Cleavage of Alzheimer's Amyloid Precursor Protein (APP) by Secretases Occurs after O-Glycosylation of APP in the Protein Secretory Pathway IDENTIFICATION OF INTRACELLULAR COMPARTMENTS IN WHICH APP CLEAVAGE OCCURS WITHOUT USING TOXIC AGENTS THAT INTERFERE WITH PROTEIN METABOLISM*
Tomita S, Kirino Y, Suzuki T. Cleavage of Alzheimer's Amyloid Precursor Protein (APP) by Secretases Occurs after O-Glycosylation of APP in the Protein Secretory Pathway IDENTIFICATION OF INTRACELLULAR COMPARTMENTS IN WHICH APP CLEAVAGE OCCURS WITHOUT USING TOXIC AGENTS THAT INTERFERE WITH PROTEIN METABOLISM*. Journal Of Biological Chemistry 1998, 273: 6277-6284. PMID: 9497354, DOI: 10.1074/jbc.273.11.6277.Peer-Reviewed Original ResearchConceptsAlzheimer amyloid precursor proteinAmyloid precursor proteinAPP cleavageParenchymal amyloid depositsAPP carboxyl-terminal fragmentsPrecursor proteinBeta-amyloid peptideProtein metabolismNormal protein metabolismPossible intracellular siteAbeta generationAmyloid depositsAlzheimer's diseaseCarboxyl-terminal fragmentDefective O-glycosylationToxic agentsIntracellular secretory pathwayDiseasePresent studyIntracellular sitesBetaReticular compartmentAlphaCellsMetabolism