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Localization of amyloid precursor protein in GAP43-immunoreactive aberrant sprouting neurites in Alzheimer's disease.

Abstract
Previous in vitro studies have suggested that amyloid precursor protein (APP) could be involved in cell surface adhesion, neuritic growth and survival of hippocampal neurons. In the present study, involvement of APP in aberrant sprouting in Alzheimer's disease (AD) was studied by comparing immunolabeling patterns of anti-APP and anti-growth-associated protein 43 (anti-GAP43). Confocal laser imaging of frontal cortex sections double-immunolabeled for APP and GAP43 showed an increase, in AD, of presynaptic boutons immunostained with anti-GAP43 that contained anti-APP immunoreactivity. The neuritic plaques in AD cases presented intense anti-GAP43 immunoreactive abnormal neurites colocalized with anti-APP. Three-dimensional reconstruction of the plaques showed that anti-APP was colocalized with anti-GAP43 in 57.5% of the aberrant sprouting neurites. We conclude that co-expression of APP with GAP43 in the plaque might be involved in the aberrant sprouting response observed in AD.
AuthorsE Masliah, M Mallory, L Hansen, M Alford, R DeTeresa, R Terry, J Baudier, T Saitoh
JournalBrain research (Brain Res) Vol. 574 Issue 1-2 Pg. 312-6 (Mar 06 1992) ISSN: 0006-8993 [Print] Netherlands
PMID1386275 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S.)
Chemical References
  • Amyloid beta-Protein Precursor
  • GAP-43 Protein
  • Growth Substances
  • Membrane Glycoproteins
  • Nerve Tissue Proteins
Topics
  • Aged
  • Aged, 80 and over
  • Alzheimer Disease (metabolism)
  • Amyloid beta-Protein Precursor (analysis)
  • GAP-43 Protein
  • Growth Substances (analysis)
  • Humans
  • Lasers
  • Membrane Glycoproteins (analysis)
  • Nerve Tissue Proteins (analysis)
  • Neurites (chemistry)

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