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. Author manuscript; available in PMC: 2007 Jun 15.

Published in final edited form as: Arch Biochem Biophys. 2006 Oct 16;460(2):285–292. doi: 10.1016/j.abb.2006.09.027

The truncated VDR binds RXRα and to VDREs. Panel A. VDRs labeled with [³⁵S]-methionine by in vitro coupled transcription-translation were incubated with GST-RXRα in the presence of vehicle or graded concentrations of calcitriol. The samples were then subjected to GST-pull down assays and SDS-PAGE. Bands were visualized by autoradiography. The autoradiograph shows that the truncated VDR binds weakly to GST-RXRα and does not exhibit a 1,25(OH)₂D₃ dependent increase in binding as exhibited by the WT VDR. Panel B. Empty vector (pSG5) and WT and Y401X VDRs were expressed in COS-7 cells. Cell extracts were incubated with [³²P]-labeled osteopontin VDRE with and without 10 nM 1,25(OH)₂D₃. For supershift assays VDR antibody was added. SS, supershift.

The truncated VDR binds RXRα and to VDREs. Panel A. VDRs labeled with [³⁵S]-methionine by in vitro coupled transcription-translation were incubated with GST-RXRα in the presence of vehicle or graded concentrations of calcitriol. The samples were then subjected to GST-pull down assays and SDS-PAGE. Bands were visualized by autoradiography. The autoradiograph shows that the truncated VDR binds weakly to GST-RXRα and does not exhibit a 1,25(OH)₂D₃ dependent increase in binding as exhibited by the WT VDR. Panel B. Empty vector (pSG5) and WT and Y401X VDRs were expressed in COS-7 cells. Cell extracts were incubated with [³²P]-labeled osteopontin VDRE with and without 10 nM 1,25(OH)₂D₃. For supershift assays VDR antibody was added. SS, supershift.