New mechanisms of regulation of the genomic actions of vitamin D in bone cells: interaction of the vitamin D receptor with non-classical response elements and with the multifunctional protein, calreticulin

Front Biosci. 1996 Aug 1:1:d177-88. doi: 10.2741/a124.

Abstract

Vitamin D exerts its genomic effects following binding to a specific receptor which is a member of the steroid hormone receptor superfamily. The vitamin D receptor (VDR) forms heterodimers with retinoid X receptors (RXRs) and the dimer then interacts with its cognate binding site, termed vitamin D response element (VDRE), to affect the transcription of target genes. Recent studies have identified novel sequence motifs for VDREs as well as novel protein-protein interactions involving the VDR. These will be reviewed with particular emphasis on the complex VDRE from the c-fos proto-oncogene promoter region and the inhibition of the vitamin D signal transduction pathway by the multifunctional protein, calreticulin. Thus research on the control of gene transcription by vitamin D reveals examples of molecular interplay between transcriptional regulatory pathways and provides new insight into the molecular mechanism of action of vitamin D.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Base Sequence
  • Binding Sites
  • Bone and Bones / cytology
  • Bone and Bones / physiology*
  • Calcitriol / physiology
  • Calreticulin / genetics
  • Calreticulin / physiology*
  • Humans
  • Promoter Regions, Genetic
  • Proto-Oncogene Mas
  • Receptors, Calcitriol / genetics
  • Receptors, Calcitriol / physiology*
  • Vitamin D / physiology*

Substances

  • Calreticulin
  • MAS1 protein, human
  • Proto-Oncogene Mas
  • Receptors, Calcitriol
  • Vitamin D
  • Calcitriol