N-truncated amyloid β (Aβ) 4-42 forms stable aggregates and induces acute and long-lasting behavioral deficits

@inproceedings{Bouter2013NtruncatedA,
  title={N-truncated amyloid β (Aβ) 4-42 forms stable aggregates and induces acute and long-lasting behavioral deficits},
  author={Yvonne Bouter and Katharina Dietrich and Jessica L. Wittnam and Nasrollah Rezaei-Ghaleh and Thierry Pillot and Sophie Papot-Couturier and Thomas Lefebvre and Frederick Sprenger and Oliver Wirths and Markus Zweckstetter and Thomas A. Bayer},
  booktitle={Acta Neuropathologica},
  year={2013}
}
N-truncated Aβ4-42 is highly abundant in Alzheimer disease (AD) brain and was the first Aβ peptide discovered in AD plaques. However, a possible role in AD aetiology has largely been neglected. In the present report, we demonstrate that Aβ4-42 rapidly forms aggregates possessing a high aggregation propensity in terms of monomer consumption and oligomer formation. Short-term treatment of primary cortical neurons indicated that Aβ4-42 is as toxic as pyroglutamate Aβ3-42 and Aβ1-42. In line with… CONTINUE READING

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N-terminal pyroglutamate (pglu) formation of Aβ38 and Aβ40 enforces oligomer formation and potency to disrupt hippocampal lTP

D Schlenzig, r rönicke, H Cynis
  • J Neurochem
  • 2012
VIEW 1 EXCERPT