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The Catalytic Subunit of Telomerase Protects Neurons Against Amyloid β‐Peptide‐Induced Apoptosis
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Abstract : The catalytic subunit of telomerase (TERT) is a specialized reverse transcriptase that has been associated with cell immortalization and cancer. It was reported recently that TERT is expressed in neurons throughout the brain in embryonic and early postnatal development, but is absent from neurons in the adult brain. We now report that suppression of TERT levels and function in embryonic mouse hippocampal neurons in culture using antisense technology and the telomerase inhibitor 3' ‐azido‐2' 3' ‐dideoxythymidine significantly increases their vulnerability to cell death induced by amyloid β‐peptide, a neurotoxic protein believed to promote neuronal degeneration in Alzheimer's disease. Neurons in which TERT levels were reduced exhibited increased levels of oxidative stress and mitochondrial dysfunction following exposure to amyloid β‐peptide. Overexpression of TERT in pheochromocytoma cells resulted in decreased vulnerability to amyloid β‐peptide‐induced apoptosis. Our findings demonstrate a neuroprotective function of TERT in an experimental model relevant to Alzheimer's disease, and suggest the possibility that restoration of TERT expression in neurons in the adult brain may protect against age‐related neurodegeneration.
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“and against amyloid-β-induced cell death in embryonic mouse hippocampal neurons in vitro166”
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“Nevertheless, they already described a protective function of telomerase/TERT both during brain development [33] and also for neurodegeneration by treating neuronal cultures with amyloid-β (Aβ) [34].”
BackgroundAmyloid-β peptide triggers Fas-independent apoptosis and differentiation of neural progenitor cells
Millet, P., Lages, C. S., Haı̈k, S., Nowak, E., Allemand, I., Granotier, C., & Boussin, F. D. (2005) · Neurobiology of Disease · doi:10.1016/j.nbd.2004.11.006 · Cited by 36
Telomerase expression in amyotrophic lateral sclerosis (ALS) patients
Felice, B. D., Annunziata, A., Fiorentino, G., Manfellotto, F., D‘Alessandro, R., Marino, R., Borra, M., & Biffali, E. (2014) · Journal of Human Genetics · doi:10.1038/jhg.2014.72 · Cited by 35
Telomerase Activity is Downregulated Early During Human Brain Development
Ishaq, A., Hanson, P. S., Morris, C. M., & Saretzki, G. C. (2016) · Genes · doi:10.3390/genes7060027 · Cited by 34
“TERT protein has been found to reduce cellular ROS (reactive oxygen species) levels and inhibit endogenous ROS production and apoptosis induction in cultured human cells [17–20], as well as mouse neurons [3,21–23].”
BackgroundTERT Extra-Telomeric Roles: Antioxidant Activity and Mitochondrial Protection
Marinaccio, J., Micheli, E., Udroiu, I., Nottia, M. D., Carrozzo, R., Baranzini, N., Grimaldi, A., Leone, S., Moreno, S., Muzzi, M., et al. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24054450 · Cited by 35
“The enhanced resistance to oxidative stress observed in TERT-overexpressing cells could be related to increased levels of the ROS scavenger glutathione (GSH), as well as of manganese superoxide dismutase (MnSOD or SOD2) and forkhead-box-protein O3 (FoxO3a) proteins [25,26,31].”
BackgroundMicroenvironmental Regulation of Telomerase Isoforms in Human Embryonic Stem Cells
Radan, L., Hughes, C. S., Teichroeb, J. H., Zamora, F., Jewer, M., Postovit, L.-M. M., & Betts, D. H. (2014) · Stem Cells and Development · doi:10.1089/scd.2013.0373 · Cited by 34
“Since several TERT splice variants are abundantly expressed and individually do not exhibit telomeric function, alternative protein isoforms of TERT, especially those without reverse transcriptase activity, are a likely source of these noncanonical, extra-telomeric functions [44–47].”
Thomas, M., Suwa, T., Yang, L., Zhao, L., Hawks, C. L., & Hornsby, P. J. (2002) · Neoplasia · doi:10.1038/sj.neo.7900262 · Cited by 32
Telomerase induction in astrocytes of Sprague?Dawley rat after ischemic brain injury
Baek, S., Bu, Y., Kim, H., & Kim, H. (2004) · Neuroscience Letters · doi:10.1016/j.neulet.2004.03.059 · Cited by 30
Human Telomerase Reverse Transcriptase (hTERT) Positively Regulates 26S Proteasome Activity
Im, E., Yoon, J. B., Lee, H., & Chung, K. C. (2016) · Journal of Cellular Physiology · doi:10.1002/jcp.25607 · Cited by 28
“In addition, hTERT increases genomic stability and DNA repair (Sharma et al., 2003), and displays cytoprotective effects (Zhu et al., 2000; Honma et al., 2006).”
BackgroundDissecting the non-canonical functions of telomerase
Parkinson, E. K., Fitchett, C., & Cereser, B. (2008) · Cytogenetic and Genome Research · doi:10.1159/000167813 · Cited by 30
AATF protects neural cells against oxidative damage induced by amyloid β-peptide
Xie, J., & Guo, Q. (2004) · Neurobiology of Disease · doi:10.1016/j.nbd.2004.02.003 · Cited by 28
“Ah 1–42, the major component of amyloid plaques, has been shown to be neurotoxic and may cause apoptotic cell death in many in vitro and in vivo experimental setting (Guo et al., 1997; Kajkowski et al., 2001; Medina et al., 2002; Peng et al., 2002; Zhu et al., 2000).”
BackgroundTelomerase reverse transcriptase and neurodegenerative diseases
Yu, X., Liu, M., Zheng, C., Liu, Y., Wang, Z., & Wang, Z.-Y. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1165632 · Cited by 25
“Furthermore, neurons treated with TERT inhibitors were found to be more susceptible to Ab damage, while TERT was able to protect neurons from Ab-induced apoptosis in an experimental model of AD (78, 79).”
BackgroundTelomere attrition in lens epithelial cells - a target for N-acetylcarnosine therapy
Mark, A. B. (2010) · Frontiers in bioscience · doi:10.2741/3655 · Cited by 26
“For example, telomerase expression conferred increased resistance to specific DNA damaging agents (66,69,70) and decreased apoptosis (60,68,71,72).”
BackgroundZhao, F., Qu, Y., Xiong, T., Duan, Z., Ye, Q., & Mu, D. (2012) · Neuroscience Letters · doi:10.1016/j.neulet.2012.03.014 · Cited by 25
Ectopic telomerase expression inhibits neuronal differentiation of NT2 neural progenitor cells
Richardson, R. M., Nguyen, B., Holt, S. E., Broaddus, W. C., & Fillmore, H. L. (2007) · Neuroscience Letters · doi:10.1016/j.neulet.2007.03.079 · Cited by 25
Chiu, W., Shen, S., Yang, L., Chow, J., Wu, C.-Y., & Chen, Y. (2010) · Journal of Cellular Physiology · doi:10.1002/jcp.22536 · Cited by 23
“Ab1–42 and Ab1–43 are the major constituents of senile plaques in patients with AD (Zhu et al., 2000).”
Background
Metadata
- Authors
- Zhu, H., Fu, W., & Mattson, M. P.
- Affiliations
- University of Kentucky (US)
- National Institutes of Health (US)
- Venue
- Journal of Neurochemistry
- Publisher
- Wiley
- Published
- 2000-07
- Volume
- 75
- Issue
- 1
- Pages
- 117-124
- ISSN
- 0022-3042 (ISSN-L)
- 1471-4159
- OpenAlex
- W2071245320
- Cited by
- 175
- References
- 64
- Citations by year
- 2024: 2 · 2023: 3 · 2022: 4 · 2021: 5 · 2020: 7 · 2019: 5 · 2018: 6 · 2017: 6 · 2016: 7 · 2015: 8 · 2014: 7 · 2013: 10 · 2012: 3
- FWCI
- 7.98
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Neurochemistry (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Telomeres, Telomerase, and Senescence
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- telomerase reverse transcriptase, amyloid-beta, neuronal apoptosis, neuroprotection, Alzheimer's disease, oxidative stress, mitochondrial dysfunction, hippocampal neurons, telomerase inhibitors, zidovudine, age-related neurodegeneration
- MeSH terms
- Alzheimer Disease, Animals, Cells, Cultured, DNA-Binding Proteins, Embryo, Mammalian, Enzyme Inhibitors, Hippocampus, Immunohistochemistry, Mitochondria, Neurons, RNA, Gene Expression, Amyloid beta-Peptides, Oligonucleotides, Antisense, PC12 Cells, Apoptosis, Oxidative Stress, Telomerase, Catalytic Domain, Mice, Rats
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