Heat shock response
Heat-shock proteins
Also searched as Heat-shock proteins.
You want them abundant: robust chaperone capacity keeps the proteome folded and blocks the aggregation that drives decline.
In depth
The chaperone proteins that refold the misfolded and triage the damaged — the cell's protein-repair crew.
What drives it
Heat shock master switch increases it.
Åkerfelt 2010, Nat Rev Mol Cell Biol 11:545 — HSF1 is the master transcription factor of the heat-shock response, inducing the molecular chaperones (heat-shock proteins). doi 10.1038/nrm2938
Heat exposure increases it.
Verbatim: 'The expression levels of a series of heat-shock proteins (HSPs), including HSP90, HSP70, HSP60, and HSP40, were significantly up-regulated from the HA training.' (10.3389/fmicb.2024.1385333). Tier: animal. rat · environmental heat acclimation training · 21 consecutive days of HA training (temperature not stated in abstract) · n not stated in abstract · controlled animal model of hea. doi 10.3389/fmicb.2024.1385333
Social engagement increases it.
Whole-body environmental heat stress in healthy humans increased extracellular heat-shock protein HSP72 by 48.7% (P < .001), while the matched unheated control trials produced no change, showing that an environmental stressor induces heat-shock protein expression. doi 10.4085/1062-6050-47.2.184 · PMID 22488284
What it drives
It increases Protein quality control.
Hartl 2011, Nature 475:324 — molecular chaperones (heat-shock proteins) prevent aggregation and promote folding, maintaining protein homeostasis (proteostasis). doi 10.1038/nature10317
It reduces Cell turnover.
Beere 2000, Nat Cell Biol 2:469 — HSP70 inhibits apoptosis by binding Apaf-1 and blocking assembly of the apoptosome (preventing procaspase-9 recruitment). PMID 10934466
It increases Adaptive stress response.
Heat-shock protein induction is the molecular signature of a hormetic heat stimulus. Carried by the hormesis, inflammaging and thermogenesis reviews. doi 10.1002/med.21743
Blends that modulate it
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See it on the map
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