γ-Secretase Heterogeneity in the Aph1 Subunit: Relevance for Alzheimer’s Disease

Autor:	Patrick C. May, Bradley T. Hyman, Bart De Strooper, Hermann Esselmann, Raf Sciot, Lutgarde Serneels, Martin K.-H. Schäfer, Eric Karran, Tim Dejaegere, Jérôme Van Biervliet, Tine Van Houtvin, Katleen Craessaerts, Oksana Berezovska, Rudi D'Hooge, Sabine Paul, Katrien Horré, Lieve Moons, Mathias Jucker, Zhixiang Yang, Jens Wiltfang, Ben Sprangers
Rok vydání:	2009
Předmět:	medicine.medical_specialty Protein subunit Biology Regulated Intramembrane Proteolysis Presenilin Amyloid beta-Protein Precursor Mice Alzheimer Disease Memory Internal medicine Endopeptidases Presenilin-1 Amyloid precursor protein medicine Animals Humans Receptor Notch1 Maze Learning Neurons Amyloid beta-Peptides Multidisciplinary Brain Membrane Proteins Human brain medicine.disease Peptide Fragments Cell biology Disease Models Animal Protein Subunits medicine.anatomical_structure Endocrinology biology.protein Female Amyloid Precursor Protein Secretases Alzheimer's disease Signal transduction Amyloid precursor protein secretase Peptide Hydrolases Signal Transduction
Zdroj:	Science. 324:639-642
ISSN:	1095-9203 0036-8075
DOI:	10.1126/science.1171176
Popis:	Tactical Target Intramembrane proteolysis by the γ-secretase complex is important during development and in the pathology of Alzheimer's disease. γ-Secretase has usually been considered as a homogeneous activity. Serneels et al. (p. 639 , published online 19 March; see the Perspective by Golde and Kukar ) now show that the Aph1B component of the γ-secretase complex is responsible for the generation of long β-amyloid species involved in Alzheimer's disease. In a mouse model of Alzheimer's disease, full knockout of Aph1B improved disease phenotypes, without the sort of toxicity previously observed when targeting γ-secretase more generally.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::86bc2e055ff5ed10d4c653799b70dabd https://doi.org/10.1126/science.1171176 Zobrazit plný text záznamu