Cited by 1,006Alzheimer's disease research and treatmentsNeuroscience and Neuropharmacology ResearchNeuroinflammation and Neurodegeneration Mechanisms

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Cellular actions of beta-amyloid precursor protein and its soluble and fibrillogenic derivatives

Mattson, M. P.·1997·Physiological Reviews

DOI 10.1152/physrev.1997.77.4.1081

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Abstract

beta-Amyloid precursor protein (beta-APP), the source of the fibrillogenic amyloid beta-peptide (A beta) that accumulates in the brain of victims of Alzheimer's disease, is a multifunctional protein that is widely expressed in the nervous system. beta-Amyloid precursor protein is axonally transported and accumulates in presynaptic terminals and growth cones. A secreted form of beta-APP (sAPP alpha) is released from neurons in response to electrical activity and may function in modulation of neuronal excitability, synaptic plasticity, neurite outgrowth, synaptogenesis, and cell survival. A signaling pathway involving guanosine 3',5'-cyclic monophosphate is activated by sAPP alpha and modulates the activities of potassium channels, N-methyl-D-aspartate receptors, and the transcription factor NF kappa B. Additional functions of beta-APP may include modulation of cell adhesion and regulation of proliferation of nonneuronal cells. Alternative enzymatic processing of beta-APP liberates A beta, which has a propensity to form amyloid fibrils; A beta can damage and kill neurons and increase their vulnerability to excitotoxicity. The mechanism involves generation of oxyradicals and impairment of membrane transport systems (e.g., ion-motive ATPases and glutamate and glucose transporters). Genetic mutations or age-related metabolic changes may promote neuronal degeneration in Alzheimer's disease by increasing production of A beta and/or decreasing levels of neuroprotective sAPP alpha.

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Authors: Mattson, M. P.
Affiliations: University of Kentucky (US)
Corresponding author: Mattson, M. P.
ORCID: Mattson, M. P.
Venue: Physiological Reviews
Publisher: American Physiological Society
Published: 1997-10-01
Volume: 77
Issue: 4
Pages: 1081-1132
ISSN: 0031-9333 (ISSN-L)
1522-1210
DOI: 10.1152/physrev.1997.77.4.1081
OpenAlex: W1762207349
Cited by: 1,006
References: 0
Citations by year: 2026: 1 · 2025: 8 · 2024: 13 · 2023: 22 · 2022: 12 · 2021: 17 · 2020: 20 · 2019: 14 · 2018: 26 · 2017: 23 · 2016: 27 · 2015: 30 · 2014: 38 · 2013: 31 · 2012: 43
FWCI: 29.37
Type: journal article
Language: en
Open access: closed
Locations: Physiological Reviews (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (5r01ns029001-07, 5r01ns030583-04)
National Institute of Neurological Disorders and Stroke (NS29001, NS30583)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Keywords: amyloid precursor protein, soluble APP alpha, amyloid-beta, Alzheimer's disease, axonal transport, presynaptic terminals, neuronal excitability, synaptic plasticity, neurite outgrowth, synaptogenesis, cAMP signaling, potassium channels, NMDA receptor, NF-κB, cell adhesion, excitotoxicity, neurodegeneration
MeSH terms: Alzheimer Disease, Animals, Apolipoproteins E, Humans, Membrane Proteins, Mutation, Nervous System, Neurons, Protein Processing, Post-Translational, Synapses, Amyloid beta-Peptides, Neurites, Amyloid beta-Protein Precursor, Presenilin-1, Presenilin-2

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Cellular actions of beta-amyloid precursor protein and its soluble and fibrillogenic derivatives

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