

R H Kottel

W H FISHMAN

Affiliations

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Abstract

Expression of the oncodevelopmental protein, placental alkaline phosphatase, was observed in DoT cells, an epidermoid cell line derived from cervical carcinoma. Under normal conditions of growth in vitro, biochemical inhibition, cytochemical and immunological studies revealed that these cells express the term-placental (Regan) isoenzyme. Thus alkaline phosphatase activity was observed to be heat-stable and inhibited by L-phenylalanine. These properties, supported by immunoelectrophoretic analysis using antisera specific for liver, intestinal or term-placental isoenzymes, identified the isoenzyme as placental type. DoT cells treated with prednisolone (1 microgram/ml) increased total alkaline phosphatase specific activity. This activity was also identified as term-placental phosphatase isoenzyme. On the other hand, treatment of the same cells with sodium butyrate (1 mM) did not induce increased activity of the term-placental isoenzyme, an unexpected observation. As a result of these studies, DoT cells are proposed as a representative cell line for studies of the regulation of oncodevelopmental gene expression in human tumour cells of cervical origin.

Citing Articles

Microsomal and lysosomal enzymes of triacylglycerol metabolism in rat placenta.

Coleman R, Haynes E Biochem J. 1984; 217(2):391-7.

PMID: 6696738 PMC: 1153229. DOI: 10.1042/bj2170391.

Alkaline phosphatase isozymes in cultured human cancer cells.

Herz F Experientia. 1985; 41(11):1357-61.

PMID: 3905429 DOI: 10.1007/BF01949989.

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