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Open AccessJournal ArticleDOI

Stress proteins in aging and life span.

TLDR
Among many signalling mechanisms involved in altering longevity and aging, the insulin/IGF-1 pathway and the Sir2 deacetylase are highly significant and an enquires into the role of some of these pathways in longevity/aging along with HSP.
Abstract
Heat shock proteins (HSP) are molecular chaperones and have been implicated in longevity and aging in many species. Their major functions include chaperoning misfolded or newly synthesised polypeptides, protecting cells from proteotoxic stress, and processing of immunogenic agents. These proteins are expressed constitutively and can be induced by stresses such as heat, oxidative stress and many more. The induction of HSP in aging could potentially maintain protein homeostasis and longevity by refolding the damaged proteins which accumulate during aging and are toxic to cells. HSP are shown to increase life span in model organisms such as Caenorhabditis elegans and decrease aging-related proteotoxicity. Thus, decrease in HSP in aging is associated with disruption of cellular homeostasis which causes diseases such as cancer, cell senescence and neurodegeneration. HSP levels are decreased with aging in most organs including neurons. Aging also causes attenuation or alteration of many signalling pathw...

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The Biology of Aging and Cancer: A Brief Overview of Shared and Divergent Molecular Hallmarks

TL;DR: It is now clear that aging and cancer development either share or diverge in several disease mechanisms, and aging can be considered an aging disease, though the shared mechanisms underpinning the two processes remain unclear.
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Roles of Extracellular HSPs as Biomarkers in Immune Surveillance and Immune Evasion

TL;DR: Release of ex-HSP and HSP-rich oncosomes are essential in RASP, by which molecular co-transfer of HSPs with oncogenic factors to recipient cells can promote cancer progression and resistance against stresses such as hypoxia, radiation, drugs, and immune systems.
Journal ArticleDOI

Transcription factors Hsf1 and Nrf2 engage in crosstalk for cytoprotection

TL;DR: Although each is regulated by distinct mechanisms, it is emerging that these transcription factors engage in crosstalk by sharing overlapping transcriptional targets, such as heat shock protein (HSP)70, p62, and activating transcription factor (ATF)3, and in certain cases, compensating for each other.
References
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Journal ArticleDOI

Hsp70 chaperones: cellular functions and molecular mechanism.

TL;DR: This work has shown that for specific tasks the Hsp70 cycle is coupled to the action of other chaperones, such as Hsp90 and Hsp100, and this ATPase cycle is controlled by co-chaperones of the family of J-domain proteins, which target H Sp70s to their substrates, and by nucleotide exchange factors, which determine the lifetime of the HSp70-substrate complex.
Journal ArticleDOI

Extending Healthy Life Span-From Yeast to Humans

TL;DR: Dietary restriction and reduced activity of nutrient-sensing pathways may slow aging by similar mechanisms, which have been conserved during evolution, and their potential application to prevention of age-related disease and promotion of healthy aging in humans, and the challenge of possible negative side effects.
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Adapting proteostasis for disease intervention.

TL;DR: The proteostasis network is described, a set of interacting activities that maintain the health of proteome and the organism that has the potential to ameliorate some of the most challenging diseases of this era.
Journal ArticleDOI

Heat shock proteins in cancer: diagnostic, prognostic, predictive, and treatment implications

TL;DR: Although Hsp levels are not informative at the diagnostic level, they are useful biomarkers for carcinogenesis in some tissues and signal the degree of differentiation and the aggressiveness of some cancers.
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