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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| Veröffentlicht in: | Aging (Albany, NY.) NY.), 2023-06, Vol.15 (11), p.4685-4698 |
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| container_title | Aging (Albany, NY.) |
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| creator | Zhang, Katherine K Zhang, Peichuan Kodur, Anagha Erturk, Ilkim Burns, Calvin M Kenyon, Cynthia Miller, Richard A Endicott, S Joseph |
| 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. |
| doi_str_mv | 10.18632/aging.204796 |
| format | Article |
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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.</description><identifier>ISSN: 1945-4589</identifier><identifier>EISSN: 1945-4589</identifier><identifier>DOI: 10.18632/aging.204796</identifier><identifier>PMID: 37315291</identifier><language>eng</language><publisher>United States: Impact Journals</publisher><subject>Aging - genetics ; Animals ; Autophagy - genetics ; Autophagy-Related Proteins - metabolism ; Chaperone-Mediated Autophagy - genetics ; Female ; Lysosomal-Associated Membrane Protein 2 - metabolism ; Lysosomes - metabolism ; Male ; Mice ; Molecular Chaperones - genetics ; Molecular Chaperones - metabolism ; Rats ; Research Paper</subject><ispartof>Aging (Albany, NY.), 2023-06, Vol.15 (11), p.4685-4698</ispartof><rights>Copyright: © 2023 Zhang et al.</rights><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c344t-8d767bf0a35e91580f704b9973978550eac9c9505c887dcacab7746ea614b4e83</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC10292871/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC10292871/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/37315291$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhang, Katherine K</creatorcontrib><creatorcontrib>Zhang, Peichuan</creatorcontrib><creatorcontrib>Kodur, Anagha</creatorcontrib><creatorcontrib>Erturk, Ilkim</creatorcontrib><creatorcontrib>Burns, Calvin M</creatorcontrib><creatorcontrib>Kenyon, Cynthia</creatorcontrib><creatorcontrib>Miller, Richard A</creatorcontrib><creatorcontrib>Endicott, S Joseph</creatorcontrib><title>LAMP2A, and other chaperone-mediated autophagy related proteins, do not decline with age in genetically heterogeneous UM-HET3 mice</title><title>Aging (Albany, NY.)</title><addtitle>Aging (Albany NY)</addtitle><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.</description><subject>Aging - genetics</subject><subject>Animals</subject><subject>Autophagy - genetics</subject><subject>Autophagy-Related Proteins - metabolism</subject><subject>Chaperone-Mediated Autophagy - genetics</subject><subject>Female</subject><subject>Lysosomal-Associated Membrane Protein 2 - metabolism</subject><subject>Lysosomes - metabolism</subject><subject>Male</subject><subject>Mice</subject><subject>Molecular Chaperones - genetics</subject><subject>Molecular Chaperones - metabolism</subject><subject>Rats</subject><subject>Research Paper</subject><issn>1945-4589</issn><issn>1945-4589</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVUU1v1DAUtBCIlsKRK_KRQ1Nsx58ntKpairQVHNqz5ThvE6OsHWwvaK_8ctLdUpXTe5o3mjejQeg9JRdUy5Z9ckOIwwUjXBn5Ap1Sw0XDhTYvn-0n6E0pPwiRQnD5Gp20qqWCGXqK_qxXt9_Z6hy72ONUR8jYj26GnCI0W-iDq9Bjt6tpHt2wxxmmAzLnVCHEco77hGOquAc_hQj4d6gjdgPgEPEAEWrwbpr2eIS6iD4gaVfw_W1zc3XX4m3w8Ba92ripwLvHeYbur6_uLm-a9bcvXy9X68a3nNdG90qqbkNcK8BQoclGEd4Zo1qjtBAEnDfeCCK81qr3zrtOKS7BSco7Dro9Q5-PuvOuW5J5iDW7yc45bF3e2-SC_f8Sw2iH9MtSwgzTii4KHx8Vcvq5g1LtNhQP0-QOqSzTTDIqFzsLtTlSfU6lZNg8_aHEHoqzh-LssbiF_-G5uSf2v6bavxzQlmU</recordid><startdate>20230613</startdate><enddate>20230613</enddate><creator>Zhang, Katherine K</creator><creator>Zhang, Peichuan</creator><creator>Kodur, Anagha</creator><creator>Erturk, Ilkim</creator><creator>Burns, Calvin M</creator><creator>Kenyon, Cynthia</creator><creator>Miller, Richard A</creator><creator>Endicott, S Joseph</creator><general>Impact Journals</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20230613</creationdate><title>LAMP2A, and other chaperone-mediated autophagy related proteins, do not decline with age in genetically heterogeneous UM-HET3 mice</title><author>Zhang, Katherine K ; Zhang, Peichuan ; Kodur, Anagha ; Erturk, Ilkim ; Burns, Calvin M ; Kenyon, Cynthia ; Miller, Richard A ; Endicott, S Joseph</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c344t-8d767bf0a35e91580f704b9973978550eac9c9505c887dcacab7746ea614b4e83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>Aging - genetics</topic><topic>Animals</topic><topic>Autophagy - genetics</topic><topic>Autophagy-Related Proteins - metabolism</topic><topic>Chaperone-Mediated Autophagy - genetics</topic><topic>Female</topic><topic>Lysosomal-Associated Membrane Protein 2 - metabolism</topic><topic>Lysosomes - metabolism</topic><topic>Male</topic><topic>Mice</topic><topic>Molecular Chaperones - genetics</topic><topic>Molecular Chaperones - metabolism</topic><topic>Rats</topic><topic>Research Paper</topic><toplevel>online_resources</toplevel><creatorcontrib>Zhang, Katherine K</creatorcontrib><creatorcontrib>Zhang, Peichuan</creatorcontrib><creatorcontrib>Kodur, Anagha</creatorcontrib><creatorcontrib>Erturk, Ilkim</creatorcontrib><creatorcontrib>Burns, Calvin M</creatorcontrib><creatorcontrib>Kenyon, Cynthia</creatorcontrib><creatorcontrib>Miller, Richard A</creatorcontrib><creatorcontrib>Endicott, S Joseph</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Aging (Albany, NY.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zhang, Katherine K</au><au>Zhang, Peichuan</au><au>Kodur, Anagha</au><au>Erturk, Ilkim</au><au>Burns, Calvin M</au><au>Kenyon, Cynthia</au><au>Miller, Richard A</au><au>Endicott, S Joseph</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>LAMP2A, and other chaperone-mediated autophagy related proteins, do not decline with age in genetically heterogeneous UM-HET3 mice</atitle><jtitle>Aging (Albany, NY.)</jtitle><addtitle>Aging (Albany NY)</addtitle><date>2023-06-13</date><risdate>2023</risdate><volume>15</volume><issue>11</issue><spage>4685</spage><epage>4698</epage><pages>4685-4698</pages><issn>1945-4589</issn><eissn>1945-4589</eissn><abstract>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.</abstract><cop>United States</cop><pub>Impact Journals</pub><pmid>37315291</pmid><doi>10.18632/aging.204796</doi><tpages>14</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Aging - genetics Animals Autophagy - genetics Autophagy-Related Proteins - metabolism Chaperone-Mediated Autophagy - genetics Female Lysosomal-Associated Membrane Protein 2 - metabolism Lysosomes - metabolism Male Mice Molecular Chaperones - genetics Molecular Chaperones - metabolism Rats Research Paper |
| title | LAMP2A, and other chaperone-mediated autophagy related proteins, do not decline with age in genetically heterogeneous UM-HET3 mice |
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