Cell-permeable parkin proteins suppress Parkinson disease-associated phenotypes in cultured cells and animals

PLoS One. 2014 Jul 14;9(7):e102517. doi: 10.1371/journal.pone.0102517. eCollection 2014.

Abstract

Parkinson's disease (PD) is a neurodegenerative disorder of complex etiology characterized by the selective loss of dopaminergic neurons, particularly in the substantia nigra. Parkin, a tightly regulated E3 ubiquitin ligase, promotes the survival of dopaminergic neurons in both PD and Parkinsonian syndromes induced by acute exposures to neurotoxic agents. The present study assessed the potential of cell-permeable parkin (CP-Parkin) as a neuroprotective agent. Cellular uptake and tissue penetration of recombinant, enzymatically active parkin was markedly enhanced by the addition of a hydrophobic macromolecule transduction domain (MTD). The resulting CP-Parkin proteins (HPM13 and PM10) suppressed dopaminergic neuronal toxicity in cells and mice exposed to 6-hydroxydopamine (6-OHDH) and 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP). These included enhanced survival and dopamine expression in cultured CATH.a and SH-SY5Y neuronal cells; and protection against MPTP-induced damage in mice, notably preservation of tyrosine hydroxylase-positive cells with enhanced dopamine expression in the striatum and midbrain, and preservation of gross motor function. These results demonstrate that CP-Parkin proteins can compensate for intrinsic limitations in the parkin response and provide a therapeutic strategy to augment parkin activity in vivo.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Apoptosis
  • Cell Line
  • Cells, Cultured
  • Corpus Striatum / metabolism
  • Dopamine / biosynthesis
  • Dopamine / metabolism
  • Female
  • Hydrophobic and Hydrophilic Interactions
  • Mesencephalon / metabolism
  • Mice
  • Mice, Inbred BALB C
  • Motor Activity
  • Neuroprotective Agents / pharmacology*
  • Parkinson Disease / genetics
  • Parkinson Disease / metabolism
  • Parkinson Disease / pathology
  • Phenotype
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / pharmacology*
  • Tyrosine 3-Monooxygenase / metabolism
  • Ubiquitin-Protein Ligases / chemistry
  • Ubiquitin-Protein Ligases / pharmacology*
  • Ubiquitin-Protein Ligases / physiology

Substances

  • Neuroprotective Agents
  • Recombinant Proteins
  • Tyrosine 3-Monooxygenase
  • Ubiquitin-Protein Ligases
  • parkin protein
  • Dopamine

Grants and funding

This work was supported by a grant of the Rising Professor Support Program (KRF-2006-331-E00102 to D.J.) of Ministry of Education, Science and Technology, Republic of Korea. The funders had no role in study design, data collection and analysis, decision to publish, or preparation ofthe manuscript.