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A commonly used Drosophila model of Alzheimer's disease generates an aberrant species of amyloid‐β with an additional N‐terminal glutamine residue
Author(s) -
Allan Kirsten,
Perez Keyla A.,
Barnham Kevin J.,
Camakaris James,
Burke Richard
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.08.022
Subject(s) - drosophila melanogaster , drosophila (subgenus) , alzheimer's disease , schneider 2 cells , in vivo , peptide , biology , residue (chemistry) , glutamine , amyloid (mycology) , biochemistry , signal peptide , microbiology and biotechnology , gene , chemistry , peptide sequence , amino acid , disease , genetics , medicine , pathology , botany , rna , rna interference
Expression of human amyloid‐β (Aβ) in Drosophila is frequently used to investigate its toxicity in vivo. We expressed Aβ 1–42 in the fly using a secretion signal derived from the Drosophila necrotic gene, as described in several previous publications. Surface‐enhanced laser desorption/ionization TOF MS analysis revealed that the Aβ produced contained an additional glutamine residue at the N‐terminus. Aβ Q+1–42 was found to have increased protein abundance and to cause more severe neurodegenerative effects than wild type Aβ 1–42 as assessed by locomotor activity and lifespan assays. These data reveal that a commonly used model of Alzheimer's disease generates incorrect Aβ peptide.