Heat Shock Proteins in Aquatic Stress Response

Summary

Heat shock proteins (HSPs) constitute a highly conserved class of molecular chaperones that safeguard cellular proteostasis under a wide range of stressors, including thermal fluctuations, chemical pollutants and pathogenic challenges. In aquatic organisms, HSP families—most notably HSP70, HSP40, HSP60, HSP27 and HSP90—mediate protein folding, prevent aggregation and facilitate the refolding or degradation of denatured substrates. Their inducible expression underpins both acute stress tolerance and long-term acclimation strategies, making HSPs prime biomarkers for monitoring ecosystem health. Beyond environmental sensing, HSPs interact with immune pathways, modulating innate and adaptive responses to pathogens. In fisheries and aquaculture, characterising HSP dynamics informs selective breeding for stress resilience, guides husbandry practices and assists in the assessment of sublethal pollutant exposures. Interdisciplinary research has thus unified molecular, ecological and applied perspectives to reveal how HSP networks shape the survival, distribution and performance of aquatic species in a rapidly changing world.

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Heat Shock Proteins in Aquatic Stress Response publication trend

The graph below shows the total number of articles in heat shock proteins in aquatic stress response across all publications each year (not limited to Nature Index journals).

Technical terms

Heat shock protein (HSP): A class of conserved proteins that assist in proper folding, prevent aggregation and stabilise denatured proteins during cellular stress.

Molecular chaperone: A protein that transiently binds unfolded or partially folded polypeptides to guide correct folding or target misfolded species for degradation.

Upregulation: An increase in the expression level of a gene or protein in response to a specific stimulus.

Biomarker: A measurable molecular indicator used to assess physiological or pathological processes, or responses to environmental exposures.

Polyinosinic-polycytidylic acid (Poly(I:C)): A synthetic analogue of double-stranded RNA that mimics viral infection and triggers innate immune responses.

References

  1. Heat shock protein 70 reflected the state of inhabited fish response to water quality within lake ecosystem. International Journal of Environmental Science and Technology (2023).
  2. Schizothorax prenanti Heat Shock Protein 27 Gene: Cloning, Expression, and Comparison with Other Heat Shock Protein Genes after Poly (I:C) Induction. Animals (2022).
  3. The hsp40 Gene Family in Japanese Flounder: Identification, Phylogenetic Relationships, Molecular Evolution Analysis, and Expression Patterns. Frontiers in Marine Science (2021).

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