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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Bedse, G., Domenico, F. D., Serviddio, G., & Cassano, T. (2015) · Frontiers in Neuroscience · doi:10.3389/fnins.2015.00204 · Cited by 313
“In the following section we will discuss the evidence of relation of insulin signaling deficiency with AD pathology and disease progression.”
Background
Green tea catechins as brain‐permeable, natural iron chelators‐antioxidants for the treatment of neurodegenerative disorders
Mandel, S. A., Amit, T., Reznichenko, L., Weinreb, O., & Youdim, M. B. H. (2006) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.200500156 · Cited by 293
The Disintegrins ADAM10 and TACE Contribute to the Constitutive and Phorbol Ester-regulated Normal Cleavage of the Cellular Prion Protein
Vincent, B., Paitel, E., Säftig, P., Frobert, Y., Hartmann, D., Strooper, B. D., Grassi, J. J., Lopez‐Perez, E., & Checler, F. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105677200 · Cited by 289
Meal size and frequency affect neuronal plasticity and vulnerability to disease: cellular and molecular mechanisms
Mattson, M. P., Duan, W., & Guo, Z. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01586.x · Cited by 289
Self-citation
Structural and kinetic features of amyloid β-protein fibrillogenesis
Teplow, D. B. (1998) · Amyloid · doi:10.3109/13506129808995290 · Cited by 284
The amyloid‐β precursor protein: integrating structure with biological function
Reinhard, C., Hébert, S. S., & Strooper, B. D. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600860 · Cited by 294
“Soba et al (2005) Regulator of neuronal processes Neurite outgrowth sAPP Undefined Reviewed in Mattson (1997) and Small et al (1999) Ab Undefined Reviewed in Mattson (1997) and Small et al (1999) Dendritic arborization CAPPD Undefined Reviewed in Mattson (1997) and De Strooper and Annaert (2000)…”
BackgroundInfluential
β‐Amyloid neurotoxicity is mediated by a glutamate‐triggered excitotoxic cascade in rat nucleus basalis
Harkany, T., Ábrahám, I. M., Timmerman, W., Laskay, G., Tóth, B., Sasvári, M., Kónya, C., Sebens, J. B., Korf, J., Nyakas, C. J., et al. (2000) · European Journal of Neuroscience · doi:10.1046/j.1460-9568.2000.00164.x · Cited by 283
“" - !”
Lithium protects cultured neurons against β‐amyloid‐induced neurodegeneration
Alvarez, G., Muñoz-Montaño, J. R., Satrústegui, J., Ávila, J., Bogónez, E., & Díaz‐Nido, J. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00685-7 · Cited by 270
Chemokines/chemokine receptors in the central nervous system and Alzheimer's disease
Xia, M., & Hyman, B. T. (1999) · Journal of NeuroVirology · doi:10.3109/13550289909029743 · Cited by 269
“…- ques ( at least a substantial proportion ) are believed to represent aberrant regenerating neurites ( Geddes et al , 1986 ; Masliah et al , 1991 ; 1992 ) and APP has been shown to play a role in promoting neurite outgrowth and neuronal survival in vitro ( Mattson , 1997 ; Milward et al , 1992 ) .”
Background
Heme oxygenase-1: role in brain aging and neurodegeneration
Schipper, H. M. (2000) · Experimental Gerontology · doi:10.1016/s0531-5565(00)00148-0 · Cited by 268
“Oxidative stress has been amply documented in AD-affected brain tissues (Mattson , 1997) and may be responsible for induction of HO-1 and other stress proteins in these patients (Schipper et al., 1995).”
Background
The Drosophila β-Amyloid Precursor Protein Homolog Promotes Synapse Differentiation at the Neuromuscular Junction
Torroja, L., Packard, M. C., Gorczyca, M. G., White, K., & Budnik, V. (1999) · Journal of Neuroscience · doi:10.1523/jneurosci.19-18-07793.1999 · Cited by 268
“The effects of APP on neuronal development and function have been extensively studied because of their implication in Alzheimer’s disease (for review, see Mattson, 1997; Small, 1998).”
Background
Par-4 is a mediator of neuronal degeneration associated with the pathogenesis of Alzheimer disease
Guo, Q., Fu, W., Xie, J., Luo, H., Sells, S. F., Geddes, J. W., Bondada, V., Rangnekar, V. M., & Mattson, M. P. (1998) · Nature Medicine · doi:10.1038/nm0898-957 · Cited by 260
Self-citation
Amyloid β‐peptide interactions with neuronal and glial cell plasma membrane: binding sites and implications for Alzheimer's disease
Verdier, Y., Zarándi, M., & Penke, B. (2004) · Journal of Peptide Science · doi:10.1002/psc.573 · Cited by 267
Amyloid β-peptide induces apoptosis-related events in synapses and dendrites
Mattson, M. P., Partin, J. V., & Begley, J. G. (1998) · Brain Research · doi:10.1016/s0006-8993(98)00763-x · Cited by 258
Self-citation
Genetic Neurodegenerative Diseases: The Human Illness and Transgenic Models
Price, D. L., Sisodia, S. S., & Borchelt, D. (1998) · Science · doi:10.1126/science.282.5391.1079 · Cited by 258
Peroxynitrite Mediates Neurotoxicity of Amyloid β-Peptide 1–42 - and Lipopolysaccharide-Activated Microglia
Xie, Z., Wei, M., Morgan, T. E., Fabrizio, P., Han, D., Finch, C. E., & Longo, V. D. (2002) · The Journal of Neuroscience · doi:10.1523/jneurosci.22-09-03484.2002 · Cited by 272
“AD brains show widespread oxidative damage (Mattson, 1997; Smith et al., 2000).”
Background
Inhibition of γ‐secretase causes increased secretion of amyloid precursor protein C‐terminal fragments in association with exosomes
Sharples, R. A., Vella, L. J., Nisbet, R. M., Naylor, R., Perez, K. A., Barnham, K. J., Masters, C. L., & Hill, A. F. (2008) · The FASEB Journal · doi:10.1096/fj.07-9357com · Cited by 253
Conformational transition of amyloid β-peptide
Xu, Y., Shen, J., Luo, X., Zhu, W., Chen, K., Ma, J., & Jiang, H. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0501218102 · Cited by 250
Crystal structure of the N-terminal, growth factor-like domain of Alzheimer amyloid precursor protein.
Parker, M. W., Rossjohn, J., Cappai, R., Feil, S. C., Henry, A., McKinstry, W. J., Galatis, D., Hesse, L., Multhaup, G., Beyreuther, K. T., et al. (1999) · Nature Structural Biology · doi:10.1038/7562 · Cited by 242
Aβ1–40-related reduction in functional hyperemia in mouse neocortex during somatosensory activation
Niwa, K., Younkin, L. H., Ebeling, C., Turner, S. K., Westaway, D. A., Younkin, S. G., Ashe, K. H., Carlson, G. A., & Iadecola, C. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.17.9735 · Cited by 247
Amyloid-β Peptide Inhibits Activation of the Nitric Oxide/cGMP/cAMP-Responsive Element-Binding Protein Pathway during Hippocampal Synaptic Plasticity
Puzzo, D., Vitolo, O. V., Trinchese, F., Jacob, J. P., Palmeri, A., & Arancio, O. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.5291-04.2005 · Cited by 248
Energetics and Oxidative Stress in Synaptic Plasticity and Neurodegenerative Disorders
Mattson, M. P., & Liu, D. (2002) · NeuroMolecular Medicine · doi:10.1385/nmm:2:2:215 · Cited by 242
Self-citation
Neuroprotective signaling and the aging brain: take away my food and let me run11Published on the World Wide Web on 24 August 2000.
Mattson, M. P. (2000) · Brain Research · doi:10.1016/s0006-8993(00)02790-6 · Cited by 239
Self-citation
Disruption of Neurogenesis in the Subventricular Zone of Adult Mice,and in Human Cortical Neuronal Precursor Cells in Culture, by Amyloid β-Peptideby Amyloid β-Peptide
Haughey, N. J., Liu, D., Nath, A., Borchard, A. C., & Mattson, M. P. (2002) · NeuroMolecular Medicine · doi:10.1385/nmm:1:2:125 · Cited by 203
Self-citation
Correlation of β-Amyloid Aggregate Size and Hydrophobicity with Decreased Bilayer Fluidity of Model Membranes
Kremer, J. J., Pallitto, M. M., Sklansky, D. J., & Murphy, R. M. (2000) · Biochemistry · doi:10.1021/bi0001980 · Cited by 237
Antihypertensive Drugs, Prevention of Cognitive Decline and Dementia: A Systematic Review of Observational Studies, Randomized Controlled Trials and Meta-Analyses, with Discussion of Potential Mechanisms
Rouch, L., Cestac, P., Hanon, O., Cool, C., Helmer, C., Bouhanick, B., Chamontin, B., Dartigues, J.-F., Vellas, B. J., & Andrieu, S. (2015) · CNS Drugs · doi:10.1007/s40263-015-0230-6 · Cited by 244
“Reactive oxygen species (ROS) caused by Ab accumulation may have an effect on NMDA receptors and L-VGCCs, leading to a greater influx of calcium [72, 73].”
The Alzheimer Amyloid Precursor Protein (APP) and Fe65, an APP-Binding Protein, Regulate Cell Movement
Sabo, S. L., Ikin, A. F., Buxbaum, J. D., & Greengard, P. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.153.7.1403 · Cited by 237
“APP and FE65 Regulate Cell Movement 1405 where r is the correlation and v is the covariance of two scalars, x and y .”
Background
The channel hypothesis of Alzheimer’s disease: current status
Kagan, B. L., Hirakura, Y., Azimov, R., Azimova, R., & Lin, M. (2002) · Peptides · doi:10.1016/s0196-9781(02)00067-0 · Cited by 230

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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