Cited by 113Alzheimer's disease research and treatmentsCell Adhesion Molecules ResearchNeuroinflammation and Neurodegeneration Mechanisms

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Aberrant Activation of Focal Adhesion Proteins Mediates Fibrillar Amyloid β-Induced Neuronal Dystrophy

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Grace, Elizabeth A., Busciglio, Jorge·2003·The Journal of Neuroscience

DOI 10.1523/jneurosci.23-02-00493.2003PMC PMC6741895

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Abstract

Neuronal dystrophy is a pathological hallmark of Alzheimer's disease (AD) that is not observed in other neurodegenerative disorders that lack amyloid deposition. Treatment of cortical neurons with fibrillar amyloid beta (Abeta) peptides induces progressive neuritic dystrophy accompanied by a marked loss of synaptophysin immunoreactivity (Grace et al., 2002). Here, we report that fibrillar Abeta-induced neuronal dystrophy is mediated by the activation of focal adhesion (FA) proteins and the formation of aberrant FA structures adjacent to Abeta deposits. In the AD brain, activated FA proteins are observed associated with the majority of senile plaques. Clustered integrin receptors and activated paxillin (phosphorylated at Tyr-31) and focal adhesion kinase (phosphorylated at Tyr-297) are mainly detected in dystrophic neurites surrounding Abeta plaque cores, where they colocalize with hyperphosphorylated tau. Deletion experiments demonstrated that the presence of the LIM domains in the paxillin C terminus and the recruitment of the protein-Tyr phosphatase (PTP)-PEST to the FA complex are required for Abeta-induced neuronal dystrophy. Therefore, both paxillin and PTP-PEST appear to be critical elements in the generation of the dystrophic response. Paxillin is a scaffolding protein to which other FA proteins bind, leading to the formation of the FA contact and initiation of signaling cascades. PTP-PEST plays a key role in the dynamic regulation of focal adhesion contacts in response to extracellular cues. Thus, in the AD brain, fibrillar Abeta may induce neuronal dystrophy by triggering a maladaptive plastic response mediated by FA protein activation and tau hyperphosphorylation.

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Authors: Grace, E. A., & Busciglio, J.
Affiliations: UConn Health (US)
ORCID: Busciglio, Jorge
Venue: The Journal of Neuroscience
Publisher: Society for Neuroscience
Published: 2003-01-15
Volume: 23
Issue: 2
Pages: 493-502
ISSN: 0270-6474 (ISSN-L)
1529-2401
DOI: 10.1523/jneurosci.23-02-00493.2003
PMC: PMC6741895
OpenAlex: W1562586507
Cited by: 113
References: 81
Citations by year: 2026: 1 · 2025: 1 · 2024: 3 · 2023: 2 · 2022: 3 · 2021: 1 · 2020: 4 · 2019: 2 · 2018: 2 · 2017: 5 · 2016: 5 · 2015: 4 · 2014: 3 · 2013: 7 · 2012: 4
FWCI: 6.72
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Journal of Neuroscience (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: Alzheimer's Association
University of Connecticut
National Institutes of Health
Eunice Kennedy Shriver National Institute of Child Health and Human Development (HD-38466, R01HD038466)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Keywords: Alzheimer's disease, fibrillar amyloid-beta, neuronal dystrophy, focal adhesion proteins, paxillin, PTP-PEST, focal adhesion kinase, integrins, tau hyperphosphorylation, synaptophysin, LIM domain, amyloid plaques, synaptic dysfunction, maladaptive plasticity
MeSH terms: Alzheimer Disease, Animals, Cells, Cultured, Cytoskeletal Proteins, Cytoskeleton, Luminescent Proteins, Neurons, Phosphoproteins, Phosphorylation, Recombinant Fusion Proteins, Transfection, Signal Transduction, Cell Adhesion Molecules, Integrins, Amyloid beta-Peptides, Neurites, tau Proteins, Cell Death, Protein Tyrosine Phosphatases, Protein Structure, Tertiary, Protein Transport, Focal Adhesions, Macromolecular Substances, Green Fluorescent Proteins, Rats, Paxillin, Protein Tyrosine Phosphatase, Non-Receptor Type 12

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Aberrant Activation of Focal Adhesion Proteins Mediates Fibrillar Amyloid β-Induced Neuronal Dystrophy

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