Cited by 1,447Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

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Production of the Alzheimer Amyloid β Protein by Normal Proteolytic Processing

Shoji, Mikio, Golde, Todd E., Ghiso, Jorge, Cheung, Tobun T., Estus, Steven, Shaffer, Lillian M., Cai, Xiao-Dan, McKay, Deborah M., Tintner, Ron, Frangione, Bias, Younkin, Steven G.·1992·Science

DOI 10.1126/science.1439760

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Abstract

The 4-kilodalton (39 to 43 amino acids) amyloid β protein (βAP), which is deposited as amyloid in the brains of patients with Alzheimer's disease, is derived from a large protein, the amyloid β protein precursor (βAPP). Human mononuclear leukemic (K562) cells expressing a βAP-bearing, carboxyl-terminal βAPP derivative released significant amounts of a soluble 4-kilodalton βAPP derivative essentially identical to the βAP deposited in Alzheimer's disease. Human neuroblastoma (M17) cells transfected with constructs expressing full-length βAPP and M17 cells expressing only endogenous βAPP also released soluble 4-kilodalton βAP, and a similar, if not identical, fragment was readily detected in cerebrospinal fluid from individuals with Alzheimer's disease and normal individuals. Thus cells normally produce and release soluble 4-kilodalton βAP that is essentially identical to the 4-kilodalton βAP deposited as insoluble amyloid fibrils in Alzheimer's disease.

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Clinical diagnosis of Alzheimer's disease: Report of the NINCDS‐ADRDA Work Group* under the auspices of Department of Health and Human Services Task Force on Alzheimer's Disease
McKhann, G., Drachman, D., Folstein, M., Katzman, R., Price, D., & Stadlan, E. M. (1984) · Neurology · doi:10.1212/wnl.34.7.939 · Cited by 27,915
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
Alzheimer's disease and Down's syndrome: Sharing of a unique cerebrovascular amyloid fibril protein
Glenner, G. G., & Wong, C. W. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(84)91209-9 · Cited by 1,693
Amyloid β Protein Gene: cDNA, mRNA Distribution, and Genetic Linkage Near the Alzheimer Locus
Tanzi, R. E., Gusella, J. F., Watkins, P. C., Bruns, G. A. P., St George-Hyslop, P., Van Keuren, M. L., Patterson, D., Pagan, S., Kurnit, D. M., & Neve, R. L. (1987) · Science · doi:10.1126/science.2949367 · Cited by 1,611
Cleavage of Amyloid β Peptide During Constitutive Processing of Its Precursor
Esch, F. S., Keim, P. S., Beattie, E. C., Blacher, R. W., Culwell, A. R., Oltersdorf, T., McClure, D., & Ward, P. J. (1990) · Science · doi:10.1126/science.2111583 · Cited by 1,403
Characterization and Chromosomal Localization of a cDNA Encoding Brain Amyloid of Alzheimer's Disease
Goldgaber, D., Lerman, M. I., McBride, O. W., Saffiotti, U., & Gajdusek, D. C. (1987) · Science · doi:10.1126/science.3810169 · Cited by 1,359
Identification, biogenesis, and localization of precursors of Alzheimer's disease A4 amyloid protein
Weidemann, A., König, G., Bunke, D., Fischer, P. Q., Salbaum, J. M., Masters, C. L., & Beyreuther, K. T. (1989) · Cell · doi:10.1016/0092-8674(89)90177-3 · Cited by 1,233
Assembly and aggregation properties of synthetic Alzheimer's A4/beta amyloid peptide analogs.
Burdick, D., Soreghan, B., Kwon, M., Kosmoski, J., Knauer, M., Henschen, A., Yates, J., Cotman, C., & Glabe, C. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48529-8 · Cited by 1,014
Targeting of cell-surface β-amyloid precursor protein to lysosomes: alternative processing into amyloid-bearing fragments
Haass, C., Koo, E. H., Mellon, A., Hung, A. Y., & Selkoe, D. J. (1992) · Nature · doi:10.1038/357500a0 · Cited by 919

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Show all 32 references

Research works printed but not linked: 5

Cole, G. M., Molecular Biology and Genetics of Alzheimer's Disease: 113 (1990).
FRUCHT, S. J., JOURNAL OF NEUROPATHOLOGY AND EXPERIMENTAL NEUROLOGY 51: 369 (1992).
GLENNER, G, BRANBURY REPORT 15: 137 (1983).
KIM, K.S., NEUROSCIENCE RESEARCH COMMUNICATIONS 2: 121 (1988).
TERRY, R.D., BRAIN 311: 528 (1963).

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Cruz, L., Urbanc, B., Buldyrev, S. V., Christie, R. H., Gómez‐Isla, T., Havlin, S., McNamara, M. J., Stanley, E., & Hyman, B. T. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.14.7612 · Cited by 115
Cell surface APP751 forms complexes with protease nexin 2 ligands and is internalized via the low density lipoprotein receptor-related protein (LRP)
Knauer, M. F., Orlando, R. A., & Glabe, C. G. (1996) · Brain Research · doi:10.1016/s0006-8993(96)00711-1 · Cited by 115
Extracellular deposition of beta-amyloid upon p53-dependent neuronal cell death in transgenic mice.
LaFerla, F. M., Hall, C. K., Ngo, L. T., & Jay, G. D. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118957 · Cited by 112
Functional Expression and Localization of P-glycoprotein in the Central Nervous System: Relevance to the Pathogenesis and Treatment of Neurological Disorders
Lee, G. S., & Bendayan, R. (2004) · Pharmaceutical Research · doi:10.1023/b:pham.0000036905.82914.8e · Cited by 116
Preferential adsorption, internalization and resistance to degradation of the major isoform of the Alzheimer's amyloid peptide, Aβ1–42, in differentiated PC12 cells
Burdick, D., Kosmoski, J., Knauer, M. F., & Glabe, C. G. (1997) · Brain Research · doi:10.1016/s0006-8993(96)01262-0 · Cited by 102
Cell-type and Amyloid Precursor Protein-type Specific Inhibition of Aβ Release by Bafilomycin A1, a Selective Inhibitor of Vacuolar ATPases
Knops, J., Suomensaari, S., Lee, M., McConlogue, L., Seubert, P. A., & Sinha, S. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.6.2419 · Cited by 118
Accumulation of β‐amyloid precursor protein in HIV encephalitis: Relationship with neuropsychological abnormalities
Giometto, B., An, S., Groves, M., Scaravilli, T., Geddes, J. F., Miller, R., Tavolato, B. F., Beckett, A. A. J., & Scaravilli, F. (1997) · Annals of Neurology · doi:10.1002/ana.410420108 · Cited by 114
Examining the zinc binding site of the amyloid‐β peptide
Yang, D., McLaurin, J., Qin, K., Westaway, D. A., & Fraser, P. E. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01767.x · Cited by 113
Alzheimer's Disease, β-Amyloid Protein and Zinc
Huang, X., Cuajungco, M. P., Atwood, C., Moir, R. D., Tanzi, R. E., & Bush, A. I. (2000) · Journal of Nutrition · doi:10.1093/jn/130.5.1488s · Cited by 114
Regulation of β-amyloid precursor protein isoform mRNAs by transforming growth factor-β1 and interleukin-1β in astrocytes
Gray, C. W., & Patel, A. J. (1993) · Molecular Brain Research · doi:10.1016/0169-328x(93)90037-p · Cited by 117
Cerebrospinal fluid levels of amyloid β‐protein in alzheimer's disease: Inverse correlation with severity of dementia and effect of apolipoprotein e genotype
Nitsch, R. M., Rebeck, G. W., Deng, M., Richardson, U. I., Tennis, M., Schenk, D. B., Vigo‐Pelfrey, C., Lieberburg, I., Wurtman, R. J., Hyman, B. T., et al. (1995) · Annals of Neurology · doi:10.1002/ana.410370414 · Cited by 113
Passage of human amyloid β-protein 1–40 across the murine blood-brain barrier
Maness, L. M., Banks, W. A., Podlisny, M. B., Selkoe, D. J., & Kastin, A. J. (1994) · Life Sciences · doi:10.1016/0024-3205(94)00331-9 · Cited by 97
Treatment with the selective muscarinic ml agonist talsaclidine decreases cerebrospinal fluid levels of Aβ42in patients with Alzheimer's disease
Höck, C., Maddalena, A. S., Raschig, A., Müller-Spahn, F., Eschweiler, G. W., Huger, K., Hewer, I., Hampel, H. J., Müller-Thornsen, T., Oertel, W. H., et al. (2003) · Amyloid · doi:10.3109/13506120308995249 · Cited by 110
Alzheimer's disease and soluble Aβ
Wısnıewskı, T., Ghiso, J. A., & Frangione, B. (1994) · Neurobiology of Aging · doi:10.1016/0197-4580(94)90105-8 · Cited by 112
Self-citation
Amyloid Peptide-Induced Cytokine and Chemokine Expression in THP-1 Monocytes Is Blocked by Small Inhibitory RNA Duplexes for Early Growth Response-1 Messenger RNA
Giri, R. K., Selvaraj, S. K., & Kalra, V. K. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.170.10.5281 · Cited by 111
Cognitive changes and modified processing of amyloid precursor protein in the cortical and hippocampal system after cholinergic synapse loss and muscarinic receptor activation
Lin, L., Georgievska, B., Mattsson, A., & Ole Isacson, A. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.21.12108 · Cited by 110
Amyloid-β(1–42) Aggregation Initiates Its Cellular Uptake and Cytotoxicity
Jin, S., Kedia, N., Illes‐Toth, E., Haralampiev, I., Prisner, S., Herrmann, A., Wanker, E. E., & Bieschke, J. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.691840 · Cited by 109
A Reductionist View of Alzheimer's Disease
Lansbury, P. T. (1996) · Accounts of Chemical Research · doi:10.1021/ar950159u · Cited by 109
Cell Surface Amyloid β-Protein Precursor Colocalizes with β1 Integrins at Substrate Contact Sites in Neural Cells
Yamazaki, T., Koo, E. H., & Selkoe, D. J. (1997) · Journal of Neuroscience · doi:10.1523/jneurosci.17-03-01004.1997 · Cited by 147
Synaptic Dysfunction in Alzheimer’s Disease
Marcello, E. E., Epis, R., Saraceno, C., & Luca, M. D. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-3-7091-0932-8_25 · Cited by 115
Aminopeptidase A contributes to the N‐terminal truncation of amyloid β‐peptide
Sévalle, J., Amoyel, A., Robert, P. H., Fournié‐Zaluski, M., Roques, B. P., & Checler, F. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.05950.x · Cited by 108
Huperzine A Activates Wnt/β-Catenin Signaling and Enhances the Nonamyloidogenic Pathway in an Alzheimer Transgenic Mouse Model
Wang, C., Zheng, W. H., Wang, T., Xie, J., Wang, S., Zhao, B., Teng, W., & Wang, Z. (2011) · Neuropsychopharmacology · doi:10.1038/npp.2010.245 · Cited by 108
β‐Amyloid protein oligomers induced by metal ions and acid pH are distinct from those generated by slow spontaneous ageing at neutral pH
Klug, G. M., Lošić, D., Supundi, Subasinghe, S., Aguilar, M., Martin, L. L., & Small, D. H. (2003) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2003.03815.x · Cited by 109
Substitution at codon 22 reduces clearance of Alzheimer's amyloid-β peptide from the cerebrospinal fluid and prevents its transport from the central nervous system into blood
Monro, O. (2002) · Neurobiology of Aging · doi:10.1016/s0197-4580(01)00317-7 · Cited by 107
Cell‐free assays for γ‐secretase activity
McLendon, C., Xin, T. A., Ziani‐Cherif, C., Murphy, M. P., Findlay, K. A., Lewis, P. A., Pinnix, I., Sambamurti, K., Wang, R., Fauq, A. H., et al. (2000) · The FASEB Journal · doi:10.1096/fj.00-0286fje · Cited by 106
Self-citation
Transglutaminase facilitates the formation of polymers of the β-amyloid peptide
Dudek, S. M., & Johnson, G. V. W. (1994) · Brain Research · doi:10.1016/0006-8993(94)90688-2 · Cited by 106
The Cell-Selective Neurotoxicity of the Alzheimer's Aβ Peptide Is Determined by Surface Phosphatidylserine and Cytosolic ATP Levels. Membrane Binding Is Required for Aβ Toxicity
Šimáková, O., & Arispe, N. J. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.3006-07.2007 · Cited by 106
Generation of βA4 from the amyloid protein precursor and fragments thereof
Dyrks, T., Dyrks, E., Mönning, U., Urmoneit, B., Turner, J. D., & Beyreuther, K. T. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)80446-2 · Cited by 105
Review: Model Peptides and the Physicochemical Approach to β-Amyloids
Lynn, D. G., & Meredith, S. C. (2000) · Journal of Structural Biology · doi:10.1006/jsbi.2000.4287 · Cited by 105
Proteolytic Processing of Alzheimer's Disease βA4 Amyloid Precursor Protein in Human Platelets
Li, Q., Evin, G. M., Small, D. H., Multhaup, G., Beyreuther, K. T., & Masters, C. L. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.23.14140 · Cited by 105
Accumulation of intercellular adhesion molecule-1 in senile plaques in brain tissue of patients with Alzheimer's disease.
(1994) · PubMed Central · Cited by 105
Apolipoprotein E polymorphism and susceptibility to Alzheimer's disease.
Kamboh, M. I. (1995) · PubMed · Cited by 105
The involvement of mitogen‐activated protein (MAP) kinase in the regulation of amyloid precursor protein processing by novel cholinesterase inhibitors derived from rasagiline
Yogev‐Falach, M., Amit, T., Bar‐Am, O., Weinstock, M., & Youdim, M. B. H. (2002) · The FASEB Journal · doi:10.1096/fj.02-0198fje · Cited by 104

Authors: Shoji, M., Golde, T. E., Ghiso, J., Cheung, T. T., Estus, S., Shaffer, L. M., Cai, X.-D., McKay, D. M., Tintner, R., Frangione, B., & Younkin, S. G.
Affiliations: Gunma University (JP)
Case Western Reserve University (US)
NYU Langone Health (US)
Washington University in St. Louis (US)
The University of Texas Southwestern Medical Center (US)
ORCID: Shoji, Mikio
Golde, Todd E.
Ghiso, Jorge
Estus, Steven
Younkin, Steven G.
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 1992-10-02
Volume: 258
Issue: 5079
Pages: 126-129
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.1439760
OpenAlex: W2033382511
Cited by: 1,447
References: 32
Citations by year: 2026: 4 · 2025: 6 · 2024: 16 · 2023: 13 · 2022: 13 · 2021: 18 · 2020: 23 · 2019: 16 · 2018: 18 · 2017: 15 · 2016: 37 · 2015: 26 · 2014: 28 · 2013: 38 · 2012: 37
FWCI: 80.08
Type: journal article
Language: en
Open access: closed
Locations: Science (publishedVersion)
PubMed (publishedVersion)
Funders: National Institute on Aging (AG06656, R01AG006656, AG05891)
National Institute of Arthritis and Musculoskeletal and Skin Diseases (AR02594)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › 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, Alzheimer's disease, amyloid precursor protein, proteolytic processing, soluble amyloid-beta, amyloid fibrils, cerebrospinal fluid, K562 cells, neuroblastoma cells, transfection, protein secretion
MeSH terms: Alzheimer Disease, Amino Acid Sequence, Animals, Base Sequence, Cell Line, Leukemia, Myeloid, Molecular Sequence Data, Neuroblastoma, Transfection, Immunoblotting, Amyloid beta-Peptides, Amyloid beta-Protein Precursor

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Production of the Alzheimer Amyloid β Protein by Normal Proteolytic Processing

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