Journal
FRONTIERS IN MOLECULAR NEUROSCIENCE
Volume 10, Issue -, Pages -Publisher
FRONTIERS MEDIA SA
DOI: 10.3389/fnmol.2017.00021
Keywords
amyloid precursor protein (APP); zinc; copper; synaptic transmission; Alzheimer's disease
Categories
Funding
- Deutsche Forschungsgemeinschaft [FOR1332]
- Stiftung Rheinland-Pfalz fur Innovation
- Heidelberg University Biochemistry Center (BZH)
Ask authors/readers for more resources
Alzheimer's disease (AD) is ultimately linked to the amyloid precursor protein (APP). However, current research reveals an important synaptic function of APP and APP-like proteins (APLP1 and 2). In this context various neurotrophic and neuroprotective functions have been reported for the APP proteolytic fragments sAPPot, sAPPI3 and the monomeric amyloid-beta peptide (AN. APP is a metalloprotein and binds copper and zinc ions. Synaptic activity correlates with a release of these ions into the synaptic cleft and dysregulation of their homeostasis is linked to different neurodegenerative diseases. Metal binding to APP or its fragments affects its structure and its proteolytic cleavage and therefore its physiological function at the synapse. Here, we summarize the current data supporting this hypothesis and provide a model of how these different mechanisms might be intertwined with each other.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available