Abnormal alpha-synuclein solubility, aggregation and nitration in the frontal cortex in Pick's disease.
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.
Dalfó
Esther
E
Institut de Neuropatologia, Servei Anatomia Patològica, IDIBELL/Hospital Universitari de Bellvitge, carrer Feixa Llarga sn, 08907 Hospitalet de Llobregat, Spain.
Martinez
Anna
A
Muntané
Gerard
G
Ferrer
Isidre
I
D000368:Aged; D015153:Blotting, Western / Q000379:methods; D016022:Case-Control Studies; D005260:Female; D005625:Frontal Lobe / Q000378:metabolism*; D006801:Humans; D007150:Immunohistochemistry / Q000379:methods; D008297:Male; D008970:Molecular Weight; D010300:Parkinson Disease / Q000378:metabolism; D020774:Pick Disease of the Brain / Q000378:metabolism* / Q000473:pathology*; D011180:Postmortem Changes; D014443:Tyrosine / Q000378:metabolism; D051844:alpha-Synuclein / Q000378:metabolism*
D051844:alpha-Synuclein; D014443:Tyrosine