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LAMP2A, and other chaperone-mediated autophagy related proteins, do not decline with age in genetically heterogeneous UM-HET3 mice
Chaperone-mediated autophagy (CMA) selectively degrades proteins that are crucial for glycolysis, fatty acid metabolism, and the progression of several age-associated diseases. Several previous studies, each of which evaluated males of a single inbred mouse or rat strain, have reported that CMA decl...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Impact Journals
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10292871/ https://www.ncbi.nlm.nih.gov/pubmed/37315291 http://dx.doi.org/10.18632/aging.204796 |
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author | Zhang, Katherine K. Zhang, Peichuan Kodur, Anagha Erturk, Ilkim Burns, Calvin M. Kenyon, Cynthia Miller, Richard A. Endicott, S. Joseph |
author_facet | Zhang, Katherine K. Zhang, Peichuan Kodur, Anagha Erturk, Ilkim Burns, Calvin M. Kenyon, Cynthia Miller, Richard A. Endicott, S. Joseph |
author_sort | Zhang, Katherine K. |
collection | PubMed |
description | Chaperone-mediated autophagy (CMA) selectively degrades proteins that are crucial for glycolysis, fatty acid metabolism, and the progression of several age-associated diseases. Several previous studies, each of which evaluated males of a single inbred mouse or rat strain, have reported that CMA declines with age in many tissues, attributed to an age-related loss of LAMP2A, the primary and indispensable component of the CMA translocation complex. This has led to a paradigm in the field of CMA research, stating that the age-associated decline in LAMP2A in turn decreases CMA, contributing to the pathogenesis of late-life disease. We assessed LAMP2A levels and CMA substrate uptake in both sexes of the genetically heterogeneous UM-HET3 mouse stock, which is the current global standard for the evaluation of anti-aging interventions. We found no evidence for age-related changes in LAMP2A levels, CMA substrate uptake, or whole liver levels of CMA degradation targets, despite identifying sex differences in CMA. |
format | Online Article Text |
id | pubmed-10292871 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Impact Journals |
record_format | MEDLINE/PubMed |
spelling | pubmed-102928712023-06-27 LAMP2A, and other chaperone-mediated autophagy related proteins, do not decline with age in genetically heterogeneous UM-HET3 mice Zhang, Katherine K. Zhang, Peichuan Kodur, Anagha Erturk, Ilkim Burns, Calvin M. Kenyon, Cynthia Miller, Richard A. Endicott, S. Joseph Aging (Albany NY) Research Paper Chaperone-mediated autophagy (CMA) selectively degrades proteins that are crucial for glycolysis, fatty acid metabolism, and the progression of several age-associated diseases. Several previous studies, each of which evaluated males of a single inbred mouse or rat strain, have reported that CMA declines with age in many tissues, attributed to an age-related loss of LAMP2A, the primary and indispensable component of the CMA translocation complex. This has led to a paradigm in the field of CMA research, stating that the age-associated decline in LAMP2A in turn decreases CMA, contributing to the pathogenesis of late-life disease. We assessed LAMP2A levels and CMA substrate uptake in both sexes of the genetically heterogeneous UM-HET3 mouse stock, which is the current global standard for the evaluation of anti-aging interventions. We found no evidence for age-related changes in LAMP2A levels, CMA substrate uptake, or whole liver levels of CMA degradation targets, despite identifying sex differences in CMA. Impact Journals 2023-06-13 /pmc/articles/PMC10292871/ /pubmed/37315291 http://dx.doi.org/10.18632/aging.204796 Text en Copyright: © 2023 Zhang et al. https://creativecommons.org/licenses/by/3.0/This is an open access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/3.0/) (CC BY 3.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Research Paper Zhang, Katherine K. Zhang, Peichuan Kodur, Anagha Erturk, Ilkim Burns, Calvin M. Kenyon, Cynthia Miller, Richard A. Endicott, S. Joseph LAMP2A, and other chaperone-mediated autophagy related proteins, do not decline with age in genetically heterogeneous UM-HET3 mice |
title | LAMP2A, and other chaperone-mediated autophagy related proteins, do not decline with age in genetically heterogeneous UM-HET3 mice |
title_full | LAMP2A, and other chaperone-mediated autophagy related proteins, do not decline with age in genetically heterogeneous UM-HET3 mice |
title_fullStr | LAMP2A, and other chaperone-mediated autophagy related proteins, do not decline with age in genetically heterogeneous UM-HET3 mice |
title_full_unstemmed | LAMP2A, and other chaperone-mediated autophagy related proteins, do not decline with age in genetically heterogeneous UM-HET3 mice |
title_short | LAMP2A, and other chaperone-mediated autophagy related proteins, do not decline with age in genetically heterogeneous UM-HET3 mice |
title_sort | lamp2a, and other chaperone-mediated autophagy related proteins, do not decline with age in genetically heterogeneous um-het3 mice |
topic | Research Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10292871/ https://www.ncbi.nlm.nih.gov/pubmed/37315291 http://dx.doi.org/10.18632/aging.204796 |
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