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Visualizing interaction of proteins relevant to Alzheimer's disease in intact cells.

Authors
  • Thomas, Anne V1
  • Berezovska, Oksana
  • Hyman, Bradley T
  • von Arnim, Christine A F
  • 1 Department of Neurology, University of Cologne, Germany. , (Germany)
Type
Published Article
Journal
Methods (San Diego, Calif.)
Publication Date
Apr 01, 2008
Volume
44
Issue
4
Pages
299–303
Identifiers
DOI: 10.1016/j.ymeth.2007.02.003
PMID: 18374273
Source
Medline
Language
English
License
Unknown

Abstract

To understand normal function of memory studying models of pathological memory decline is essential. The most common form of dementia leading to memory decline is Alzheimer's disease (AD), which is characterized by the presence of neurofibrillary tangles and amyloid plaques in the affected brain regions. Altered production of amyloid beta (Abeta) through sequential cleavage of amyloid precursor protein (APP) by beta- and gamma-secretases seems to be a central event in the molecular pathogenesis of the disease. Thus, the study of the complex interplay of proteins that are involved in or modify Abeta production is very important to gain insight into the pathogenesis of AD. Here, we describe the use of Fluorescence lifetime imaging microscopy (FLIM), a Fluorescence resonance energy transfer (FRET)-based method, to visualize protein-protein-interaction in intact cells, which has proven to be a valuable method in AD research.

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