Amyloid Precursor Protein and Presenilin 1 Interaction Studied by FRET in Human H4 Cells
The mayor pathologic hallmarks of Alzheimer's disease (AD) are senile plaque and neurofibrillary tangles. Senile plaque are primarily made up of deposits of amyloid-? protein, a proteolytic product derived from the amyloid precursor protein (APP). APP is a transmembrane protein detected into the endoplasmic reticulum, in the Golgi apparatus, at the cell surface, recycled by endocytosis to endosomes, whose physiological function is unclear. Presenilins (PS), are a component of ?-secretase complex that cleave ?-CTFs (carboxy-terminal fragment), or ?-CTFs, leaving 40 or 42 amino acids amyloid-? peptides and 58 or 56 amino acids intracellular domains (AICD). Where the amyloid-? peptides is generated is not clear. The study of APPPS interaction in specific cell compartments provides a good opportunity to light upon the molecular mechanisms regulating the activity of the ?-secretase complex, and where ?-amyloid is generated. In our study we used a biophysical assay of protein proximit
amyloid precursor protein presenilins fret alzheimer's disease confocal microscopy centrosomes