Cited by 391Alzheimer's disease research and treatmentsNeuroinflammation and Neurodegeneration MechanismsNF-κB Signaling Pathways

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Tumor Necrosis Factor-α, Interleukin-1β, and Interferon-γ Stimulate γ-Secretase-mediated Cleavage of Amyloid Precursor Protein through a JNK-dependent MAPK Pathway

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Liao, Yung-Feng, Wang, Bo-Jeng, Cheng, Hui-Ting, Kuo, Lan-Hsin, Wolfe, Michael S.·2004·Journal of Biological Chemistry

DOI 10.1074/jbc.m402034200

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Abstract

The deposition of the amyloid beta (Abeta) peptide in neuritic plaques plays a critical role in the pathogenesis of Alzheimer's disease (AD). Abeta is generated through the proteolysis of amyloid precursor protein (APP) by the sequential actions of beta- and gamma-secretases. Although recent evidence has unveiled much about the biochemical identity and characteristics of gamma-secretase, the mechanism regulating endogenous gamma-secretase activity remains elusive. To identify possible extracellular signals and associated signaling cascades that could regulate APP proteolysis by gamma-secretase activity, we have developed a cell-based reporter gene assay by stably cotransfecting HEK293 cells with the Gal4-driven luciferase reporter gene and the Gal4/VP16-tagged C-terminal fragment of APP (C99-GV), the immediate substrate of gamma-secretase. The cleavage of C99-GV by gamma-secretase releases the transcription factor that activates luciferase expression, providing a quantitative measurement of gamma-secretase activity. Using this reporter assay, we have demonstrated that interferon-gamma, interleukin-1beta, and tumor necrosis factor-alpha can specifically stimulate gamma-secretase activity, concomitant with increased production of Abeta and the intracellular domain of APP (AICD). The gamma-secretase-dependent cleavage of Notch is also enhanced upon the stimulation of these cytokines. The cytokine-enhanced gamma-secretase activity can be suppressed by a potent inhibitor of c-Jun N-terminal kinase (JNK). Furthermore, cells transfected with dominant-positive MEKK1, one of the most potent activators of the JNK cascade, exhibit increased gamma-secretase activity, suggesting that the JNK-dependent mitogen-activated protein kinase pathway could mediate the cytokine-elicited regulation of gamma-secretase. Our studies provide direct evidence that cytokine-elicited signaling cascades control Abeta production by modulating gamma-secretase activity.

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Alzheimer's Disease: Genes, Proteins, and Therapy
Selkoe, D. J. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.2.741 · Cited by 6,063
Nuclear Factor-κB — A Pivotal Transcription Factor in Chronic Inflammatory Diseases
Barnes, P. J., & Karin, M. (1997) · New England Journal of Medicine · doi:10.1056/nejm199704103361506 · Cited by 4,622
Inflammation and Alzheimer’s disease
Akiyama, H. (2000) · Neurobiology of Aging · doi:10.1016/s0197-4580(00)00124-x · Cited by 4,514
SP600125, an anthrapyrazolone inhibitor of Jun N-terminal kinase
Bennett, B. L., Sasaki, D. T., Murray, B. W., O'Leary, E. C., Sakata, S. T., Xu, W., Leisten, J. C., Motiwala, A., Pierce, S., Satoh, Y., et al. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.251194298 · Cited by 2,558
Signal transduction by tumor necrosis factor and its relatives.
Baud, V., & Karin, M. (2001) · Trends in Cell Biology · doi:10.1016/s0962-8924(01)02064-5 · Cited by 1,741
Notch-1 signalling requires ligand-induced proteolytic release of intracellular domain
Schroeter, E. H., Kisslinger, J. A., & Kopan, R. (1998) · Nature · doi:10.1038/30756 · Cited by 1,624
Amyloid, the presenilins and Alzheimer’s disease
Hardy, J. (1997) · Trends in Neurosciences · doi:10.1016/s0166-2236(96)01030-2 · Cited by 1,370
The Molecular Cell Biology of Interferon-Gamma and Its Receptor
Farrar, M. A., & Schreiber, R. D. (1993) · Annual Review of Immunology · doi:10.1146/annurev.iy.11.040193.003035 · Cited by 1,353
Differential Activation of ERK and JNK Mitogen-Activated Protein Kinases by Raf-1 and MEKK
Minden, A., Lin, A., McMahon, M., Lange, C. A., Dérijard, B., Davis, R. J., Johnson, G. L., & Karin, M. (1994) · Science · doi:10.1126/science.7992057 · Cited by 1,069
Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and βAPP processing
Yu, G., Nishimura, M., Arawaka, S., Levitan, D. J., Zhang, L., Tandon, A., Song, Y., Rogaeva, E. A., Chen, F., Kawarai, T., et al. (2000) · Nature · doi:10.1038/35024009 · Cited by 929

Show all 57 references

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Kim, E. K., & Choi, E.-J. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.12.009 · Cited by 2,472
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Kinney, J. W., Bemiller, S. M., Murtishaw, A. S., Leisgang, A. M., Salazar, A. M., & Lamb, B. T. (2018) · Alzheimer's & Dementia: Translational Research & Clinical Interventions · doi:10.1016/j.trci.2018.06.014 · Cited by 2,253
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“TNF , IL-1 , and interferon- were also found to stimulate -secretase-mediated cleavage of APP (Liao et al., 2004).”
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Lukiw, W. J. (2005) · Journal of Clinical Investigation · doi:10.1172/jci25420 · Cited by 897
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Self-citation

Authors: Liao, Y.-F., Wang, B.-J., Cheng, H.-T., Kuo, L.-H., & Wolfe, M. S.
Affiliations: Academia Sinica (TW)
Brigham and Women's Hospital (US)
Corresponding author: Liao, Yung-Feng
ORCID: Liao, Yung-Feng
Wolfe, Michael S.
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 2004-11
Volume: 279
Issue: 47
Pages: 49523-49532
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.m402034200
OpenAlex: W1992680479
Cited by: 389
References: 57
Citations by year: 2026: 12 · 2025: 16 · 2024: 29 · 2023: 28 · 2022: 25 · 2021: 21 · 2020: 22 · 2019: 16 · 2018: 14 · 2017: 12 · 2016: 13 · 2015: 13 · 2014: 15 · 2013: 25 · 2012: 14
FWCI: 9.04
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 5833 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Funders: Alzheimer's Association
National Science Council
Academia Sinica
National Institutes of Health
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
Keywords: gamma-secretase, amyloid precursor protein, amyloid-beta, Alzheimer's disease, TNF-α, IL-1β, interferon-gamma, JNK, MAPK signaling, MEKK1, Notch cleavage, APP intracellular domain, cytokine signaling
MeSH terms: Animals, Cell Line, DNA, Dose-Response Relationship, Drug, Electrophoresis, Polyacrylamide Gel, Enzyme-Linked Immunosorbent Assay, Genes, Dominant, Humans, Interferon-gamma, Interleukin-1, Luciferases, Membrane Proteins, Mutation, Endopeptidases, Transfection, Tumor Necrosis Factor-alpha, Blotting, Western, Signal Transduction, Aspartic Acid Endopeptidases, Amyloid beta-Protein Precursor, Culture Media, Serum-Free, Protein Structure, Tertiary, Genes, Reporter, COS Cells, Mitogen-Activated Protein Kinase Kinases, MAP Kinase Signaling System, JNK Mitogen-Activated Protein Kinases, MAP Kinase Kinase 4, Receptors, Notch, Amyloid Precursor Protein Secretases

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Tumor Necrosis Factor-α, Interleukin-1β, and Interferon-γ Stimulate γ-Secretase-mediated Cleavage of Amyloid Precursor Protein through a JNK-dependent MAPK Pathway

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