G. König

TL;DR: To study the putative precursor proteins of Alzheimer's disease A4 amyloid protein, polyclonal and monoclonal antibodies were raised against a recombinant bacterial PreA4(695) fusion protein to identify the precursors in different cell lines as well as in human brain homogenates and cerebrospinal fluid.

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: Upon acute activation, microglia, the immuneffector cells of the brain parenchyma, express the amyloid precursor protein (APP) that is otherwise prominent in pathological structures related to Alzheimer's disease.

TL;DR: The localization of APP at synaptic sites in brain suggests that APP regulation and expression are critical determinants of a potential and early impairment of central synapses.

TL;DR: Induction of differentiation of SH‐SY5Y cells with NGF leads to a fivefold increase of total APP mRNA without change in the splicing pattern, suggesting that RA but not NGF induces factor(s) which are responsible for an APP hnRNA splicing favoring APP695 mRNA.