Probing the structural requirements for vitamin D3 inhibition of the hedgehog signaling pathway

Bioorg Med Chem Lett. 2012 Jul 15;22(14):4859-63. doi: 10.1016/j.bmcl.2012.05.037. Epub 2012 May 23.

Abstract

A structure-activity relationship study to elucidate the structural basis for hedgehog (Hh) signaling inhibition by vitamin D3 (VD3) was performed. Functional and non-functional regions of VD3 and VD2 were obtained through straightforward synthetic means and their biological activity was determined in a variety of cell-based assays. Several of these compounds inhibited Hh signaling at levels comparable to the parent VD3 with no effects on canonical vitamin D signaling. Most notably, compounds 5 and 9, demonstrated potent inhibition of the Hh pathway, exhibited no binding affinity for the vitamin D receptor (VDR), and did not activate VDR in cell culture. In addition, several compounds exhibited anti-proliferative activity against two human cancer cell lines through a mechanism distinct from the Hh or VDR pathways, suggesting a new cellular mechanism of action for this class of compounds.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Line, Tumor
  • Cell Proliferation / drug effects
  • Cholecalciferol / antagonists & inhibitors*
  • Hedgehog Proteins / metabolism
  • Humans
  • Molecular Structure
  • Signal Transduction / drug effects*
  • Structure-Activity Relationship

Substances

  • Hedgehog Proteins
  • Cholecalciferol