
DOI . ORG {
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Title[redir]:
Restoration of chaperone-mediated autophagy in aging liver improves cellular maintenance and hepatic function | Nature Medicine
Description:
Chaperone-mediated autophagy (CMA), a mechanism for the lysosomal degradation of proteins, declines in aging cells. Using transgenic mice in which such a decline does not occur in the liver, the authors found that preserving CMA leads to reduced accumulation of damaged proteins and improved organ function in aged mice ( pages 909–910 ). Chaperone-mediated autophagy (CMA), a selective mechanism for degradation of cytosolic proteins in lysosomes, contributes to the removal of altered proteins as part of the cellular quality-control systems1,2. We have previously found that CMA activity declines in aged organisms and have proposed that this failure in cellular clearance could contribute to the accumulation of altered proteins, the abnormal cellular homeostasis and, eventually, the functional loss characteristic of aged organisms. To determine whether these negative features of aging can be prevented by maintaining efficient autophagic activity until late in life, in this work we have corrected the CMA defect in aged rodents. We have generated a double transgenic mouse model in which the amount of the lysosomal receptor for CMA, previously shown to decrease in abundance with age3, can be modulated. We have analyzed in this model the consequences of preventing the age-dependent decrease in receptor abundance in aged rodents at the cellular and organ levels. We show here that CMA activity is maintained until advanced ages if the decrease in the receptor abundance is prevented and that preservation of autophagic activity is associated with lower intracellular accumulation of damaged proteins, better ability to handle protein damage and improved organ function.
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Keywords {🔍}
mice, liver, aged, lysosomes, fig, transgenic, article, cma, pubmed, lysosomal, proteins, wildtype, autophagy, mouse, groups, google, scholar, protein, activity, lampa, supplementary, nature, cellular, cas, aging, monthold, livers, abundance, age, sections, function, content, chaperonemediated, cuervo, doxycycline, degradation, membrane, albtetoffla, young, amount, online, group, analysis, shown, levels, improved, cells, isolated, higher, differences,
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nature portfolio permissions reprints privacy policy nature medicine website ladd research industries fluorogenic substrate arg-arg-7-amc28 advertising aging research social media ana maria cuervo author information authors nature 451 nature chaperone-mediated autophagy depends index full access transgenic tre-lamp-2a mouse grant access discard insertion-related effects chaperone-substrate complex binds author correspondence periodic acid–schiff stain peptidylglutamyl-peptide hydrolase activities chaperone-mediated autophagy celltiter-glo assay kit initial acid-precipitable radioactivity older wild-type littermates cellular quality-control systems1 macroautophagy effector atg5-atg12 zoxazolamine-induced paralysis test permissions nen-life science products aged wild-type mice young wild-type mice long-term feeding fluorescence-conjugated secondary antibodies light mitochondrial-lysosomal fraction gene encoding lamp-2a wild-type mice maintained article zhang wattiaux-de coninck full size image single wild-type 6-month single wild-type 22-month protease inhibitor–treated lysosomes hsp90 chaperone abundance total β-hexosaminidase activity age-related cma defect personal data late-activated alb-tet
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- Age-related changes in liver structure and function: Implications for disease?
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headline:Restoration of chaperone-mediated autophagy in aging liver improves cellular maintenance and hepatic function
description:Chaperone-mediated autophagy (CMA), a mechanism for the lysosomal degradation of proteins, declines in aging cells. Using transgenic mice in which such a decline does not occur in the liver, the authors found that preserving CMA leads to reduced accumulation of damaged proteins and improved organ function in aged mice (
pages 909â910
). Chaperone-mediated autophagy (CMA), a selective mechanism for degradation of cytosolic proteins in lysosomes, contributes to the removal of altered proteins as part of the cellular quality-control systems1,2. We have previously found that CMA activity declines in aged organisms and have proposed that this failure in cellular clearance could contribute to the accumulation of altered proteins, the abnormal cellular homeostasis and, eventually, the functional loss characteristic of aged organisms. To determine whether these negative features of aging can be prevented by maintaining efficient autophagic activity until late in life, in this work we have corrected the CMA defect in aged rodents. We have generated a double transgenic mouse model in which the amount of the lysosomal receptor for CMA, previously shown to decrease in abundance with age3, can be modulated. We have analyzed in this model the consequences of preventing the age-dependent decrease in receptor abundance in aged rodents at the cellular and organ levels. We show here that CMA activity is maintained until advanced ages if the decrease in the receptor abundance is prevented and that preservation of autophagic activity is associated with lower intracellular accumulation of damaged proteins, better ability to handle protein damage and improved organ function.
datePublished:2008-08-10T00:00:00Z
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headline:Restoration of chaperone-mediated autophagy in aging liver improves cellular maintenance and hepatic function
description:Chaperone-mediated autophagy (CMA), a mechanism for the lysosomal degradation of proteins, declines in aging cells. Using transgenic mice in which such a decline does not occur in the liver, the authors found that preserving CMA leads to reduced accumulation of damaged proteins and improved organ function in aged mice (
pages 909â910
). Chaperone-mediated autophagy (CMA), a selective mechanism for degradation of cytosolic proteins in lysosomes, contributes to the removal of altered proteins as part of the cellular quality-control systems1,2. We have previously found that CMA activity declines in aged organisms and have proposed that this failure in cellular clearance could contribute to the accumulation of altered proteins, the abnormal cellular homeostasis and, eventually, the functional loss characteristic of aged organisms. To determine whether these negative features of aging can be prevented by maintaining efficient autophagic activity until late in life, in this work we have corrected the CMA defect in aged rodents. We have generated a double transgenic mouse model in which the amount of the lysosomal receptor for CMA, previously shown to decrease in abundance with age3, can be modulated. We have analyzed in this model the consequences of preventing the age-dependent decrease in receptor abundance in aged rodents at the cellular and organ levels. We show here that CMA activity is maintained until advanced ages if the decrease in the receptor abundance is prevented and that preservation of autophagic activity is associated with lower intracellular accumulation of damaged proteins, better ability to handle protein damage and improved organ function.
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