R. Prior

TL;DR: A preferential localization of APP is reported at synaptic sites of human and rat brain and at neuromuscular junctions, implying a role of APP in physiological synaptic activity and a potential and early impairment of central synapses when synaptic APP is converted to beta A4 amyloid during the pathological evolution of Alzheimer's disease and Down's syndrome.

TL;DR: It is shown that T-lymphocytes, macrophages, and microglial cells expressed a new APP isoform by selection of a novel alternative splice site and exclusion of exon 15 of the APP gene, which leads to a transmembrane, beta A4 sequence containing APP variant, lacking 18 amino acid residues close to the amyloidogenic region.

TL;DR: It is suggested that APP may play an important role in the construction of the immunological network and the differentiation of T cells.

TL;DR: Total APP, APP695 and APP751/770 were significantly decreased in the AD and in the MID groups, but were not correlated to the ages of patients or controls, suggesting an intracerebral source.

TL;DR: The present results are consistent with the possibility that amyloid formation requires membrane damage or APP molecules that are not or are incorrectly integrated into membranes, and could show that the ability of synthetic beta A4 to form amyloids depositions is mainly based on hydrophobic parts of the sequence that have to interact with each other and build up large aggregates under physiologic conditions.