Intraneuronal advanced glycation endproducts in presenilin-I Alzheimer's disease

Gerald Münch, Claire E. Shepherd, Heather McCann, William S. Brooks, John B.J. Kwok, Thomas Arendt, Marianne Hallupp, Peter R. Schofield, Ralph N. Martins, Glenda M. Halliday*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

31 Citations (Scopus)

Abstract

The most frequently mutated gene resulting in dominantly inherited Alzheimer's disease is presenilin-I. We have used antibodies against advanced glycation endproducts (AGE) in brain tissue sections of four patients with three different presenilin I mutations. Accumulation of intracellular AGE was observed in 75-95% of pyramidal neurons in patients with presenilin-I mutations, far exceeding the percentage of presenilin-I-, tau- or ubiquitin-positive neurons. This high level of AGE-modified proteins in vulnerable neurons is most likely explained by higher levels of their precursors (reactive (di)carbonyl products) or a slower turnover of the participating proteins. These conditions of carbonyl stress may contribute to increased neuronal dysfunction and vulnerability leading to the early disease onset.

Original languageEnglish
Pages (from-to)601-604
Number of pages4
JournalNeuroReport
Volume13
Issue number5
Publication statusPublished - 16 Apr 2002
Externally publishedYes

Keywords

  • Advanced glycation endproducts
  • Alzheimer's disease
  • Presenilin
  • Pyramidal neurons

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