Protective effect of pyrroloquinoline quinone against Abeta-induced neurotoxicity in human neuroblastoma SH-SY5Y cells

Neurosci Lett. 2009 Oct 30;464(3):165-9. doi: 10.1016/j.neulet.2009.08.037. Epub 2009 Aug 20.


The neurotoxicity of aggregated beta-amyloid (Abeta) has been implicated as a critical cause in the pathogenesis of Alzheimer's disease (AD). It can cause neurotoxicity in AD by evoking a cascade of oxidative damage-dependent apoptosis to neurons. In the present study, we for the first time investigated the protective effect of pyrroloquinoline quinone (PQQ), an anionic, water soluble compound that acts as a redox cofactor of bacterial dehydrogenases, on Abeta-induced SH-SY5Y cytotoxicity. Abeta(25-35) significantly reduced cell viability, increased the number of apoptotic-like cells, and increased ROS production. All of these phenotypes induced by Abeta(25-35) were markedly reversed by PQQ. PQQ pretreatment recovered cells from Abeta(25-35)-induced cell death, prevented Abeta(25-35)-induced apoptosis, and decreased ROS production. PQQ strikingly decreased Bax/Bcl-2 ratio, and suppressed the cleavage of caspase-3. These results indicated that PQQ could protect SH-SY5Y cells against beta-amyloid induced neurotoxicity.

MeSH terms

  • Amyloid beta-Peptides / physiology*
  • Amyloid beta-Peptides / toxicity
  • Apoptosis
  • Caspase 3 / metabolism
  • Cell Line, Tumor
  • Cell Survival / drug effects
  • Humans
  • Neuroblastoma
  • Neurons / cytology
  • Neurons / drug effects*
  • Neurons / metabolism
  • Neuroprotective Agents / pharmacology*
  • PQQ Cofactor / pharmacology*
  • Peptide Fragments / physiology*
  • Peptide Fragments / toxicity
  • Proto-Oncogene Proteins c-bcl-2 / metabolism
  • Reactive Oxygen Species / metabolism


  • Amyloid beta-Peptides
  • Neuroprotective Agents
  • Peptide Fragments
  • Proto-Oncogene Proteins c-bcl-2
  • Reactive Oxygen Species
  • amyloid beta-protein (25-35)
  • PQQ Cofactor
  • Caspase 3