Topic: immunoprecipitation

Aβ assemblies plays a crucial role in AD pathology. We aimed at characterizing pathological Aβ assemblies produced by cells and investigate their seeding properties and their contribution to amyloid pathology in a FAD mouse model.To that end, coiled-coil constructs were designed to study precise APP orientations controlling Aβ production lines. Immunoprecipitation combined to mass spectrometry was used for the characterization of Aβ assemblies produced by cells, and knock-down were performed to identify the type of γ-secretase involved in their production. Nucleation properties of cell-derived

Cytoplasmic FMR1-interacting protein family contains two members, CYFIP1 and CYFIP2, evolutionarily conserved multifunctional proteins. Despite their high sequence homology, varied evidence indicates that CYFIP1 and CYFIP2 have distinct functions in vivo and are linked to different brain disorders. However, the underlying mechanisms remain largely unknown.We conducted reciprocal immunoprecipitation experiments to explore the underlying mechanisms using CYFIP1-2×Myc and CYFIP2-3×Flag knock-in mice. The results revealed that CYFIP1 and CYFIP2 are not significantly co-immunoprecipitated with each

Amyloid beta1-42(Aβ1-42) peptide, a major pathological component of Alzheimer's disease(AD), is known to locate and accumulate in the mitochondria.Research has demonstrated that nuclear transcription factors(nTF) play a direct or indirect role in the transcriptional regulation of mitochondria, which lose function in the early stages of neurodegenerative diseases.Based on this information, our study investigates the interactions between Aβ and nTFs in mitochondria.In this study, the interaction of 48 nTFs with Aβ was examined using a nTF-interaction kit. Mitochondrial lysate isolations were per

Under normal conditions, α-synuclein (αS) is preferentially localized within synaptic boutons. Changes in αS localization may occur, however, as a consequence of a variety of pathophysiological conditions that include increased protein expression. The purpose of this study was to investigate intraneuronal sites of overexpression-induced αS accumulation. In particular, we assessed αS burden within neuronal perikarya and nuclei; the latter analysis was facilitated by a newly developed assay that detected interactions between αS and histones.Experiments were carried out in the substantia pars com