Proteolysis dysfunction in the process of aging and age-related diseases
In this review, we discuss in detail the most relevant proteolytic systems that together with chaperones contribute to creating the proteostasis network that is kept in dynamic balance to maintain overall functionality of cellular proteomes. Data accumulated over decades demonstrate that the effecti...
Main Authors: | , , |
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Format: | Article |
Language: | English |
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Frontiers Media S.A.
2022-07-01
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Series: | Frontiers in Aging |
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Online Access: | https://www.frontiersin.org/articles/10.3389/fragi.2022.927630/full |
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author | Natalia Frankowska Katarzyna Lisowska Jacek M. Witkowski |
author_facet | Natalia Frankowska Katarzyna Lisowska Jacek M. Witkowski |
author_sort | Natalia Frankowska |
collection | DOAJ |
description | In this review, we discuss in detail the most relevant proteolytic systems that together with chaperones contribute to creating the proteostasis network that is kept in dynamic balance to maintain overall functionality of cellular proteomes. Data accumulated over decades demonstrate that the effectiveness of elements of the proteostasis network declines with age. In this scenario, failure to degrade misfolded or faulty proteins increases the risk of protein aggregation, chronic inflammation, and the development of age-related diseases. This is especially important in the context of aging-related modification of functions of the immune system. |
first_indexed | 2024-12-10T08:40:22Z |
format | Article |
id | doaj.art-fc489b935a214d649422049cd768f40d |
institution | Directory Open Access Journal |
issn | 2673-6217 |
language | English |
last_indexed | 2024-12-10T08:40:22Z |
publishDate | 2022-07-01 |
publisher | Frontiers Media S.A. |
record_format | Article |
series | Frontiers in Aging |
spelling | doaj.art-fc489b935a214d649422049cd768f40d2022-12-22T01:55:52ZengFrontiers Media S.A.Frontiers in Aging2673-62172022-07-01310.3389/fragi.2022.927630927630Proteolysis dysfunction in the process of aging and age-related diseasesNatalia FrankowskaKatarzyna LisowskaJacek M. WitkowskiIn this review, we discuss in detail the most relevant proteolytic systems that together with chaperones contribute to creating the proteostasis network that is kept in dynamic balance to maintain overall functionality of cellular proteomes. Data accumulated over decades demonstrate that the effectiveness of elements of the proteostasis network declines with age. In this scenario, failure to degrade misfolded or faulty proteins increases the risk of protein aggregation, chronic inflammation, and the development of age-related diseases. This is especially important in the context of aging-related modification of functions of the immune system.https://www.frontiersin.org/articles/10.3389/fragi.2022.927630/fullagingproteostasischaperonesubiquitin-proteasome systemautophagylysosome |
spellingShingle | Natalia Frankowska Katarzyna Lisowska Jacek M. Witkowski Proteolysis dysfunction in the process of aging and age-related diseases Frontiers in Aging aging proteostasis chaperones ubiquitin-proteasome system autophagy lysosome |
title | Proteolysis dysfunction in the process of aging and age-related diseases |
title_full | Proteolysis dysfunction in the process of aging and age-related diseases |
title_fullStr | Proteolysis dysfunction in the process of aging and age-related diseases |
title_full_unstemmed | Proteolysis dysfunction in the process of aging and age-related diseases |
title_short | Proteolysis dysfunction in the process of aging and age-related diseases |
title_sort | proteolysis dysfunction in the process of aging and age related diseases |
topic | aging proteostasis chaperones ubiquitin-proteasome system autophagy lysosome |
url | https://www.frontiersin.org/articles/10.3389/fragi.2022.927630/full |
work_keys_str_mv | AT nataliafrankowska proteolysisdysfunctionintheprocessofagingandagerelateddiseases AT katarzynalisowska proteolysisdysfunctionintheprocessofagingandagerelateddiseases AT jacekmwitkowski proteolysisdysfunctionintheprocessofagingandagerelateddiseases |