Abstract:
:Tau proteins aggregate into different neuronal inclusions in several neurodegenerative disorders. In Alzheimer's disease (AD), hyperphosphorylated Tau from paired helical filaments (PHF) of neurofibrillary tangles, named PHF-Tau, have an electrophoretic profile with four main bands (Tau 55, 64, 69, 74 kDa). In Pick's disease, phosphorylated Tau from Pick bodies are made of two major components (Tau 55, 64 kDa) and a minor 69 kDa. Here we show, using specific antibodies against translated exon 2, 3 or 10 of Tau isoforms, that the set of Tau isoforms engaged in the most insoluble part of PHF in AD is made of Tau isoforms with exon 10 while they are lacking in phosphorylated Tau from Pick's disease. Our results suggest that specific sets of Tau isoforms distinguish between typical neuronal inclusions.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Sergeant N,David JP,Lefranc D,Vermersch P,Wattez A,Delacourte Adoi
10.1016/s0014-5793(97)00859-4subject
Has Abstractpub_date
1997-08-04 00:00:00pages
578-82issue
3eissn
0014-5793issn
1873-3468pii
S0014-5793(97)00859-4journal_volume
412pub_type
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