Topic: AETA peptides

The amyloid-β precursor protein (APP) is a transmembrane protein constitutively expressed in the brain and highly implicated in Alzheimer’s disease aetiology. We previously identified a novel cleavage site of APP, the η-secretase site (Willem et al. Nature 2015, PMID:26322584). Peptides resulting from this cleavage and α- or β-secretase-dependent proteolysis are the extracellular soluble AETA peptides (Aη-α or Aη-β, respectively). Our previous work also demonstrated that AETA modulates synaptic plasticity and significantly reduces calcium activity in the hippocampus (HPC) in vivo. These result

The amyloid-β precursor protein (APP), physiologically cleaved, allows the secretion of Amyloid-β (Aβ) but also of other peptides, including the peptides secreted from the η-secretase pathway (AETA peptides) that we described previously (Willem et al., Nature 2015, PMID:26322584). We now obtained reliable data showing that AETA controls both ionotropic and non-ionotropic signalling of NMDA receptors (NMDAr) (Dunot et al, in revision). Here we asked whether AETA, due to its new-found role as a modulator of NMDArs, could be implicated in Alzheimer’s disease (AD) aetiology. First, we quantified A