Polyglutamine disease: acetyltransferases awry.
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.
Hughes
Robert E
RE
Division of Medical Genetics, Box 357720, University of Washington, Seattle, Washington 98195, USA. rehughes.u.washington.edu
D000123:Acetyltransferases / Q000378:metabolism*; D050882:CREB-Binding Protein; D004791:Enzyme Inhibitors / Q000627:therapeutic use; D015316:Genetic Therapy; D056572:Histone Deacetylase Inhibitors; D006655:Histone Deacetylases / Q000378:metabolism; D006801:Humans; D006816:Huntington Disease / Q000201:enzymology* / Q000235:genetics* / Q000378:metabolism / Q000628:therapy; D019636:Neurodegenerative Diseases / Q000201:enzymology* / Q000235:genetics* / Q000378:metabolism / Q000628:therapy; D009687:Nuclear Proteins / Q000378:metabolism; D010455:Peptides / Q000235:genetics / Q000378:metabolism*; D015534:Trans-Activators / Q000378:metabolism; D014158:Transcription, Genetic / Q000235:genetics; D019680:Trinucleotide Repeat Expansion / Q000235:genetics
D004791:Enzyme Inhibitors; D056572:Histone Deacetylase Inhibitors; D009687:Nuclear Proteins; D010455:Peptides; D015534:Trans-Activators; C097188:polyglutamine; D000123:Acetyltransferases; D050882:CREB-Binding Protein; C494363:CREBBP protein, human; D006655:Histone Deacetylases