Journal
FRONTIERS IN CELLULAR NEUROSCIENCE
Volume 8, Issue -, Pages -Publisher
FRONTIERS MEDIA SA
DOI: 10.3389/fncel.2014.00410
Keywords
Alzheimer's disease; amyloid precursor protein; APP processing; cell adhesion; SAM; synaptogenic activity
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Funding
- Deutsche Forschungsgemeinschaft (DFG)
- BioComp Forschungsschwerpunkt Rheinland-Pfalz
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The amyloid precursor protein (APP) plays a central role in Alzheimer's disease (AD) and has essential synapse promoting functions. Synaptogenic activity as well as cell adhesion properties of APP presumably depend on trans-cellular dimerization via its extracellular domain. Since neuronal APP is extensively processed by secretases, it raises the question if APP shedding affects its cell adhesion and synaptogenic properties. We show that inhibition of APP shedding using cleavage deficient forms of APP or a dominant negative alpha-secretase strongly enhanced its cell adhesion and synaptogenic activity suggesting that synapse promoting function of APP is tightly regulated by alpha-secretase mediated processing, similar to other trans-cellular synaptic adhesion molecules.
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