The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Matrix Metalloproteinase 14 Mediates APP Proteolysis and Lysosomal Alterations Induced by Oxidative Stress in Human Neuronal Cells
Abstract
The alteration of amyloid precursor protein (APP) proteolysis is a hallmark of Alzheimer’s disease (AD). Recent studies have described noncanonical pathways of APP processing that seem partly executed by lysosomal enzymes. Our laboratory’s in vitro human SK-N-MC model has shown that oxidative stress (OS) alters the lysosomal degradation pathway and the processing/metabolism of APP. The present study identifies the lysosomal protein matrix metalloproteinase 14 (MMP14) as a protease involved in the APP noncanonical processing. Previous expression analyses of the above cells showed MMP14 to be overexpressed under OS. In the present work, its role in changes in OS-induced APP proteolysis and lysosomal load was examined. The results show that MMP14 mediates the accumulation of an ≈85 kDa N-terminal APP fragment and increases the lysosome load induced by OS. These results were validated in neurons and neural progenitor cells generated from the induced pluripotent stem cells of patients with sporadic AD, reinforcing the idea that MMP14 may offer a therapeutic target in this disease.
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MT1-MMP, MMP-9 and MMP-2 are close MT5-MMP homologues involved in the control of APP metabolism and amyloidogenesis.
“all close MT5-MMP homologues, also involved in the control of APP metabolism and amyloidogenesis [33, 34, 54, 55]”
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Alzheimer's disease drug development pipeline: 2018
Cummings, J., Lee, G., Ritter, A., & Zhong, K. (2018) · Alzheimer's & Dementia: Translational Research & Clinical Interventions · doi:10.1016/j.trci.2018.03.009 · Cited by 697
Modeling Alzheimer’s disease with iPSC-derived brain cells
Penney, J., Ralvenius, W. T., & Tsai, L.-H. (2020) · Molecular Psychiatry · doi:10.1038/s41380-019-0468-3 · Cited by 471
η-Secretase processing of APP inhibits neuronal activity in the hippocampus
Willem, M., Tahirovic, S., Busche, M. A., Ovsepian, S. V., Chafai, M., Kootar, S., Hornburg, D., Evans, L. D. B., Moore, S., Daria, A., et al. (2015) · Nature · doi:10.1038/nature14864 · Cited by 398 · cited 3×
“According to the literature, this fragment is compatible with the action of noncanonical secretases, particularly MMP14, MMP24, and AEP [7, 8, 18].”
BackgroundEndo‐lysosomal and autophagic dysfunction: a driving factor in Alzheimer's disease?
Whyte, L. S., Lau, A. A., Hemsley, K. M., Hopwood, J. J., & Sargeant, T. J. (2017) · Journal of Neurochemistry · doi:10.1111/jnc.13935 · Cited by 150
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Pilat, D., Paumier, J.-M., García-González, L., Louis, L., Stephan, D., Manrique, C., Khrestchatisky, M., Di Pasquale, E., Baranger, K., & Rivera, S. (2022) · Journal of Neuroinflammation · doi:10.1186/s12974-022-02407-z · Cited by 28
Metadata
- Authors
- Llorente, P., Martins, S., Sastre, I., Aldudo, J., Recuero, M., Adjaye, J., & Bullido, M. J.
- Affiliations
- Centro de Biologia Molecular “Severo Ochoa” (C.S.I.C.-U.A.M.), Universidad Autonoma de Madrid, C/Nicolas Cabrera 1, 28049 Madrid, Spain
- Institute for Stem Cell Research and Regenerative Medicine, Medical Faculty, Heinrich-Heine-University Düsseldorf, Moorenstr. 5, 40225 Düsseldorf, Germany
- Venue
- Oxidative Medicine and Cellular Longevity
- Publisher
- Wiley
- Published
- 2020-11-16
- Volume
- 2020
- Pages
- 1-13
- ISSN
- 1942-0994
- 1942-0900
- PMC
- PMC7685830
- Cited by
- 10
- References
- 4
- Language
- en
- Funders
- Medical Faculty of Heinrich Heine University, Duesseldorf, Germany (SAF2017-85747-R)
- Banco de Santander to the Centro de Biología Molecular Severo Ochoa (SAF2017-85747-R)
- Fundación Ramón Areces (SAF2017-85747-R)
- Ministerio de Ciencia, Innovación y Universidades (SAF2017-85747-R)
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