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Functional analysis of vitamin D receptor (VDR) using adenovirus vector. | LitMetric

Functional analysis of vitamin D receptor (VDR) using adenovirus vector.

J Steroid Biochem Mol Biol

Department of Pharmaceutical Engineering, Faculty of Engineering, Toyama Prefectural University, 5180 Kurokawa, Imizu, Toyama 939-0398, Japan. Electronic address:

Published: June 2023

AI Article Synopsis

  • Researchers created several genetically modified rat models of type II rickets using genome editing, all displaying symptoms like growth retardation and abnormal bone formation, with only Vdr-KO rats also showing skin issues and hair loss.
  • The team utilized adenovirus vectors to express different variations of the vitamin D receptor (VDR) in human cells, examining how these receptors respond to vitamin D forms to understand their functions and link them to rickets symptoms.
  • Key findings revealed that while wild type VDR and VDR(V342M) successfully translocate to the nucleus with vitamin D treatment, VDR(R270L) and VDR(R270L/H301Q) exhibited impaired translocation, suggesting that these variations might affect hair growth

Article Abstract

Recently, we generated type II rickets model rats, including Vdr(R270L), Vdr(H301Q), Vdr(R270L/H301Q), and Vdr-knockout (KO), by genome editing. All generated animals showed symptoms of rickets, including growth retardation and abnormal bone formation. Among these, only Vdr-KO rats exhibited abnormal skin formation and alopecia. To elucidate the relationship between VDR function and rickets symptoms, each VDR was expressed in human HaCaT-VDR-KO cells using an adenovirus vector. We also constructed an adenovirus vector expressing VDR(V342M) corresponding to human VDR(V346M) which causes alopecia. We compared the nuclear translocation of VDRs after adding 1α,25-dihydroxyvitamin D3 (1,25D3) or 25-hydroxyvitamin D3 (25D3) at final concentrations of 10 and 100 nM, respectively. Both 25D3 and 1,25D3 induced the nuclear translocation of wild type VDR and VDR(V342M). Conversely, VDR(R270L) translocation was observed in the presence of 100 nM 25D3, with almost no translocation following treatment with 10 nM 1,25D3. VDR(R270L/H301Q) failed to undergo nuclear translocation. These results were consistent with their affinity for each ligand. Notably, VDR(R270L/H301Q) may exist in an unliganded form under physiological conditions, and factors interacting with VDR(R270L/H301Q) may be involved in the hair growth cycle. Thus, this novel system using an adenovirus vector could be valuable in elucidating vitamin D receptor functions.

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Source
http://dx.doi.org/10.1016/j.jsbmb.2023.106275DOI Listing

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