| RRC ID |
310
|
| 著者 |
Takahashi M, Kanuka H, Fujiwara H, Koyama A, Hasegawa M, Miura M, Iwatsubo T.
|
| タイトル |
Phosphorylation of alpha-synuclein characteristic of synucleinopathy lesions is recapitulated in alpha-synuclein transgenic Drosophila.
|
| ジャーナル |
Neurosci Lett
|
| Abstract |
alpha-Synuclein is a major component of Lewy bodies in the brains of patients with Parkinson's disease (PD) as well as of neuronal/glial inclusions in a subset of neurodegenerative disorders collectively termed synucleinopathies. Here we studied by immunohistochemistry the accumulation of alpha-synuclein in transgenic (TG) Drosophila overexpressing wild-type (WT) or familial PD-linked mutant (i.e. A30P and A53T) alpha-synuclein in neurons, with special reference to the phosphorylation at Ser129, that is characteristic of human synucleinopathy lesions. Progressive accumulation of human alpha-synuclein was widely observed in the cell bodies and neurites of major neuronal nuclei in TG Drosophila brains, and phosphorylation of alpha-synuclein at Ser129 was detected in a limited subset of neurons approximately 1 week after alpha-synuclein immunoreactivity was first detected. Phosphorylated alpha-synuclein was most abundant in A53T mutant, followed by A30P and WT Drosophila. These results suggest that accumulation and phosphorylation of alpha-synuclein is recapitulated in neurons of alpha-synuclein transgenic Drosophila, that underscores the relevance of this model to human synucleinopatheis.
|
| 巻・号 |
336(3)
|
| ページ |
155-8
|
| 公開日 |
2003-1-23
|
| DOI |
10.1016/s0304-3940(02)01258-2
|
| PII |
S0304394002012582
|
| PMID |
12505616
|
| MeSH |
Animals
Drosophila
Immunohistochemistry
Mutation*
Nerve Tissue Proteins / genetics
Nerve Tissue Proteins / metabolism*
Neurodegenerative Diseases / metabolism*
Neurons / metabolism*
Phosphorylation
Serine / metabolism
Synucleins
Time Factors
alpha-Synuclein
|
| IF |
2.274
|
| 引用数 |
90
|
|
WOS 分野
|
NEUROSCIENCES
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| リソース情報 |
| ショウジョウバエ |
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