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Updated: May 19, 2026

Imaging the Intracellular Trafficking of APP with Photoactivatable GFP

Imaging the Intracellular Trafficking of APP with Photoactivatable GFP

Published on: October 17, 2015

Amyloid precursor protein (APP) regulates synaptic structure and function.

Sheue-Houy Tyan¹, Ann Yu-Jung Shih, Jessica J Walsh

¹Department of Neurosciences, University of California San Diego, La Jolla, CA 92093, USA. s1tyan@ucsd.edu

Molecular and Cellular Neurosciences

|August 14, 2012

Summary

This summary is machine-generated.

Amyloid precursor protein (APP) loss impairs synaptic structure and function, particularly in older mice. Soluble APP (sAPP) may be crucial for maintaining hippocampal dendritic integrity, independent of amyloid-beta toxicity.

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Imaging the Intracellular Trafficking of APP with Photoactivatable GFP

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Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain

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Stereotaxic Infusion of Oligomeric Amyloid-beta into the Mouse Hippocampus

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Published on: June 17, 2015

Area of Science:

Neuroscience
Molecular Biology
Neurodegenerative Diseases

Background:

Amyloid precursor protein (APP) is central to Alzheimer's disease (AD) pathogenesis, producing amyloid-beta (Aβ) peptides.
Synaptic deficits and dendritic spine loss occur early in AD models, preceding amyloid plaque deposition.
The specific role of APP itself, independent of Aβ, in synaptic regulation remains unclear.

Purpose of the Study:

To investigate the role of APP in regulating synaptic structure and function.
To examine the consequences of APP deficiency using an APP knock-out (APP-/-) mouse model.

Main Methods:

Primary hippocampal neuron cultures from APP-/- mice and littermate controls.
In vivo analysis of CA1 hippocampal neurons in APP-/- mice.
Assessment of dendritic spine density, dendritic morphology, and long-term potentiation (LTP).

Main Results:

APP-/- neurons showed significantly reduced dendritic spine density (~35% in vitro, ~15% in vivo), partially restored by sAPPα.
APP deficiency led to diminished apical dendritic length and arborization in hippocampal neurons.
Neuronal morphology deficits were associated with reduced long-term potentiation, evident only in aged (12-15 months) APP-/- mice.

Conclusions:

APP, specifically its soluble form (sAPP), is essential for maintaining hippocampal dendritic integrity in an age-dependent manner.
These APP-dependent, age-related synaptic changes may contribute to Alzheimer's disease pathology independently of Aβ toxicity.
Findings highlight a novel, non-amyloidogenic role for APP in synaptic maintenance relevant to aging and AD.