Description
Mutations in several genes associated with early onset Alzheimer's result in increased extracellular concentrations of the longer form of the beta-amyloid peptide Ab 1-42 relative to Ab 1-40. It is this longer form of Ab that has been shown to be toxic to neurons and may serve as a catalyst for the aggregation and deposition of Ab to produce the neurotoxic effects associated with senile plaque formation. Using the Ab peptide in a yeast two-hybrid screen, a novel interacting protein designated the endoplasmic reticulum-associated amyloid betapeptide-binding protein (ERAB)/L-3-hydroxyacyl-CoA dehydrogenase type II has been identified. It is shown to be expressed at high levels in Alzheimer's disease-affected brain. ERAB may contribute to neuronal dysfunction in Alzheimer's disease