Synaptic activity reduces intraneuronal Aβ, promotes APP transport to synapses, and protects against Aβ-related synaptic alterations
(2009) In The Journal of Neuroscience 29(31). p.9704-9713- Abstract
A central question in Alzheimer's disease research is what role synaptic activity plays in the disease process. Synaptic activity has been shown to induce β-amyloid peptide release into the extracellular space, and extracellular β-amyloid has been shown to be toxic to synapses. We now provide evidence that the well established synaptotoxicity of extracellular β-amyloid requires β-secretase processing of amyloid precursor protein. Recent evidence supports an important role for intraneuronal β-amyloid in the pathogenesis of Alzheimer's disease. We show that synaptic activity reduces intraneuronal β-amyloid and protects against β-amyloid-related synaptic alterations. Wedemonstrate that synaptic activity promotes the transport of the... (More)
A central question in Alzheimer's disease research is what role synaptic activity plays in the disease process. Synaptic activity has been shown to induce β-amyloid peptide release into the extracellular space, and extracellular β-amyloid has been shown to be toxic to synapses. We now provide evidence that the well established synaptotoxicity of extracellular β-amyloid requires β-secretase processing of amyloid precursor protein. Recent evidence supports an important role for intraneuronal β-amyloid in the pathogenesis of Alzheimer's disease. We show that synaptic activity reduces intraneuronal β-amyloid and protects against β-amyloid-related synaptic alterations. Wedemonstrate that synaptic activity promotes the transport of the amyloid precursor protein to synapses using live cell imaging, and that the protease neprilysin is involved in reduction of intraneuronal β-amyloid with synaptic activity.
(Less)
- author
- publishing date
- 2009-08-05
- type
- Contribution to journal
- publication status
- published
- in
- The Journal of Neuroscience
- volume
- 29
- issue
- 31
- pages
- 10 pages
- publisher
- Society for Neuroscience
- external identifiers
-
- scopus:68549127183
- pmid:19657023
- ISSN
- 0270-6474
- DOI
- 10.1523/JNEUROSCI.2292-09.2009
- language
- English
- LU publication?
- no
- id
- f18df2c6-00f5-4440-8c59-08ceadcb147e
- date added to LUP
- 2020-02-20 14:20:32
- date last changed
- 2024-04-03 03:09:09
@article{f18df2c6-00f5-4440-8c59-08ceadcb147e, abstract = {{<p>A central question in Alzheimer's disease research is what role synaptic activity plays in the disease process. Synaptic activity has been shown to induce β-amyloid peptide release into the extracellular space, and extracellular β-amyloid has been shown to be toxic to synapses. We now provide evidence that the well established synaptotoxicity of extracellular β-amyloid requires β-secretase processing of amyloid precursor protein. Recent evidence supports an important role for intraneuronal β-amyloid in the pathogenesis of Alzheimer's disease. We show that synaptic activity reduces intraneuronal β-amyloid and protects against β-amyloid-related synaptic alterations. Wedemonstrate that synaptic activity promotes the transport of the amyloid precursor protein to synapses using live cell imaging, and that the protease neprilysin is involved in reduction of intraneuronal β-amyloid with synaptic activity.</p>}}, author = {{Tampellini, Davide and Rahman, Nawreen and Gallo, Eduardo F. and Huang, Zhenyong and Dumont, Magali and Capetillo-Zarate, Estibaliz and Ma, Tao and Zheng, Rong and Lu, Bao and Nanus, David M. and Lin, Michael T. and Gouras, Gunnar K.}}, issn = {{0270-6474}}, language = {{eng}}, month = {{08}}, number = {{31}}, pages = {{9704--9713}}, publisher = {{Society for Neuroscience}}, series = {{The Journal of Neuroscience}}, title = {{Synaptic activity reduces intraneuronal Aβ, promotes APP transport to synapses, and protects against Aβ-related synaptic alterations}}, url = {{http://dx.doi.org/10.1523/JNEUROSCI.2292-09.2009}}, doi = {{10.1523/JNEUROSCI.2292-09.2009}}, volume = {{29}}, year = {{2009}}, }