Relationship between heat shock protein 70 expression and life span in Daphnia

Schumpert, Charles; Handy, Indhira; Dudycha, Jeffry L.; Patel, Rekha C.

doi:10.1016/j.mad.2014.04.001

Cited by 29 publications

(29 citation statements)

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“…Also HSPs react more strongly to heat stress in female Daphnia [55]. In comparisons among Daphnia species elevated HSP expression is associated with longer lifespan [56]. We observed 80% of the differentially expressed heat shock proteins (11/14 genes) having higher expression in female compared to male Daphnia, including heat shock transcription factor 1 (HSF1; Daplx7pEVm005655, log 2 FC = 0.52), despite HSF1 having (9.43%) higher methylation level in male Daphnia.…”

Section: Discussionmentioning

confidence: 75%

A comprehensive epigenomic analysis of phenotypically distinguishable, genetically identical female and male Daphnia pulex

et al. 2020

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Background: Daphnia species reproduce by cyclic parthenogenesis involving both sexual and asexual reproduction. The sex of the offspring is environmentally determined and mediated via endocrine signalling by the mother. Interestingly, male and female Daphnia can be genetically identical, yet display large differences in behaviour, morphology, lifespan and metabolic activity. Our goal was to integrate multiple omics datasets, including gene expression, splicing, histone modification and DNA methylation data generated from genetically identical female and male Daphnia pulex under controlled laboratory settings with the aim of achieving a better understanding of the underlying epigenetic factors that may contribute to the phenotypic differences observed between the two genders. Results: In this study we demonstrate that gene expression level is positively correlated with increased DNA methylation, and histone H3 trimethylation at lysine 4 (H3K4me3) at predicted promoter regions. Conversely, elevated histone H3 trimethylation at lysine 27 (H3K27me3), distributed across the entire transcript length, is negatively correlated with gene expression level. Interestingly, male Daphnia are dominated with epigenetic modifications that globally promote elevated gene expression, while female Daphnia are dominated with epigenetic modifications that reduce gene expression globally. For examples, CpG methylation (positively correlated with gene expression level) is significantly higher in almost all differentially methylated sites in male compared to female Daphnia. Furthermore, H3K4me3 modifications are higher in male compared to female Daphnia in more than 3/4 of the differentially regulated promoters. On the other hand, H3K27me3 is higher in female compared to male Daphnia in more than 5/6 of differentially modified sites. However, both sexes demonstrate roughly equal number of genes that are up-regulated in one gender compared to the other sex. Since, gene expression analyses typically assume that most genes are expressed at equal level among samples and different conditions, and thus cannot detect global changes affecting most genes. Conclusions: The epigenetic differences between male and female in Daphnia pulex are vast and dominated by changes that promote elevated gene expression in male Daphnia. Furthermore, the differences observed in both gene expression changes and epigenetic modifications between the genders relate to pathways that are physiologically relevant to the observed phenotypic differences.

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Section: Discussionmentioning

confidence: 75%

A comprehensive epigenomic analysis of phenotypically distinguishable, genetically identical female and male Daphnia pulex

et al. 2020

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“…HSPs are required for longevity (2,3), and a number of studies suggest that longer-lived species have higher constitutive expression of HSPs (4)(5)(6)(7). Consistent with this finding, overexpression of HSP genes increased longevity in Drosophila, Caenorhabditis elegans, and vertebrates (1,8,9).…”

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confidence: 71%

Exogenous Hsp70 delays senescence and improves cognitive function in aging mice

Бобкова

Евгеньев

Гарбуз

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

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Molecular chaperone Heat Shock Protein 70 (Hsp70) plays an important protective role in various neurodegenerative disorders often associated with aging, but its activity and availability in neuronal tissue decrease with age. Here we explored the effects of intranasal administration of exogenous recombinant human Hsp70 (eHsp70) on lifespan and neurological parameters in middle-aged and old mice. Long-term administration of eHsp70 significantly enhanced the lifespan of animals of different age groups. Behavioral assessment after 5 and 9 mo of chronic eHsp70 administration demonstrated improved learning and memory in old mice. Likewise, the investigation of locomotor and exploratory activities after eHsp70 treatment demonstrated a significant therapeutic effect of this chaperone. Measurements of synaptophysin show that eHsp70 treatment in old mice resulted in larger synaptophysin-immunopositive areas and higher neuron density compared with control animals. Furthermore, eHsp70 treatment decreased accumulation of lipofuscin, an aging-related marker, in the brain and enhanced proteasome activity. The potential of eHsp70 intranasal treatment to protect synaptic machinery in old animals offers a unique pharmacological approach for various neurodegenerative disorders associated with human aging.

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“…Understanding of Hsp70's ability to promote the degradation of oxidatively damaged proteins may be especially important in the field of aging research, since it is known that oxidized proteins and protein aggregates accumulate during aging and various age-related diseases due to the impairment of the proteasomal system [59,60]. Furthermore, there is increasing evidence that the stress-related inducibility of Hsp70 expression declines in aged cell models and organisms [61–64] and that the chaperones are overloaded in aged cells due to increasing formation and accumulation of oxidized proteins [65,66]. Thus, modulating Hsp70 levels may be a possible pharmaceutical goal to maintain protein homeostasis and prevent the formation of toxic protein aggregates that can disrupt cellular function.…”

Section: Discussionmentioning

confidence: 99%

The molecular chaperone Hsp70 promotes the proteolytic removal of oxidatively damaged proteins by the proteasome

Reeg

Jung

Castro

et al. 2016

Free Radical Biology and Medicine

101

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One hallmark of aging is the accumulation of protein aggregates, promoted by the unfolding of oxidized proteins. Unraveling the mechanism by which oxidized proteins are degraded may provide a basis to delay the early onset of features, such as protein aggregate formation, that contribute to the aging phenotype. In order to prevent aggregation of oxidized proteins, cells recur to the 20S proteasome, an efficient turnover proteolysis complex. It has previously been shown that upon oxidative stress the 26S proteasome, another form, dissociates into the 20S form. A critical player implicated in its dissociation is the Heat Shock Protein 70 (Hsp70), which promotes an increase in free 20S proteasome and, therefore, an increased capability to degrade oxidized proteins. The aim of this study was to test whether or not Hsp70 is involved in cooperating with the 20S proteasome for a selective degradation of oxidatively damaged proteins. Our results demonstrate that Hsp70 expression is induced in HT22 cells as a result of mild oxidative stress conditions. Furthermore, Hsp70 prevents the accumulation of oxidized proteins and directly promotes their degradation by the 20S proteasome. In contrast the expression of the Heat shock cognate protein 70 (Hsc70) was not changed in recovery after oxidative stress and Hsc70 has no influence on the removal of oxidatively damaged proteins. We were able to demonstrate in HT22 cells, in brain homogenates from 129/SV mice and in vitro, that there is an increased interaction of Hsp70 with oxidized proteins, but also with the 20S proteasome, indicating a role of Hsp70 in mediating the interaction of oxidized proteins with the 20S proteasome. Thus, our data clearly implicate an involvement of Hsp70 oxidatively damaged protein degradation by the 20S proteasome.

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Relationship between heat shock protein 70 expression and life span in Daphnia

Cited by 29 publications

References 50 publications

A comprehensive epigenomic analysis of phenotypically distinguishable, genetically identical female and male Daphnia pulex

A comprehensive epigenomic analysis of phenotypically distinguishable, genetically identical female and male Daphnia pulex

Exogenous Hsp70 delays senescence and improves cognitive function in aging mice

The molecular chaperone Hsp70 promotes the proteolytic removal of oxidatively damaged proteins by the proteasome

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