Cited by 1,975Alzheimer's disease research and treatmentsNeuropeptides and Animal PhysiologyNeuroinflammation and Neurodegeneration Mechanisms

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Neurotrophic and Neurotoxic Effects of Amyloid β Protein: Reversal by Tachykinin Neuropeptides

Yankner, Bruce A., Duffy, Lawrence K., Kirschner, Daniel A.·1990·Science

DOI 10.1126/science.2218531

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Abstract

The amyloid β protein is deposited in the brains of patients with Alzheimer's disease but its pathogenic role is unknown. In culture, the amyloid β protein was neurotrophic to undifferentiated hippocampal neurons at low concentrations and neurotoxic to mature neurons at higher concentrations. In differentiated neurons, amyloid β protein caused dendritic and axonal retraction followed by neuronal death. A portion of the amyloid β protein (amino acids 25 to 35) mediated both the trophic and toxic effects and was homologous to the tachykinin neuropeptide family. The effects of the amyloid β protein were mimicked by tachykinin antagonists and completely reversed by specific tachykinin agonists. Thus, the amyloid β protein could function as a neurotrophic factor for differentiating neurons, but at high concentrations in mature neurons, as in Alzheimer's disease, could cause neuronal degeneration.

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Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
Glenner, G. G., & Wong, C. W. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(84)80190-4 · Cited by 5,404
The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
Kang, J., Lemaire, H.-G., Unterbeck, A., Salbaum, J. M., Masters, C. L., Grzeschik, K.-H., Multhaup, G., Beyreuther, K., & Müller-Hill, B. (1987) · Nature · doi:10.1038/325733a0 · Cited by 4,619
Amyloid plaque core protein in Alzheimer disease and Down syndrome.
Masters, C. L., Simms, G., Weinman, N. A., Multhaup, G., McDonald, B. L., & Beyreuther, K. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.12.4245 · Cited by 4,431
The establishment of polarity by hippocampal neurons in culture.
Dotti, C., Sullivan, C., & Banker, G. (1988) · The Journal of Neuroscience · doi:10.1523/jneurosci.08-04-01454.1988 · Cited by 1,862
Glutamate neurotoxicity in cortical cell culture
Choi, D. W., Maulucci-Gedde, M., & Kriegstein, A. (1987) · Journal of Neuroscience · doi:10.1523/jneurosci.07-02-00357.1987 · Cited by 1,506
Rat hippocampal neurons in dispersed cell culture.
Banker, G. A., & Cowan, W. M. (1977) · Brain Research · doi:10.1016/0006-8993(77)90594-7 · Cited by 1,110
Neuronal origin of a cerebral amyloid: neurofibrillary tangles of Alzheimer's disease contain the same protein as the amyloid of plaque cores and blood vessels.
Masters, C. L., Multhaup, G., Simms, G., Pottgiesser, J., Martins, R. N., & Beyreuther, K. T. (1985) · The EMBO Journal · doi:10.1002/j.1460-2075.1985.tb04000.x · Cited by 1,048
Neurotoxicity of a Fragment of the Amyloid Precursor Associated with Alzheimer's Disease
Yankner, B. A., Dawes, L. R., Fisher, S., Villa-Komaroff, L., Oster-Granite, M. L., & Neve, R. L. (1989) · Science · doi:10.1126/science.2474201 · Cited by 907
Self-citation
Outgrowth-regulating actions of glutamate in isolated hippocampal pyramidal neurons
Mattson, M. P., Dou, P., & Kater, S. B. (1988) · Journal of Neuroscience · doi:10.1523/jneurosci.08-06-02087.1988 · Cited by 557
Tachykinins
Maggio, J. E. (1988) · Annual Review of Neuroscience · doi:10.1146/annurev.ne.11.030188.000305 · Cited by 550

Show all 31 references

Research works printed but not linked: 2

Dayhoff, M. O., Atlas of Protein Sequence and Structure 5 3: 345 (1978).
GLENNER, G, BRANBURY REPORT 15: 137 (1983).

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Gong, Q., Pan, L., Liu, X., Wang, Q., Huang, H., & Zhu, Y. Z. (2010) · Amino Acids · doi:10.1007/s00726-010-0685-1 · Cited by 47
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Esler, W. P., Stimson, E. R., Fishman, J. B., Ghilardi, J. R., Vinters, H. V., Mantyh, P. W., & Maggio, J. E. (1999) · Biopolymers · doi:10.1002/(sici)1097-0282(199905)49:6 · Cited by 47
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Toide, K., Fujiwara, T., Iwamoto, Y., Shinoda, M., Okamiya, K., & Kato, T. (1996) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/bf00168640 · Cited by 47
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Administration of Aggregated Beta-Amyloid Peptide (25–35) Induces Changes in Long-Term Potentiation in the Hippocampus in Vivo
Trubetskaya, V. V., Stepanichev, M. Y., Onufriev, M. V., Лазарева, Н. А., Markevich, V. A., & Gulyaeva, N. V. (2003) · Neuroscience and Behavioral Physiology · doi:10.1023/a:1021761310435 · Cited by 43
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Dargusch, R., Piasecki, D. P., Tan, S., Liu, Y., & Schubert, D. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00035.x · Cited by 43
Specific interaction of VEGF165 with β‐amyloid, and its protective effect on β‐amyloid‐induced neurotoxicity
Yang, S., Kwon, B., Gho, Y. S., & Chae, C. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02993.x · Cited by 43
Amyloid precursor protein is enriched in radial glia: Implications for neuronal development
Trapp, B. D., & Hauer, P. (1994) · Journal of Neuroscience Research · doi:10.1002/jnr.490370413 · Cited by 43
Reorganization of Cingulate Cortex in Alzheimer's Disease: Neuron Loss, Neuritic Plaques, and Muscarinic Receptor Binding
Vogt, B. A., Crino, P. B., & Vogt, L. J. (1992) · Cerebral Cortex · doi:10.1093/cercor/2.6.526 · Cited by 43
The legacy of nanotechnology: Revolution and prospects in neurosurgery
Khawaja, A. M. (2011) · International Journal of Surgery · doi:10.1016/j.ijsu.2011.10.002 · Cited by 42
Protective Effect of Bajijiasu Against β-Amyloid-Induced Neurotoxicity in PC12 Cells
Chen, D., Zhang, P., Lin, L., Shuai, O., He-Ming, Z., Liu, S., & Wang, J.-Y. (2013) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-013-9950-7 · Cited by 42
Binding studies of truncated variants of the Aβ peptide to the V-domain of the RAGE receptor reveal Aβ residues responsible for binding
Gospodarska, E., Kupniewska-Kozak, A., Goch, G., & Dadlez, M. (2011) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2011.02.011 · Cited by 42
Polygalae Radix Extract Prevents Axonal Degeneration and Memory Deficits in a Transgenic Mouse Model of Alzheimer’s Disease
Kuboyama, T., Hirotsu, K., Arai, T., Yamasaki, H., & Tohda, C. (2017) · Frontiers in Pharmacology · doi:10.3389/fphar.2017.00805 · Cited by 42
Presence of a mutation in PSEN1 or PSEN2 gene is associated with an impaired brain endothelial cell phenotype in vitro
Raut, S., Patel, R., & Al-Ahmad, A. J. (2021) · Fluids and Barriers of the CNS · doi:10.1186/s12987-020-00235-y · Cited by 42
The Inside-Out Amyloid Hypothesis and Synapse Pathology in Alzheimer's Disease
Gouras, G. K., Willén, K. I., & Faideau, M. (2013) · Neurodegenerative Diseases · doi:10.1159/000354776 · Cited by 42
[Retracted] Protective Effects of Rosa damascena and Its Active Constituent on Aβ(25–35)‐Induced Neuritic Atrophy
Awale, S., Tohda, C., Tezuka, Y., Miyazaki, M., & Kadota, S. (2009) · Evidence-based Complementary and Alternative Medicine · doi:10.1093/ecam/nep149 · Cited by 42
Retracted
Loss of endophilin-B1 exacerbates Alzheimer’s disease pathology
Wang, D. B., Kinoshita, Y., Kinoshita, C., Uo, T., Sopher, B. L., Cudaback, E., Keene, C. D., Bilousova, T. V., Gylys, K. H., Case, A., et al. (2015) · Brain · doi:10.1093/brain/awv128 · Cited by 42
β‐Amyloid Excitotoxicity in Rat Magnocellular Nucleus Basalis: Effect of Cortical Deafferentation on Cerebral Blood Flow Regulation and Implications for Alzheimer's Disease
Harkany, T., Penke, B., & Luiten, P. G. M. (2000) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2000.tb06389.x · Cited by 42
Amyloid β-peptide(1–40)-mediated oxidative stress in cultured hippocampal neurons
Aksenov, M. Y., Aksenova, M. V., Markesbery, W. R., & Butterfield, D. A. (1998) · Journal of Molecular Neuroscience · doi:10.1007/bf02761773 · Cited by 42
Tangle-associated neuritic clusters. A new lesion in Alzheimer's disease and aging suggests that aggregates of dystrophic neurites are not necessarily associated with beta/A4.
Muñoz, D. G., & Wang, D. (1992) · PubMed · Cited by 42
Differential regulation by β-amyloid peptides of intracellular free Ca2+ concentration in cultured rat microglia
Korotzer, A. R., Whittemore, E. R., & Cotman, C. W. (1995) · European Journal of Pharmacology Molecular Pharmacology · doi:10.1016/0922-4106(95)90006-3 · Cited by 42
Protein kinase inhibitor attenuates apoptotic cell death induced by amyloid β protein in culture of the rat cerebral cortex
Ueda, K., Yagami, T., Kageyama, H., & Kawasaki, K. (1996) · Neuroscience Letters · doi:10.1016/0304-3940(95)12288-5 · Cited by 42
Amyloid β-protein Induces Necrotic Cell Death Mediated by ICE Cascade in PC12 Cells
Suzuki, A. (1997) · Experimental Cell Research · doi:10.1006/excr.1997.3639 · Cited by 42
Neurotoxicity of Aβ amyloid protein in vitro is not altered by calcium channel blockade
Whitson, J. S., & Appel, S. H. (1995) · Neurobiology of Aging · doi:10.1016/0197-4580(95)80002-9 · Cited by 41
Mutations Alter the Geometry and Mechanical Properties of Alzheimer’s Aβ(1−40) Amyloid Fibrils
Paparcone, R., Pires, M. A., & Buehler, M. J. (2010) · Biochemistry · doi:10.1021/bi100953t · Cited by 41
All- d -Enantiomer of β-Amyloid Peptide Forms Ion Channels in Lipid Bilayers
Capone, R. F., Jang, H., Kotler, S. A., Connelly, L. S., Arce, F. T., Ramachandran, S., Kagan, B. L., Nussinov, R., & Lal, R. (2012) · Journal of Chemical Theory and Computation · doi:10.1021/ct200885r · Cited by 41
Erythropoietin prevents PC12 cells from beta-amyloid-induced apoptosis via PI3K⁄Akt pathway
Sun, Z., Yang, H., Wang, Z., Jing, P., Zhen, H., & Sheng-Di, C. (2012) · Translational Neurodegeneration · doi:10.1186/2047-9158-1-7 · Cited by 41
Acyl peptide hydrolase, a serine proteinase isolated from conditioned medium of neuroblastoma cells, degrades the amyloid‐β peptide
Yamin, R., Bagchi, S., Hildebrant, R., Scaloni, A., Widom, R. L., & Abraham, C. R. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04251.x · Cited by 41
A genome-wide association meta-analysis of plasma Aβ peptides concentrations in the elderly
Chouraki, V. A., de Bruijn, R. F. A. G., Chapuis, J., Bis, J. C., Reitz, C., Schraen‐Maschke, S., Ibrahim‐Verbaas, C. A., Grenier‐Boley, B., Delay, C., Rogers, R. S., et al. (2014) · Molecular Psychiatry · doi:10.1038/mp.2013.185 · Cited by 41
Cellular uptake of the prion protein fragment PrP106-126 in vitro
McHattie, S., Brown, D. R., & Bird, M. M. (1999) · Journal of Neurocytology · doi:10.1023/a:1007028323666 · Cited by 41
What is the dominant aβ species in human brain tissue? A review
Gregory, G. C., & Halliday, G. M. (2005) · Neurotoxicity Research · doi:10.1007/bf03033774 · Cited by 41
Protective effect of rhubarb derivatives on amyloid beta (1–42) peptide-induced apoptosis in IMR-32 cells: A case of nutrigenomic
Misiti, F., Sampaolese, B., Mezzogori, D., Orsini, F., Pezzotti, M., Giardina, B., & Clementi, M. E. (2006) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2006.07.012 · Cited by 41

Authors: Yankner, B. A., Duffy, L. K., & Kirschner, D. A.
Affiliations: Boston Children's Hospital (US)
University of Alaska Fairbanks (US)
ORCID: Yankner, Bruce A.
Duffy, Lawrence K.
Kirschner, Daniel A.
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 1990-10-12
Volume: 250
Issue: 4978
Pages: 279-282
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.2218531
OpenAlex: W2059214757
Cited by: 1,975
References: 31
Citations by year: 2026: 9 · 2025: 17 · 2024: 15 · 2023: 22 · 2022: 14 · 2021: 29 · 2020: 19 · 2019: 29 · 2018: 32 · 2017: 27 · 2016: 37 · 2015: 44 · 2014: 46 · 2013: 40 · 2012: 40
FWCI: 64.80
Type: journal article
Language: en
Open access: closed
Locations: Science (publishedVersion)
PubMed (publishedVersion)
Funders: National Institute on Aging (AG08572, R01AG008572)
National Institute of Neurological Disorders and Stroke (NS01240, K08NS001240)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuropeptides and Animal Physiology
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Keywords: amyloid-beta, Alzheimer's disease, neurotoxicity, neurotrophic effects, tachykinin antagonists, hippocampal neurons, neuronal differentiation, neuronal cell death, dendritic retraction, axonal retraction, neurotrophic factors
MeSH terms: Amino Acid Sequence, Animals, Cells, Cultured, Embryo, Mammalian, Hippocampus, Molecular Sequence Data, Neurons, Neurotoxins, Peptide Fragments, Tachykinins, Amyloid beta-Peptides, Rats

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Neurotrophic and Neurotoxic Effects of Amyloid β Protein: Reversal by Tachykinin Neuropeptides

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