Cleavage of Amyloid β Peptide During Constitutive Processing of Its Precursor

Fred Esch; Pamela S. Keim; Eric C. Beattie; Russell Blacher; Alan R. Culwell; Tilman Oltersdorf; Donald McClure; Pamela J. Ward

doi:10.1126/science.2111583

Abstract

The amyloid β peptide (AβP) is a small fragment of the much larger, broadly distributed amyloid precursor protein (APP). Abundant AβP deposition in the brains of patients with Alzheimer's disease suggests that altered APP processing may represent a key pathogenic event. Direct protein structural analyses showed that constitutive processing in human embryonic kidney 293 cells cleaves APP in the interior of the AβP, thus preventing AβP deposition. A deficiency of this processing event may ultimately prove to be the etiological event in Alzheimer's disease that gives rise to senile plaque formation.

Keywords

Amyloid precursor proteinSenile plaquesPeptideAmyloid (mycology)Amyloid betaP3 peptideAmyloid precursor protein secretaseCleavage (geology)BETA (programming language)Alzheimer's diseaseProtein precursorBiochemistry of Alzheimer's diseaseChemistryBiologyDiseaseBiochemistryMedicinePathologyEnzymeComputer science

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Publication Info

Year: 1990
Type: article
Volume: 248
Issue: 4959
Pages: 1122-1124
Citations: 1389
Access: Closed

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APA Style

                            
                                
                                    Fred Esch, 
                                
                                    Pamela S. Keim, 
                                
                                    Eric C. Beattie
                                
                                et al.
                            
                            (1990). 
                            Cleavage of Amyloid β Peptide During Constitutive Processing of Its Precursor. 
                            Science
                            , 248
                            (4959)
                            , 1122-1124.
                            https://doi.org/10.1126/science.2111583
                        

Identifiers

DOI: 10.1126/science.2111583