Premium
P4‐254: Microglia catalyze the “refolding” of Aβ peptide into amyloid, suggesting an alternate mechanism for neuritic plaque formation
Author(s) -
Finley James,
Welch Kathy,
Milici Anthony,
Klein Ann,
Stukenbrok Hans,
Nelson Robert B.
Publication year - 2008
Publication title -
alzheimer's and dementia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.713
H-Index - 118
eISSN - 1552-5279
pISSN - 1552-5260
DOI - 10.1016/j.jalz.2008.05.2323
Subject(s) - microglia , senile plaques , amyloid (mycology) , neurite , thioflavin , fibril , p3 peptide , microbiology and biotechnology , peptide , chemistry , embryonic stem cell , biochemistry of alzheimer's disease , in vitro , biophysics , amyloid precursor protein , alzheimer's disease , biology , pathology , biochemistry , immunology , inflammation , medicine , inorganic chemistry , disease , gene
ease (HD), 2 Dementia lacking distinctive histology (DLDH), 2 Alzheimer’s disease (AD), 1 Atypical Tau and 1 Neuronal Intermediate Filament Inclusion Disease (NIFID)). Results: Urea fractions demonstrated cleaved 25kD TDP-43 fragments and HMWS in 20 cases including 18 FTLD-U (8 FTLD-U1, 5 FTLD-U2, 5 FTLD-U3), 1 MND and 1 DLDH. Three cases (1 FTLD-U3, 1 CBD and 1 MND) showed 25kD/45kD fragments with no associated HMWS and 16 cases (5 FTLD-U (2 FTLD-U1, 2 FTLD-U2 and 1 FTLD3), 5 Pick’s-type histology, 1 FTDP-17T, 1 CBD, 1 AD, 1 Huntington’s disease, 1 NIFID and 1 PSP) showed a HMWS with no associated 25kD fragments. A prominent 15-17kD fragment was also detected within sarkosyl soluble fractions in 41 cases, however, this was not significantly associated with any pathological type. Conclusions: These data indicate that TDP-43 processing and deposition is highly heterogeneous and the biochemical profile of TDP-43 may be more complex than previously described.