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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...

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Autores principales: Zhang, Katherine K., Zhang, Peichuan, Kodur, Anagha, Erturk, Ilkim, Burns, Calvin M., Kenyon, Cynthia, Miller, Richard A., Endicott, S. Joseph
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Impact Journals 2023
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.
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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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