Modulating cellular aging in vitro: hormetic effects of repeated mild heat stress on protein oxidation and glycation.
Intracellular and extracellular proteins are subject to a variety of spontaneous non-enzymatic modifications which affect their structure, function and stability. Protein oxidation and glycation are tightly linked and are implicated in the development of many pathological consequences of aging. Although multiple endogenous pathways in the cell can prevent the formation of oxidized and glycated proteins, and repair and degrade abnormal proteins, such abnormal proteins do accumulate during aging. The heat shock response involving the family of stress-proteins or the so-called heat shock proteins (HSP), represents the quickest and highly conserved response to proteotoxic insults. Since repeated mild heat stress is able to prevent the onset of various age-related changes during cellular aging in vitro, we suggest that treatments which increase HSP expression should reduce the extent of accumulation of abnormal proteins during aging. Such modulation of aging is an example of hormesis, which is characterized by the beneficial effects resulting from the cellular responses to mild repeated stress.
Verbeke
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P
Danish Centre for Molecular Gerontology, Laboratory of Cellular Ageing, Department of Molecular and Structural Biology, University of Aarhus, Gustav Wieds Vej 10-C, DK-8000, Aarhus, Denmark.
Clark
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BF
Rattan
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SI
D000818:Animals; D016922:Cellular Senescence; D017127:Glycation End Products, Advanced / Q000378:metabolism; D006031:Glycosylation; D006360:Heat-Shock Proteins / Q000096:biosynthesis; D006358:Hot Temperature; D006801:Humans; D010084:Oxidation-Reduction; D011506:Proteins / Q000378:metabolism*
D017127:Glycation End Products, Advanced; D006360:Heat-Shock Proteins; D011506:Proteins