Identification of the Porcine Intestinal Accessory Factor that Enables DNA Sequence Recognition by Vitamin D Receptor

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 92; no. 7; pp. 2795 - 2799
• Main Authors: Munder, Michael, Herzberg, Ian M., Zierold, Claudia, Moss, Valerie E., Hanson, Kris, Clagett-Dame, Margaret, DeLuca, Hector F.
• Format: Journal Article
• Language: English
• Published: United States National Academy of Sciences of the United States of America 28.03.1995; National Acad Sciences; National Academy of Sciences
• Subjects: Animals; Antibodies; Base Sequence; Biochemistry; Cell Nucleus - metabolism; Chromatography; Chromatography, Affinity; Cytochrome P-450 Enzyme System; DNA - chemistry; DNA - metabolism; DNA-Binding Proteins - metabolism; Gels; Hogs; Intestinal Mucosa - metabolism; Intestines; Mice; Molecular Sequence Data; Nuclear Proteins - isolation & purification; Nuclear Proteins - metabolism; Oligodeoxyribonucleotides; Osteocalcin - genetics; Osteocalcin - metabolism; Proteins; Rats; Reading Frames; Receptors; Receptors, Calcitriol - metabolism; Receptors, Retinoic Acid - immunology; Receptors, Retinoic Acid - metabolism; Resins; Response elements; Retinoic Acid Receptor gamma; Retinoid X Receptors; Steroid Hydroxylases - genetics; Swine; Transcription Factors - immunology; Tretinoin - metabolism; Vitamin D; Vitamin D3 24-Hydroxylase
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.92.7.2795

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.