Abstract：
:Multiple system atrophy is a neurodegenerative disease caused by abnormal α-synuclein (α-syn) accumulation in oligodendrocytes and neurons. We previously demonstrated that transgenic (Tg) mice that selectively overexpressed human α-syn in oligodendrocytes exhibited neuronal α-syn accumulation. Microtubule β-III tubulin binds to endogenous neuronal α-syn to form an insoluble complex, leading to progressive neuronal degeneration. α-Syn accumulation is increased in the presynaptic terminals of Tg mice neurons and may reduce neurotransmitter release. To clarify the mechanisms underlying its involvement in neuronal dysfunction, in the present study, we investigated the effects of neuronal α-syn accumulation on synaptic function in Tg mice. Using whole-cell patch-clamp recording, we found that the frequency of miniature inhibitory postsynaptic currents was reduced in Tg mice. Furthermore, a microtubule depolymerizing agent restored normal frequencies of miniature inhibitory postsynaptic currents in Tg mice. These findings suggest that α-syn and β-III tubulin protein complex plays roles for regulation of synaptic vesicle release in GABAergic interneurons, and it causes to reduce GABAergic inhibitory transmission.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Ito H,Nakayama K,Jin C,Suzuki Y,Yazawa Idoi
10.1016/j.bbrc.2012.10.057subject
Has Abstractpub_date
2012-11-23 00:00:00pages
348-53issue
3eissn
0006-291Xissn
1090-2104pii
S0006-291X(12)02011-6journal_volume
428pub_type
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journal_title：Biochemical and biophysical research communications
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