Polyglutamine disease: acetyltransferases awry

Curr Biol. 2002 Feb 19;12(4):R141-3. doi: 10.1016/s0960-9822(02)00709-1.

Abstract

Recent evidence indicates that inhibition of histone acetyltransferases may be a primary cause of cellular pathogenesis in polyglutamine diseases such as Huntington disease; the results raise the possibility that pharmacologic manipulation of protein acetylation levels could be of therapeutic benefit.

Publication types

  • Review

MeSH terms

  • Acetyltransferases / metabolism*
  • CREB-Binding Protein
  • Enzyme Inhibitors / therapeutic use
  • Genetic Therapy
  • Histone Deacetylase Inhibitors
  • Histone Deacetylases / metabolism
  • Humans
  • Huntington Disease / enzymology*
  • Huntington Disease / genetics*
  • Huntington Disease / metabolism
  • Huntington Disease / therapy
  • Neurodegenerative Diseases / enzymology*
  • Neurodegenerative Diseases / genetics*
  • Neurodegenerative Diseases / metabolism
  • Neurodegenerative Diseases / therapy
  • Nuclear Proteins / metabolism
  • Peptides / genetics
  • Peptides / metabolism*
  • Trans-Activators / metabolism
  • Transcription, Genetic / genetics
  • Trinucleotide Repeat Expansion / genetics

Substances

  • Enzyme Inhibitors
  • Histone Deacetylase Inhibitors
  • Nuclear Proteins
  • Peptides
  • Trans-Activators
  • polyglutamine
  • Acetyltransferases
  • CREB-Binding Protein
  • CREBBP protein, human
  • Histone Deacetylases