Response element binding proteins and intracellular vitamin D binding proteins: novel regulators of vitamin D trafficking, action and metabolism

Research output: Contribution to journalArticle


  • JS Adams
  • H Chen
  • R Chun
  • MA Gacad
  • C Encinas
  • SY Ren
  • L Nguyen
  • SX Wu
  • J Barsony


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 languageEnglish
Pages (from-to)461-465
Number of pages5
JournalThe Journal of Steroid Biochemistry and Molecular Biology
Issue number1-5
Publication statusPublished - 1 May 2004


  • heat shock proteins, traffic, binding proteins, heterogeneous nuclear ribonucleoproteins, metabolism, resistance, receptors, vitamin D, transcription