A short N-terminal domain of HDAC4 preserves photoreceptors and restores visual function in retinitis pigmentosa

Nat Commun. 2015 Aug 14:6:8005. doi: 10.1038/ncomms9005.

Abstract

Retinitis pigmentosa is a leading cause of inherited blindness, with no effective treatment currently available. Mutations primarily in genes expressed in rod photoreceptors lead to early rod death, followed by a slower phase of cone photoreceptor death. Rd1 mice provide an invaluable animal model to evaluate therapies for the disease. We previously reported that overexpression of histone deacetylase 4 (HDAC4) prolongs rod survival in rd1 mice. Here we report a key role of a short N-terminal domain of HDAC4 in photoreceptor protection. Expression of this domain suppresses multiple cell death pathways in photoreceptor degeneration, and preserves even more rd1 rods than the full-length HDAC4 protein. Expression of a short N-terminal domain of HDAC4 as a transgene in mice carrying the rd1 mutation also prolongs the survival of cone photoreceptors, and partially restores visual function. Our results may facilitate the design of a small protein therapy for some forms of retinitis pigmentosa.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Electroretinography
  • Gene Deletion
  • Gene Expression Regulation
  • Genotype
  • HEK293 Cells
  • Histone Deacetylases / genetics
  • Histone Deacetylases / metabolism*
  • Histone Deacetylases / pharmacology*
  • Humans
  • Mice
  • Mice, Transgenic
  • Photoreceptor Cells / drug effects*
  • Protein Structure, Tertiary
  • Repressor Proteins / genetics
  • Repressor Proteins / metabolism*
  • Repressor Proteins / pharmacology*
  • Retinitis Pigmentosa / drug therapy*
  • Vision, Ocular / drug effects*

Substances

  • Repressor Proteins
  • HDAC4 protein, human
  • Histone Deacetylases