Secreted-APP and holo-APP bind Amyloid beta through distinct domains eliciting different toxic responses on hippocampal neurons.

GABRIELA KEDIKIAN, FLORENCIA HEREDIA, VICTORIA ROZES SALVADOR, DANIEL RAIMUNDA, NORA ISOARDI, LORENA HEREDIA AND ALFREDO LORENZO

WILEY-LISS, DIV JOHN WILEY & SONS INC

Año: 2010

strong>Amyloid beta (Aâ) is a metabolic product of Amyloid â Precursor protein (APP).  Deposition of Aâ in the brain and neuronal degeneration are characteristic hallmarks of Alzheimer?s disease (AD).  Aâ induces neuronal degeneration, but the mechanism of neurotoxicity remains elusive.  Increasing evidence implicates APP as a receptor-like protein for Aâ fibrils (fAâ).  In this study, we present further experimental support for the direct interaction of APP with fAâ, and for its involvement in Aâ neurotoxicity.  Using recombinant purified holo-APP (h-APP) we showed that