Neurotoxicity of Aβ amyloid protein in vitro is not altered by calcium channel blockade Academic Article Article uri icon


MeSH Major

  • Amyotrophic Lateral Sclerosis
  • Immunotherapy
  • Neuroimmunomodulation
  • Parkinson Disease
  • T-Lymphocytes, Regulatory


  • In cortical cultures, A beta protein destabilizes calcium homeostasis, but direct neurotoxicity of A beta is not observed. In hippocampal cultures, we and others find treatment with A beta protein decreases neuronal survival, but the mechanism of neurotoxicity is unknown. We have used low-density, serum-free cultures of hippocampal neurons to determine whether the neurotoxicity of A beta protein in vitro can be altered by voltage- or ligand-gated calcium channel antagonists or cyclic nucleotides. In these cultures, neither omega-conotoxin, nifedipine, verapamil, APV, nor MK-801 altered the survival of neurons exposed to synthetic A beta 1-40. The N-channel antagonist diltiazem decreased A beta 1-40 toxicity repeatedly, but slightly, perhaps by indirectly contributing to increased neuronal viability. Treatment of cultures with dibutyryl cAMP, 8-bromo cAMP, dibutyryl cGMP, and 8-bromo cGMP also failed to alter A beta toxicity. Thus, the toxicity of beta protein in low-density hippocampal cultures was not directly altered either by calcium channel blockers or by the addition of cyclic nucleotides.

publication date

  • January 1995



  • Academic Article


Digital Object Identifier (DOI)

  • 10.1016/0197-4580(95)80002-9

PubMed ID

  • 7723935

Additional Document Info

start page

  • 5

end page

  • 10


  • 16


  • 1