dorsal/arxiv
View SchemaAging cellular networks: chaperones as major participants
| Authors | Csaba Soti, Peter Csermely |
|---|---|
| Categories | |
| ArXiv ID | q-bio/0605030 |
| URL | https://arxiv.org/abs/q-bio/0605030 |
| DOI | 10.1016/j.exger.2006.05.017 |
| Journal | Experimental Gerontology 42, 113-119 (2007) |
Abstract
We increasingly rely on the network approach to understand the complexity of cellular functions. Chaperones (heat shock proteins) are key "networkers", which have among their functions to sequester and repair damaged protein. In order to link the network approach and chaperones with the aging process, we first summarize the properties of aging networks suggesting a "weak link theory of aging". This theory suggests that age-related random damage primarily affects the overwhelming majority of the low affinity, transient interactions (weak links) in cellular networks leading to increased noise, destabilization and diversity. These processes may be further amplified by age-specific network remodelling and by the sequestration of weakly linked cellular proteins to protein aggregates of aging cells. Chaperones are weakly linked hubs [i.e., network elements with a large number of connections] and inter-modular bridge elements of protein-protein interaction, signalling and mitochondrial networks. As aging proceeds, the increased overload of damaged proteins is an especially important element contributing to cellular disintegration and destabilization. Additionally, chaperone overload may contribute to the increase of "noise" in aging cells, which leads to an increased stochastic resonance resulting in a deficient discrimination between signals and noise. Chaperone- and other multi-target therapies, which restore the missing weak links in aging cellular networks, may emerge as important anti-aging interventions.
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"abstract": "We increasingly rely on the network approach to understand the complexity of\ncellular functions. Chaperones (heat shock proteins) are key \"networkers\",\nwhich have among their functions to sequester and repair damaged protein. In\norder to link the network approach and chaperones with the aging process, we\nfirst summarize the properties of aging networks suggesting a \"weak link theory\nof aging\". This theory suggests that age-related random damage primarily\naffects the overwhelming majority of the low affinity, transient interactions\n(weak links) in cellular networks leading to increased noise, destabilization\nand diversity. These processes may be further amplified by age-specific network\nremodelling and by the sequestration of weakly linked cellular proteins to\nprotein aggregates of aging cells. Chaperones are weakly linked hubs [i.e.,\nnetwork elements with a large number of connections] and inter-modular bridge\nelements of protein-protein interaction, signalling and mitochondrial networks.\nAs aging proceeds, the increased overload of damaged proteins is an especially\nimportant element contributing to cellular disintegration and destabilization.\nAdditionally, chaperone overload may contribute to the increase of \"noise\" in\naging cells, which leads to an increased stochastic resonance resulting in a\ndeficient discrimination between signals and noise. Chaperone- and other\nmulti-target therapies, which restore the missing weak links in aging cellular\nnetworks, may emerge as important anti-aging interventions.",
"arxiv_id": "q-bio/0605030",
"authors": [
"Csaba Soti",
"Peter Csermely"
],
"categories": [
"q-bio.MN"
],
"doi": "10.1016/j.exger.2006.05.017",
"journal_ref": "Experimental Gerontology 42, 113-119 (2007)",
"title": "Aging cellular networks: chaperones as major participants",
"url": "https://arxiv.org/abs/q-bio/0605030"
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