title: ADAM10 prodomain mutations cause late-onset Alzheimer's disease: not just the latest FAD.
abstract: In this issue of Neuron, Suh et al. (2013) describe two rare ADAM10 prodomain mutations that cause late-onset Alzheimer's disease by impairing prodomain chaperone function, attenuating α-secretase activity, and reducing adult hippocampal neurogenesis. These results support both ADAM10 as a therapeutic target and the amyloid hypothesis of Alzheimer's disease.
authors.affiliation: Department of Cell and Molecular Biology, The Feinberg School of Medicine, Northwestern University, 300 East Superior Street, Tarry 8-713, Chicago, IL 60611-3006, USA. Electronic address: r-vassar@northwestern.edu.
authors.forename: Robert
authors.initials: R
authors.lastname: Vassar
mesh_terms: D000818:Animals; D005260:Female; D006801:Humans; D008297:Male; D051722:ADAM Proteins / Q000235:genetics / Q000502:physiology; D000072197:ADAM10 Protein; D016229:Amyloid beta-Peptides / Q000378:metabolism; D053829:Amyloid Precursor Protein Secretases / Q000235:genetics / Q000502:physiology; D020022:Genetic Predisposition to Disease / Q000235:genetics; D008565:Membrane Proteins / Q000235:genetics / Q000502:physiology; D018832:Molecular Chaperones / Q000378:metabolism; D020125:Mutation, Missense / Q000235:genetics
chemical_list: D051722:ADAM Proteins; D000072197:ADAM10 Protein; C491236:ADAM10 protein, human; D016229:Amyloid beta-Peptides; D053829:Amyloid Precursor Protein Secretases; D008565:Membrane Proteins; D018832:Molecular Chaperones