Abnormal alpha-synuclein solubility, aggregation and nitration in the frontal cortex in Pick's disease

Neuroscience Letters
E DalfóI Ferrer

Abstract

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 alpha-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 alpha-synuclein nitration without formation of Lewy bodies in the frontal cortex in PiD.

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Citations

Jul 8, 2011·Journal of Molecular Cell Biology·Yanying LiuRongqiao He
Mar 9, 2007·Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences·Henrik Ryberg, Kenneth Caidahl
Apr 5, 2012·Neuropathology and Applied Neurobiology·G G KovacsH Budka
Nov 21, 2017·Journal of Alzheimer's Disease : JAD·Isidro Ferrer

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