Identification of a second human retinoic acid receptor View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1988-04

AUTHORS

Nigel Brand, Martin Petkovich, Andrée Krust, Pierre Chambon, Hugues de Thé, Agnès Marchio, Pierre Tiollais, Anne Dejean

ABSTRACT

We have previously described a human complementary DNA that encodes a novel protein which is homologous to members of the steroid/thyroid nuclear receptor multigene family1. This novel protein (hap for hepatoma) exhibits strong homology with the human retinoic acid receptor (RAR)1,2 which has been recently characterized2,3. To test the possibility that the hap protein might also be a retinoid receptor, a chimaeric receptor was created by replacing the putative DNA binding domain of hap with that of the human oestrogen receptor (ER). The resulting hap-ER chimaera was then tested for its ability to trans-activate an oestrogen-responsive reporter gene (vit–tk–CAT) in the presence of possible receptor ligands. Here we show that retinoic acid (RA) at physiological concentrations is effective in inducing the expression of this reporter gene by the hap-ER chimaeric receptor. This demonstrates the existence of two human retinoic acid receptors designated RAR-α and RAR-β. More... »

PAGES

850-853

Journal

TITLE

Nature

ISSUE

6167

VOLUME

332

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/332850a0

    DOI

    http://dx.doi.org/10.1038/332850a0

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1014576456

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/2833708


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