LAUSR

Human neurodegenerative diseases (HNDs) often involve the aggregation of several proteins, with disease resulting from their interactions rather than their coincidental co-existence [1, 10]. Dementia with Lewy bodies is character-ized by alpha-synuclein (aS) aggregation and most cases show Alzheimer’s disease neuropathology involving amyloid plaques and neurofibrillary tangles [5], which is associated with earlier onset of dementia. This suggests synergistic interactions of aS with β -amyloid or/and tau proteins. Here, we performed a pilot study in which we examined of a cohort of 13 mice obtained by breeding M83 homozygous (Ho) mice, expressing human A53T mutated aS with APPPS1-21 hemizygous (He) mice expressing human-mutated (APP) and preseni-lin-1 (PS1) were at the of months, which M83 mice develop of occurring in old M83 None of the mice had, however, paralysis, even the 6 APPxM83 mice the APP/PS1 transgene. Western analyses of samples the cortices of the abundant aggregated serine 129 phosphorylated aS