Regulation of Amyloid β Oligomer Binding to Neurons and Neurotoxicity by the Prion Protein-mGluR5 Complex.

ABSTRACT: The prion protein (PrP^C) has been suggested to operate as a scaffold/receptor protein in neurons, participating in both physiological and pathological associated events. PrP^C, laminin, and metabotropic glutamate receptor 5 (mGluR5) form a protein complex on the plasma membrane that can trigger signaling pathways involved in neuronal differentiation. PrP^C and mGluR5 are co-receptors also for β-amyloid oligomers (AβOs) and have been shown to modulate toxicity and neuronal death in Alzheimer's disease. In the present work, we addressed the potential crosstalk between these two signaling pathways, laminin-PrP^C-mGluR5 or AβO-PrP^C-mGluR5, as well as their interplay. Herein, we demonstrated that an existing complex containing PrP^C-

SUBMITTER: Beraldo FH 

PROVIDER: S-EPMC5063978 | biostudies-literature | 2016 Oct

REPOSITORIES: biostudies-literature