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TERT Extra-Telomeric Roles: Antioxidant Activity and Mitochondrial Protection
Telomerase reverse transcriptase (TERT) is the catalytic subunit of telomerase holoenzyme, which adds telomeric DNA repeats on chromosome ends to counteract telomere shortening. In addition, there is evidence of TERT non-canonical functions, among which is an antioxidant role. In order to better inv...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10002448/ https://www.ncbi.nlm.nih.gov/pubmed/36901881 http://dx.doi.org/10.3390/ijms24054450 |
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author | Marinaccio, Jessica Micheli, Emanuela Udroiu, Ion Di Nottia, Michela Carrozzo, Rosalba Baranzini, Nicolò Grimaldi, Annalisa Leone, Stefano Moreno, Sandra Muzzi, Maurizio Sgura, Antonella |
author_facet | Marinaccio, Jessica Micheli, Emanuela Udroiu, Ion Di Nottia, Michela Carrozzo, Rosalba Baranzini, Nicolò Grimaldi, Annalisa Leone, Stefano Moreno, Sandra Muzzi, Maurizio Sgura, Antonella |
author_sort | Marinaccio, Jessica |
collection | PubMed |
description | Telomerase reverse transcriptase (TERT) is the catalytic subunit of telomerase holoenzyme, which adds telomeric DNA repeats on chromosome ends to counteract telomere shortening. In addition, there is evidence of TERT non-canonical functions, among which is an antioxidant role. In order to better investigate this role, we tested the response to X-rays and H(2)O(2) treatment in hTERT-overexpressing human fibroblasts (HF-TERT). We observed in HF-TERT a reduced induction of reactive oxygen species and an increased expression of the proteins involved in the antioxidant defense. Therefore, we also tested a possible role of TERT inside mitochondria. We confirmed TERT mitochondrial localization, which increases after oxidative stress (OS) induced by H(2)O(2) treatment. We next evaluated some mitochondrial markers. The basal mitochondria quantity appeared reduced in HF-TERT compared to normal fibroblasts and an additional reduction was observed after OS; nevertheless, the mitochondrial membrane potential and morphology were better conserved in HF-TERT. Our results suggest a protective function of TERT against OS, also preserving mitochondrial functionality. |
format | Online Article Text |
id | pubmed-10002448 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-100024482023-03-11 TERT Extra-Telomeric Roles: Antioxidant Activity and Mitochondrial Protection Marinaccio, Jessica Micheli, Emanuela Udroiu, Ion Di Nottia, Michela Carrozzo, Rosalba Baranzini, Nicolò Grimaldi, Annalisa Leone, Stefano Moreno, Sandra Muzzi, Maurizio Sgura, Antonella Int J Mol Sci Article Telomerase reverse transcriptase (TERT) is the catalytic subunit of telomerase holoenzyme, which adds telomeric DNA repeats on chromosome ends to counteract telomere shortening. In addition, there is evidence of TERT non-canonical functions, among which is an antioxidant role. In order to better investigate this role, we tested the response to X-rays and H(2)O(2) treatment in hTERT-overexpressing human fibroblasts (HF-TERT). We observed in HF-TERT a reduced induction of reactive oxygen species and an increased expression of the proteins involved in the antioxidant defense. Therefore, we also tested a possible role of TERT inside mitochondria. We confirmed TERT mitochondrial localization, which increases after oxidative stress (OS) induced by H(2)O(2) treatment. We next evaluated some mitochondrial markers. The basal mitochondria quantity appeared reduced in HF-TERT compared to normal fibroblasts and an additional reduction was observed after OS; nevertheless, the mitochondrial membrane potential and morphology were better conserved in HF-TERT. Our results suggest a protective function of TERT against OS, also preserving mitochondrial functionality. MDPI 2023-02-23 /pmc/articles/PMC10002448/ /pubmed/36901881 http://dx.doi.org/10.3390/ijms24054450 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Marinaccio, Jessica Micheli, Emanuela Udroiu, Ion Di Nottia, Michela Carrozzo, Rosalba Baranzini, Nicolò Grimaldi, Annalisa Leone, Stefano Moreno, Sandra Muzzi, Maurizio Sgura, Antonella TERT Extra-Telomeric Roles: Antioxidant Activity and Mitochondrial Protection |
title | TERT Extra-Telomeric Roles: Antioxidant Activity and Mitochondrial Protection |
title_full | TERT Extra-Telomeric Roles: Antioxidant Activity and Mitochondrial Protection |
title_fullStr | TERT Extra-Telomeric Roles: Antioxidant Activity and Mitochondrial Protection |
title_full_unstemmed | TERT Extra-Telomeric Roles: Antioxidant Activity and Mitochondrial Protection |
title_short | TERT Extra-Telomeric Roles: Antioxidant Activity and Mitochondrial Protection |
title_sort | tert extra-telomeric roles: antioxidant activity and mitochondrial protection |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10002448/ https://www.ncbi.nlm.nih.gov/pubmed/36901881 http://dx.doi.org/10.3390/ijms24054450 |
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