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Degradation of the Alzheimer Disease Amyloid β-Peptide by Metal-dependent Up-regulation of Metalloprotease Activity
Open accessAbstract
Biometals play an important role in Alzheimer disease, and recent reports have described the development of potential therapeutic agents based on modulation of metal bioavailability. The metal ligand clioquinol (CQ) has shown promising results in animal models and small phase clinical trials; however, the actual mode of action in vivo has not been determined. We now report a novel effect of CQ on amyloid β-peptide (Aβ) metabolism in cell culture. Treatment of Chinese hamster ovary cells overexpressing amyloid precursor protein with CQ and Cu 2+ or Zn 2+ resulted in an ∼85–90% reduction of secreted Aβ-(1–40) and Aβ-(1–42) compared with untreated controls. Analogous effects were seen in amyloid precursor protein-overexpressing neuroblastoma cells. The secreted Aβ was rapidly degraded through up-regulation of matrix metalloprotease (MMP)-2 and MMP-3 after addition of CQ and Cu 2+ . MMP activity was increased through activation of phosphoinositol 3-kinase and JNK. CQ and Cu 2+ also promoted phosphorylation of glycogen synthase kinase-3, and this potentiated activation of JNK and loss of Aβ-(1–40). Our findings identify an alternative mechanism of action for CQ in the reduction of Aβ deposition in the brains of CQ-treated animals and potentially in Alzheimer disease patients.
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“MMPs are known to be linked to extracellular protein degradation including Aβ (72), whereas MMPs upregulated in AD may also confer neuroinflammation, synaptic dysfunction, and neuronal death (73, 74).”
From Modeling late-onset Alzheimer’s disease neuropathology via direct neuronal reprogramming (2024) · cites this paper as [72]
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Cites
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
Self-citationNeurodegenerative diseases and oxidative stress
Barnham, K. J., Masters, C. L., & Bush, A. I. (2004) · Nature Reviews Drug Discovery · doi:10.1038/nrd1330 · Cited by 3,683
Self-citationThe neurobiology of zinc in health and disease
Frederickson, C. J., Koh, J., & Bush, A. I. (2005) · Nature reviews. Neuroscience · doi:10.1038/nrn1671 · Cited by 1,841
Self-citationCherny, R. A., Atwood, C. S., Xilinas, M. E., Gray, D. N., Jones, W. D., McLean, C. A., Barnham, K. J., Volitakis, I., Fraser, F. W., Kim, Y.-S., et al. (2001) · Neuron · doi:10.1016/s0896-6273(01)00317-8 · Cited by 1,447
Self-citationThe metallobiology of Alzheimer's disease
Bush, A. I. (2003) · Trends in Neurosciences · doi:10.1016/s0166-2236(03)00067-5 · Cited by 1,315
Self-citationGSK-3α regulates production of Alzheimer's disease amyloid-β peptides
Phiel, C. J., Wilson, C., Lee, V. M. ‐., & Klein, P. S. (2003) · Nature · doi:10.1038/nature01640 · Cited by 1,211
Ritchie, C. W., Bush, A. I., Mackinnon, A., Macfarlane, S., Mastwyk, M., MacGregor, L., Kiers, L., Cherny, R., Li, Q.-X., Tammer, A., et al. (2003) · Archives of Neurology · doi:10.1001/archneur.60.12.1685 · Cited by 988
Self-citationMultiple Roles of the PI3K/PKB (Akt) Pathway in Cell Cycle Progression
Liang, J., & Slingerland, J. M. (2003) · Cell Cycle · doi:10.4161/cc.2.4.433 · Cited by 885
Leissring, M. A., Farris, W., Chang, A. Y., Walsh, D. M., Wu, X., Sun, X., Frosch, M. P., & Selkoe, D. J. (2003) · Neuron · doi:10.1016/s0896-6273(03)00787-6 · Cited by 725
Genetic or Pharmacological Iron Chelation Prevents MPTP-Induced Neurotoxicity In Vivo
Kaur, D., Yantiri, F., Rajagopalan, S., Kumar, J., Mo, J. Q., Boonplueang, R., Viswanath, V., Jacobs, R., Yang, L., Beal, M. F., et al. (2003) · Neuron · doi:10.1016/s0896-6273(03)00126-0 · Cited by 620
Self-citation
Research works printed but not linked: 2
- Miyata, 2004, Mol. Cancer Ther., 3, 839
- Wu, 1999, Am. J. Physiol., 277, L924
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Self-citationMcColl, G., Roberts, B. R., Pukala, T. L., Kenche, V. B., Roberts, C. M., Link, C. D., Ryan, T. M., Masters, C. L., Barnham, K. J., Bush, A. I., et al. (2012) · Molecular Neurodegeneration · doi:10.1186/1750-1326-7-57 · Cited by 257
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Leissring, M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r800022200 · Cited by 78
Fodero‐Tavoletti, M. T., Villemagne, V. L., Paterson, B. M., White, A. R., Li, Q., Camakaris, J., O'Keefe, G. J., Cappai, R., Barnham, K. J., & Donnelly, P. S. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-1359 · Cited by 83
Self-citationKupershmidt, L., Weinreb, O., Amit, T., Mandel, S. A., Bar‐Am, O., & Youdim, M. B. H. (2011) · Neuroscience · doi:10.1016/j.neuroscience.2011.03.040 · Cited by 80
Ferrada, E., Arancibia, V., Bárbara Loeb, L., Norambuena, E., Olea‐Azar, C., & Huidobro-Toro, J. P. (2007) · NeuroToxicology · doi:10.1016/j.neuro.2007.02.004 · Cited by 81
Weinreb, O., Amit, T., Mandel, S. A., Kupershmidt, L., & Youdim, M. B. H. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2929 · Cited by 80
Metals in alzheimer's disease: a systemic perspective
Squitti, R. (2011) · Frontiers in bioscience · doi:10.2741/3938 · Cited by 80
Cherny, R. A., Ayton, S., Finkelstein, D. I., Bush, A. I., McColl, G., & Massa, S. M. (2012) · Journal of Huntington s Disease · doi:10.3233/jhd-120029 · Cited by 78
Self-citationModeling late-onset Alzheimer’s disease neuropathology via direct neuronal reprogramming
Sun, Z., Kwon, J.-S., Ren, Y., Chen, S., Walker, C. K., Lu, X., Cates, K., Karahan, H., Sviben, S., Fitzpatrick, J. A. J., et al. (2024) · Science · doi:10.1126/science.adl2992 · Cited by 77
“MMPs are known to be linked to extracellular protein degradation including A β (72), whereas MMPs upregulated in AD may also confer neuroinflammation, synaptic dysfunction, and neuronal death (73, 74).”
Crouch, P. J., White, A. R., & Bush, A. I. (2007) · FEBS Journal · doi:10.1111/j.1742-4658.2007.05918.x · Cited by 78
Self-citationInsights into the pathogenesis and pathogenicity of cerebral amyloid angiopathy
Love, S. (2009) · Frontiers in bioscience · doi:10.2741/3567 · Cited by 78
Aspects of β-Amyloid as a Biomarker for Alzheimer's Disease
Andréasson, U., Portelius, E., Andersson, M. E., Blennow, K., & Zetterberg, H. (2007) · Biomarkers in Medicine · doi:10.2217/17520363.1.1.59 · Cited by 74
The role of GSK3 in Alzheimer disease
Hernández, F., de Barreda, E. G., Fuster-Matanzo, A., Goñi‐Oliver, P., Lucas, J. J., & Ávila, J. (2009) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2009.05.017 · Cited by 73
Ryan, T. M., Roberts, B. R., McColl, G., Hare, D. J., Doble, P., Li, Q., Lind, M., Roberts, A. M., Mertens, H. D. T., Kirby, N. M., et al. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.2912-14.2015 · Cited by 74
Self-citation
Metadata
- Authors
- White, A. R., Du, T., Laughton, K. M., Volitakis, I., Sharples, R. A., Xilinas, M. E., Hoke, D. E., Holsinger, R. M. D., Evin, G., Cherny, R. A., Hill, A. F., Barnham, K. J., Li, Q.-X., Bush, A. I., & Masters, C. L.
- Affiliations
- Mental Health Research Institute (AU)
- Corresponding author
- White, Anthony R.
- ORCID
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2006-06
- Volume
- 281
- Issue
- 26
- Pages
- 17670-17680
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2131181742
- Cited by
- 284
- References
- 44
- Citations by year
- 2026: 5 · 2025: 3 · 2024: 10 · 2023: 6 · 2022: 4 · 2021: 10 · 2020: 17 · 2019: 5 · 2018: 6 · 2017: 11 · 2016: 13 · 2015: 18 · 2014: 16 · 2013: 12 · 2012: 21
- FWCI
- 16.39
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- Victoria University Research Repository (Victoria University) (submittedVersion, cc-by)
- Funders
- National Institute on Aging (R01-AG12686, AG 05887)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- Alzheimer's disease, amyloid-beta, clioquinol, MMP-2, MMP-3, copper, zinc, amyloid precursor protein, phosphatidylinositol 3-kinase, JNK, glycogen synthase kinase-3, metal bioavailability, biometals
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