التفاصيل البيبلوغرافية
| العنوان: |
A commonly used Drosophila model of Alzheimer’s disease generates an aberrant species of amyloid-β with an additional N-terminal glutamine residue. |
| المؤلفون: |
Allan, Kirsten, Perez, Keyla A., Barnham, Kevin J., Camakaris, James, Burke, Richard |
| المصدر: |
FEBS Letters; Oct2014, Vol. 588 Issue 20, p3739-3743, 5p |
| مصطلحات موضوعية: |
ALZHEIMER'S disease treatment, AMYLOID beta-protein, DROSOPHILA, N-terminal residues, GLUTAMINE, TIME-of-flight mass spectrometry, BIOLOGICAL assay |
| مستخلص: |
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. [ABSTRACT FROM AUTHOR] |
|
Copyright of FEBS Letters is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) |
| قاعدة البيانات: |
Complementary Index |
Full Text Finder