Abstract
Using vitamin D-resistant New World primates as model of natural diversity for sterol/steroid action and metabolism, two families of novel intracellular vitamin D regulatory proteins have been discovered and their human homologs elucidated. The first family of proteins, heterogeneous nuclear ribonucleoproteins (hnRNPs), initially considered to function only as pre-mRNA-interacting proteins, have been demonstrated to be potent cis-acting, trans-dominant regulators of vitamin D hormone-driven gene transactivation. The second group of proteins bind 25-hydroxylated vitamin D metabolites. Their overexpression increases vitamin D receptor (VDR)-directed target gene expression. We found that these intracellular vitamin D binding proteins (IDBPs) are homologous to proteins in the heat shock protein-70 family. Our ongoing studies indicate directly or indirectly through a series of protein interactions that the IDBPs interact with hydroxylated vitamin D metabolites and facilitate their intracellular targeting. (C) 2004 Elsevier Ltd. All rights reserved.
Original language | English |
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Pages (from-to) | 461-465 |
Number of pages | 5 |
Journal | The Journal of Steroid Biochemistry and Molecular Biology |
Volume | 89-90 |
Issue number | 1-5 |
DOIs | |
Publication status | Published - 1 May 2004 |
Keywords
- heat shock proteins
- traffic
- binding proteins
- heterogeneous nuclear ribonucleoproteins
- metabolism
- resistance
- receptors
- vitamin D
- transcription