UMMS Affiliation

Program in Gene Function and Expression; Program in Molecular Medicine

Date

4-1-1993

Document Type

Article

Medical Subject Headings

Adenovirus E1A Proteins; Animals; Base Sequence; Binding Sites; Carrier Proteins; Chloramphenicol O-Acetyltransferase; Cyclic AMP Response Element-Binding Protein; Embryonal Carcinoma Stem Cells; Gene Expression; Mice; Molecular Sequence Data; Neoplastic Stem Cells; *Promoter Regions, Genetic; Receptors, Retinoic Acid; Recombinant Fusion Proteins; Transfection; Tretinoin; Tumor Cells, Cultured

Disciplines

Genetics and Genomics

Abstract

The retinoic acid (RA) receptor (RAR) beta 2 promoter is strongly activated by RA in embryonal carcinoma (EC) cells. We examined this activation in the P19 EC-derived END-2 cell line and in E1A-expressing counterparts and found strong RA-dependent RAR beta 2 promoter activation in the E1A-expressing cells, which was not observed in the parental cell line, indicating a possible role for E1A in RAR beta 2 activation. In transient transfection assays, E1A functioned as a coactivator of RA-dependent RAR beta 2 promoter activation and, moreover, was able to restore this activation in cells lacking RAR beta 2 activation. By deletion analysis, two regions in the RAR beta 2 promoter were identified that mediate the stimulatory effect of E1A: the RA response element and TATA box-containing region and a more up-stream region between -180 and -63, in which a cAMP response element-related motif was identified as a target element for E1A. In addition, determination of endogenous E1A-like activity by measuring E2A promoter activity in transient transfection assays in EC and differentiated cells revealed a correlation between RA-dependent RAR beta 2 promoter activation and the presence of this activity, suggesting an important role for the cellular equivalent of E1A in regulation of the RAR beta 2 promoter.

Rights and Permissions

Citation: Mol Endocrinol. 1993 Apr;7(4):604-15. Link to article on publisher's site

Comments

At the time of publication, Albertha J. Marian Walhout was not yet affiliated with the University of Massachusetts Medical School.

Related Resources

Link to Article in PubMed

PubMed ID

8389000

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