Identification of the Porcine Intestinal Accessory Factor that Enables DNA Sequence Recognition by Vitamin D Receptor
The nuclear accessory protein in porcine intestinal nuclear extracts that activates the binding of the vitamin D receptor to its vitamin D response elements has been highly purified. It contains a protein that binds 9-cis-[3H]retinoic acid, was detected on immunoblots with an anti-retinoid X recepto...
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Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1995-03, Vol.92 (7), p.2795-2799 |
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Sprache: | eng |
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Zusammenfassung: | The nuclear accessory protein in porcine intestinal nuclear extracts that activates the binding of the vitamin D receptor to its vitamin D response elements has been highly purified. It contains a protein that binds 9-cis-[3H]retinoic acid, was detected on immunoblots with an anti-retinoid X receptor (RXR) peptide antibody, and supports the binding of retinoic acid receptor γ to the retinoic acid receptor β gene response element. Most important, the two specific complexes formed by porcine nuclear extract with the vitamin D response elements from either the osteocalcin gene or the rat 24-hydroxylase gene are shifted to a larger complex by both an anti-vitamin D receptor antibody and an anti-RXR antibody, leaving no doubt that in vivo the nuclear accessory factor for the vitamin D receptor in the intestine is an RXR protein. |
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ISSN: | 0027-8424 1091-6490 |
DOI: | 10.1073/pnas.92.7.2795 |