Interaction of Reelin with Amyloid Precursor Protein Promotes Neurite Outgrowth
Open accessAbstract
The processing of amyloid precursor protein (APP) to Abeta is an important event in the pathogenesis of Alzheimer's disease, but the physiological function of APP is not well understood. Our previous work has shown that APP processing and Abeta production are regulated by the extracellular matrix protein Reelin. In the present study, we examined whether Reelin interacts with APP, and the functional consequences of that interaction in vitro. Using coimmunoprecipitation, we found that Reelin interacted with APP through the central domain of Reelin (repeats 3-6) and the E1 extracellular domain of APP. Reelin increased cell surface levels of APP and decreased endocytosis of APP in hippocampal neurons in vitro. In vivo, Reelin levels were increased in brains of APP knock-out mice and decreased in APP-overexpressing mice. RNA interference knockdown of APP decreased neurite outgrowth in vitro and prevented Reelin from increasing neurite outgrowth. Knock-out of APP or Reelin decreased dendritic arborization in cortical neurons in vivo, and APP overexpression increased dendritic arborization. APP and Reelin have previously been shown to promote neurite outgrowth through interactions with integrins. We confirmed that APP interacted with alpha3beta1 integrin, and alpha3beta1 integrin altered APP trafficking and processing. Addition of an alpha3beta1 integrin antibody prevented APP and Reelin-induced neurite outgrowth. These findings demonstrate that Reelin interacts with APP, potentially having important effects on neurite development.
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APP increases dendritic outgrowth in the presence of reelin.
“Moreover, APP also increases dendritic outgrowth in the presence of reelin [80].”
From Sorting nexin 17 regulates ApoER2 recycling and reelin signaling (2014) · cites this paper as [80]
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- Authors
- Hoe, H.-S., Lee, K. J., Carney, R. S. E., Lee, J., Markova, A., Lee, J.-Y., Howell, B. W., Hyman, B. T., Pak, D. T. S., Bu, G., & Rebeck, G. W.
- Affiliations
- Georgetown University (US)
- Georgetown University Medical Center (US)
- Children's National (US)
- Washington University in St. Louis (US)
- Massachusetts General Hospital (US)
- National Institutes of Health (US)
- Corresponding author
- Rebeck, G. W.
- Venue
- Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2009-06-10
- Volume
- 29
- Issue
- 23
- Pages
- 7459-7473
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC2759694
- OpenAlex
- W2147636813
- Cited by
- 219
- References
- 5
- Citations by year
- 2026: 8 · 2025: 4 · 2024: 9 · 2023: 9 · 2022: 10 · 2021: 14 · 2020: 12 · 2019: 7 · 2018: 4 · 2017: 15 · 2016: 16 · 2015: 13 · 2014: 18 · 2013: 27 · 2012: 20
- FWCI
- 11.14
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Neuroscience (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Rare & Special e-Zone (The Hong Kong University of Science and Technology) (submittedVersion)
- Funders
- National Institutes of Health
- National Institute on Aging (P01AG030128, R03AG030060, R01AG027924, R29AG014473, R37AG012406, R03AG032330, R01AG014473, AG032330, AG014473, R01AG035355)
- National Institute of Neurological Disorders and Stroke (R01NS048085)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Axon Guidance and Neuronal Signaling
- Life Sciences › Neuroscience › Developmental Neuroscience › Neurogenesis and neuroplasticity mechanisms
- Keywords
- reelin, amyloid precursor protein, neurite outgrowth, Alzheimer's disease, APP processing, amyloid-beta, alpha3beta1 integrin, APP trafficking, APP endocytosis, dendritic branching, hippocampal neurons, APP overexpression
- MeSH terms
- Reelin Protein, Animals, Brain, Cells, Cultured, Chlorocebus aethiops, Dendrites, Humans, Mice, Inbred C57BL, Mice, Neurologic Mutants, Mice, Transgenic, Nerve Tissue Proteins, Receptors, Cell Surface, Serine Endopeptidases, Cell Adhesion Molecules, Neuronal, Extracellular Matrix Proteins, Neurites, Amyloid beta-Protein Precursor, Rats, Sprague-Dawley, Mice, Knockout, Integrin beta1, COS Cells, Integrin alpha3beta1, Cell Line, Tumor, Mice, Rats, Protease Nexins
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