Intracellular amyloid-β in Alzheimer's disease

LaFerla, Frank M.; Green, Kim N.; Oddo, Salvatore

doi:10.1038/nrn2168

Cited by 1,942Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

Intracellular amyloid-β in Alzheimer's disease

LaFerla, Frank M., Green, Kim N., Oddo, Salvatore·2007·Nature Reviews Neuroscience

DOI 10.1038/nrn2168

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Abstract

The primal role that the amyloid-beta (Abeta) peptide has in the development of Alzheimer's disease is now almost universally accepted. It is also well recognized that Abeta exists in multiple assembly states, which have different physiological or pathophysiological effects. Although the classical view is that Abeta is deposited extracellularly, emerging evidence from transgenic mice and human patients indicates that this peptide can also accumulate intraneuronally, which may contribute to disease progression.

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Plaque deposition requires BACE1 activity.
“verified that plaque deposition requires BACE1 activity, as previously shown [17-20].”
From Neuron loss in the 5XFAD mouse model of Alzheimer’s disease correlates with intraneuronal Aβ42 accumulation and Caspase-3 activation (2013) · cites this paper as [17]
In PD, intracellular inclusions of αSYN are found in neurons and glia, while both extracellular and intracellular deposits of Aβ are present in the AD brain.
“In PD, intracellular inclusions of alpha-synuclein (αSYN) are found in neurons and glia, while both extracellular and intracellular deposits of amyloid-beta (Aβ) are present in the AD brain [2, 3].”
From Crosstalk between astrocytes and microglia results in increased degradation of α-synuclein and amyloid-β aggregates (2021) · cites this paper as [3]
Aβ accumulation occurs prior to extracellular amyloid formation, has been implicated in the onset of early cognitive alterations, and may contribute to the pathological cascade of events that leads to neuronal dysfunction and, eventually, to AD.
“A␤ accumulation occurs prior to extracellular amyloid formation, has been implicated in the onset of early cognitive alterations, and may contribute to the pathological cascade of events that leads to neuronal dysfunction and, eventually, to AD (12,13).”
From Molecular Basis for Increased Risk for Late-onset Alzheimer Disease Due to the Naturally Occurring L28P Mutation in Apolipoprotein E4 (2014) · cites this paper as [12]
The 42-amino acid Aβ (Aβ42) constitutes the majority of intraneuronal Aβ.
“Furthermore, the 42-amino acid A␤ (A␤42) constitutes the majority of intraneuronal A␤ (12).”
From Molecular Basis for Increased Risk for Late-onset Alzheimer Disease Due to the Naturally Occurring L28P Mutation in Apolipoprotein E4 (2014) · cites this paper as [12]
Accumulation of amyloid beta, the majority of which is amyloid beta 42, occurs prior to extracellular amyloid formation, has been implicated in the onset of early cognitive alterations, and may contribute to the pathological cascade of events that lead to neuronal dysfunction and, eventually, to Alzheimer disease.
“Accumulation of A␤, the majority of which is A␤42, occurs prior to extracellular amyloid formation, has been implicated in the onset of early cognitive alterations, and may contribute to the pathological cascade of events that lead to neuronal dysfunction and, eventually, to AD (12,13).”
From Molecular Basis for Increased Risk for Late-onset Alzheimer Disease Due to the Naturally Occurring L28P Mutation in Apolipoprotein E4 (2014) · cites this paper as [12]

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β Amyloid peptide (Aβ 42 ) is internalized via the G‐protein‐coupled receptor FPRL1 and forms fibrillar aggregates in macrophages 1
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Salin (1998) · doi:10.1002/(sici)1096-9861(19980720)397:1

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Pathological roles of MAPK signaling pathways in human diseases
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Authors: LaFerla, F. M., Green, K. N., & Oddo, S.
Affiliations: University of California, Irvine (US)
Corresponding author: LaFerla, Frank M.
ORCID: LaFerla, Frank M.
Green, Kim N.
Oddo, Salvatore
Venue: Nature Reviews Neuroscience
Publisher: Springer Science and Business Media LLC
Published: 2007-07
Volume: 8
Issue: 7
Pages: 499-509
ISSN: 1471-003X (ISSN-L)
1471-0048
DOI: 10.1038/nrn2168
OpenAlex: W1602771322
Cited by: 1,942
References: 153
Citations by year: 2026: 69 · 2025: 74 · 2024: 106 · 2023: 73 · 2022: 87 · 2021: 110 · 2020: 137 · 2019: 122 · 2018: 129 · 2017: 117 · 2016: 119 · 2015: 111 · 2014: 107 · 2013: 96 · 2012: 118
FWCI: 9.14
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
Locations: Nature reviews. Neuroscience (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health
Topics: Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Keywords: amyloid-beta, intraneuronal amyloid-beta, Alzheimer's disease, amyloid plaques, amyloid-beta production, neuronal pathology, transgenic mouse model
MeSH terms: Alzheimer Disease, Animals, Brain, Humans, Intracellular Fluid, Synaptic Transmission, Amyloid beta-Peptides, Amyloid beta-Protein Precursor, Extracellular Fluid, Proteasome Endopeptidase Complex, Plaque, Amyloid

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Intracellular amyloid-β in Alzheimer's disease

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