Journal of Neurochemistry · 2006 · 112 citations · 25 references
Life SciencesNeurobiologyNeuroscienceMolecular NeurobiologyMolecular NeuroscienceNeurodegenerationIon ChannelsIon PermeationMembrane PermeabilityNeurodegeneration MechanismsNeuronal Membrane PropertiesNeuroprotectionCa2+ SignalingChannel Permeability AlterationsHigh PermeabilityIon Channel PermeabilityIon PermeabilityPlasma Membrane PermeabilityPoresVoltage-gated Calcium Channels
Mutations in alpha-synuclein cause some cases of familial Parkinson's disease (PD), but the mechanism by which alpha-synuclein promotes degeneration of dopamine-producing neurons is unknown. We report that human neural cells expressing mutant alpha-synuclein (A30P and A53T) have higher plasma membrane ion permeability. The higher ion permeability caused by mutant alpha-synuclein would be because of relatively large pores through which most cations can pass non-selectively. Both the basal level of [Ca2+]i and the Ca2+ response to membrane depolarization are greater in cells expressing mutant alpha-synuclein. The membrane permeable Ca2+ chelator BAPTA-AM significantly protected the cells against oxidative stress, whereas neither L-type (nifedipine) nor N-type (omega-conotoxin-GVIA) Ca2+ channel blockers protected the cells. These findings suggest that the high membrane ion permeability caused by mutant alpha-synuclein may contribute to the degeneration of neurons in PD.
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