Mice lacking α-synuclein display functional deficits in the nigrostriatal dopamine system
Neuron, 2000•cell.com
Abstract α-Synuclein (α-Syn) is a 14 kDa protein of unknown function that has been
implicated in the pathophysiology of Parkinson's disease (PD). Here, we show that α-Syn−/−
mice are viable and fertile, exhibit intact brain architecture, and possess a normal
complement of dopaminergic cell bodies, fibers, and synapses. Nigrostriatal terminals of α-
Syn−/− mice display a standard pattern of dopamine (DA) discharge and reuptake in
response to simple electrical stimulation. However, they exhibit an increased release with …
implicated in the pathophysiology of Parkinson's disease (PD). Here, we show that α-Syn−/−
mice are viable and fertile, exhibit intact brain architecture, and possess a normal
complement of dopaminergic cell bodies, fibers, and synapses. Nigrostriatal terminals of α-
Syn−/− mice display a standard pattern of dopamine (DA) discharge and reuptake in
response to simple electrical stimulation. However, they exhibit an increased release with …
Abstract
α-Synuclein (α-Syn) is a 14 kDa protein of unknown function that has been implicated in the pathophysiology of Parkinson's disease (PD). Here, we show that α-Syn−/− mice are viable and fertile, exhibit intact brain architecture, and possess a normal complement of dopaminergic cell bodies, fibers, and synapses. Nigrostriatal terminals of α-Syn−/− mice display a standard pattern of dopamine (DA) discharge and reuptake in response to simple electrical stimulation. However, they exhibit an increased release with paired stimuli that can be mimicked by elevated Ca2+. Concurrent with the altered DA release, α-Syn−/− mice display a reduction in striatal DA and an attenuation of DA-dependent locomotor response to amphetamine. These findings support the hypothesis that α-Syn is an essential presynaptic, activity-dependent negative regulator of DA neurotransmission.
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