Neuroprotective effects of PPAR-γ agonist rosiglitazone in N171-82Q mouse model of Huntington's disease

J Neurochem. 2013 May;125(3):410-9. doi: 10.1111/jnc.12190. Epub 2013 Mar 5.

Abstract

Huntington's disease (HD) is a devastating genetic neurodegenerative disease caused by CAG trinucleotide expansion in the exon-1 region of the huntingtin gene. Currently, no cure is available. It is becoming increasingly apparent that mutant Huntingtin (HTT) impairs metabolic homeostasis and causes transcriptional dysregulation. The peroxisome proliferator-activated receptor gamma (PPAR-γ) is a transcriptional factor that plays a key role in regulating genes involved in energy metabolism; recent studies demonstrated that PPAR-γ activation prevented mitochondrial depolarization in cells expressing mutant HTT and attenuated neurodegeneration in various models of neurodegenerative diseases. PPAR-γ-coactivator 1α (PGC-1 α) transcription activity is also impaired by mutant HTT. We now report that the PPAR-γ agonist, rosiglitazone (RSG), significantly attenuated mutant HTT-induced toxicity in striatal cells and that the protective effect of RSG is mediated by activation of PPAR-γ. Moreover, chronic administration of RSG (10 mg/kg/day, i.p) significantly improved motor function and attenuated hyperglycemia in N171-82Q HD mice. RSG administration rescued brain derived neurotrophic factor(BDNF) deficiency in the cerebral cortex, and prevented loss of orexin-A-immunopositive neurons in the hypothalamus of N171-82Q HD mice. RSG also prevented PGC-1α reduction and increased Sirt6 protein levels in HD mouse brain. Our results suggest that modifying the PPAR-γ pathway plays a beneficial role in rescuing motor function as well as glucose metabolic abnormalities in HD.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Anilides / pharmacology
  • Animals
  • Brain / drug effects
  • Brain / enzymology
  • Brain / pathology
  • Brain-Derived Neurotrophic Factor / metabolism
  • Cell Line
  • Disease Models, Animal
  • Gene Expression Regulation / drug effects
  • Gene Expression Regulation / genetics
  • Glutamates / genetics
  • Humans
  • Huntingtin Protein
  • Huntington Disease / complications
  • Huntington Disease / drug therapy*
  • Huntington Disease / genetics
  • Huntington Disease / pathology
  • Hyperglycemia / drug therapy
  • Hyperglycemia / etiology
  • Intracellular Signaling Peptides and Proteins / metabolism
  • L-Lactate Dehydrogenase / metabolism
  • Male
  • Mice
  • Mice, Transgenic
  • Movement Disorders / drug therapy
  • Movement Disorders / etiology
  • Nerve Tissue Proteins / genetics
  • Neurons / drug effects*
  • Neurons / metabolism
  • Neuropeptides / metabolism
  • Neuroprotective Agents / pharmacology
  • Neuroprotective Agents / therapeutic use*
  • Orexins
  • PPAR gamma / antagonists & inhibitors
  • Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha
  • RNA, Messenger / metabolism
  • Rosiglitazone
  • Sirtuins / metabolism
  • Thiazolidinediones / pharmacology
  • Thiazolidinediones / therapeutic use*
  • Trans-Activators / genetics
  • Trans-Activators / metabolism
  • Transcription Factors
  • Transfection
  • Trinucleotide Repeat Expansion / genetics

Substances

  • 2-chloro-5-nitrobenzanilide
  • Anilides
  • Brain-Derived Neurotrophic Factor
  • Glutamates
  • HCRT protein, human
  • HTT protein, human
  • Huntingtin Protein
  • Intracellular Signaling Peptides and Proteins
  • Nerve Tissue Proteins
  • Neuropeptides
  • Neuroprotective Agents
  • Orexins
  • PPAR gamma
  • Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha
  • Ppargc1a protein, mouse
  • RNA, Messenger
  • Thiazolidinediones
  • Trans-Activators
  • Transcription Factors
  • Rosiglitazone
  • Adenosine Triphosphate
  • L-Lactate Dehydrogenase
  • SIRT6 protein, human
  • Sirtuins