Abnormal α-synuclein solubility, aggregation and nitration in the frontal cortex in Pick's disease
Abnormal α-synuclein solubility, aggregation and nitration in the frontal cortex in Pick's disease
复制标题
DOI：
10.1016/j.neulet.2006.02.033
复制
发表时间：
2006-05-29
影响因子：
2.5
通讯作者：
Ferrer, Isidre
中科院分区：
文献类型：
--
作者：
Dalfo, Esther;Martinez, Anna;Ferrer, Isidre
Abnormal solubility and aggregation of alpha-synuclein have been observed in the frontal cortex in three cases with Pick's disease (PiD) when compared with age-matched controls. Bands of 45 kDa and higher molecular weight were detected in the SDS-soluble fractions only in PiD. Patterns in PiD differed from that observed in the cerebral cortex in Lewy body diseases which were examined in parallel. Immunoblots to a-synuclein nitrated in tyrosines revealed bands of 45 and 60 kDa in Dxc- and SDS-soluble fractions in the frontal cortex (which is vulnerable to PiD) but not in the occipital cortex (which is resistant to this degenerative disease). Moreover, nitrated alpha-synuclein was found in Lewy bodies and neurites in synucleinopathies but diffusely in the cytoplasm of scattered neurons in PiD. These findings demonstrate abnormal and distinct alpha-synuclein solubility and aggregation. and a-synuclein nitration without formation of Lewy bodies in the frontal cortex in PiD. (c) 2006 Elsevier Ireland Ltd. All rights reserved.
