Targeting aggregation in the development of therapeutics for the treatment of Huntington's disease and other polyglutamine repeat diseases

Expert Opin Ther Targets. 2003 Apr;7(2):201-13. doi: 10.1517/14728222.7.2.201.

Abstract

Huntington's disease (HD) is one of a number of familial polyglutamine (polyQ) repeat diseases. These neurodegenerative disorders are caused by expression of otherwise unrelated proteins that contain an expansion of a polyQ tract, rendering them toxic to specific subsets of vulnerable neurons. These expanded repeats have an inherent propensity to aggregate; insoluble neuronal nuclear and cytoplasmic polyQ aggregates or inclusions are hallmarks of the disorders [1,2]. In HD, inclusions in diseased brains often precede onset of symptoms, and have been proposed to be involved in pathogenicity [3-5]. Various strategies to block the process of aggregation have been developed in an effort to create drugs that decrease neurotoxicity. A discussion of the effect of antibodies, caspase inhibitors, chemical inhibitors, heat-shock proteins, suppressor peptides and transglutaminase inhibitors upon aggregation and disease is presented.

Publication types

  • Review

MeSH terms

  • Active Transport, Cell Nucleus / drug effects
  • Animals
  • Antibodies, Monoclonal / pharmacology
  • Antibodies, Monoclonal / therapeutic use
  • Caenorhabditis elegans Proteins / chemistry
  • Caenorhabditis elegans Proteins / drug effects
  • Caenorhabditis elegans Proteins / physiology
  • Cysteine Proteinase Inhibitors / pharmacology
  • Cysteine Proteinase Inhibitors / therapeutic use
  • DNA Repeat Expansion*
  • Drosophila Proteins / chemistry
  • Drosophila Proteins / drug effects
  • Drosophila Proteins / physiology
  • Drug Design*
  • Drug Evaluation, Preclinical
  • Humans
  • Huntingtin Protein
  • Huntington Disease / drug therapy*
  • Huntington Disease / genetics
  • Intranuclear Inclusion Bodies / chemistry
  • Intranuclear Inclusion Bodies / drug effects
  • Mice
  • Mice, Transgenic
  • Mitochondria / drug effects
  • Mitochondria / physiology
  • Molecular Chaperones / drug effects
  • Molecular Chaperones / physiology
  • Nerve Tissue Proteins / chemistry
  • Nerve Tissue Proteins / drug effects*
  • Nerve Tissue Proteins / genetics
  • Nootropic Agents / pharmacology*
  • Nootropic Agents / therapeutic use
  • Nuclear Proteins / chemistry
  • Nuclear Proteins / drug effects*
  • Nuclear Proteins / genetics
  • Peptides / genetics*
  • Protein Conformation
  • Protein Processing, Post-Translational / drug effects
  • RNA Interference
  • Repetitive Sequences, Amino Acid
  • Transcription, Genetic / drug effects

Substances

  • Antibodies, Monoclonal
  • Caenorhabditis elegans Proteins
  • Cysteine Proteinase Inhibitors
  • Drosophila Proteins
  • HTT protein, human
  • Huntingtin Protein
  • Molecular Chaperones
  • Nerve Tissue Proteins
  • Nootropic Agents
  • Nuclear Proteins
  • Peptides
  • polyglutamine