Prevention of cytosolic IAPs degradation: a potential pharmacological target in Huntington's Disease

Pharmacol Res. 2005 Aug;52(2):140-50. doi: 10.1016/j.phrs.2005.01.006.

Abstract

Huntington's Disease (HD) is a neurodegenerative disorder caused by an abnormally expanded polyglutamine trait in the amino-terminal region of huntingtin. Pathogenic mechanisms involve a gained toxicity of mutant huntingtin and a potentially reduced neuroprotective function of the wild-type allele. Among the molecular abnormalities reported, HD cells are characterized by the presence of aggregates, transcriptional dysregulation, altered mitochondrial membrane potential and aberrant Ca++ handling. In addition, upon exposure to toxic stimuli, increased mitochondrial release of cytochrome C and activation of caspase-9 and caspase-3 are found in HD cells and tissue. Here we report that HTRA2 and Smac/DIABLO, two additional mitochondrial pro-apoptotic factors, are aberrantly released from brain-derived cells expressing mutant huntingtin. This event causes a reduction in levels of the cytosolic IAP1 (Inhibitor of Apoptosis Protein-1) and XIAP (X-linked inhibitor apoptosis) antiapoptotic IAP family members. Reduced IAP levels are also found in post-mortem HD brain tissue. Treatment with ucf101, a serine protease HTRA2 specific inhibitor, counteracts IAPs degradation in HD cells and increases their survival. These results point to the IAPs as potential pharmacological targets in Huntington's Disease.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Apoptosis Regulatory Proteins
  • Brain / metabolism
  • Carrier Proteins / metabolism*
  • Cell Line
  • Cell Survival
  • Cyclosporine / pharmacology
  • Cytosol / metabolism
  • High-Temperature Requirement A Serine Peptidase 2
  • Humans
  • Huntingtin Protein
  • Huntington Disease / genetics
  • Huntington Disease / metabolism*
  • Inhibitor of Apoptosis Proteins
  • Intracellular Signaling Peptides and Proteins
  • Mice
  • Mitochondria / metabolism
  • Mitochondrial Proteins / metabolism*
  • Mutation
  • Nerve Tissue Proteins / genetics
  • Nerve Tissue Proteins / metabolism
  • Nuclear Proteins / genetics
  • Nuclear Proteins / metabolism
  • Proteins / metabolism*
  • Pyrimidinones / pharmacology
  • Serine Endopeptidases / metabolism*
  • Thiones / pharmacology
  • Ubiquitin-Protein Ligases
  • X-Linked Inhibitor of Apoptosis Protein

Substances

  • Apoptosis Regulatory Proteins
  • Carrier Proteins
  • DIABLO protein, human
  • Diablo protein, mouse
  • HTT protein, human
  • Htt protein, mouse
  • Huntingtin Protein
  • Inhibitor of Apoptosis Proteins
  • Intracellular Signaling Peptides and Proteins
  • Mitochondrial Proteins
  • Nerve Tissue Proteins
  • Nuclear Proteins
  • Proteins
  • Pyrimidinones
  • Thiones
  • UCF 101
  • X-Linked Inhibitor of Apoptosis Protein
  • XIAP protein, human
  • Cyclosporine
  • BIRC2 protein, human
  • Birc2 protein, mouse
  • Ubiquitin-Protein Ligases
  • Serine Endopeptidases
  • HTRA2 protein, human
  • High-Temperature Requirement A Serine Peptidase 2
  • Htra2 protein, mouse