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Heat shock proteins (chaperones) in fish and shellfish and their potential role in relation to fish health: a review

(2010) JOURNAL OF FISH DISEASES. 33(10). p.789-801
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Abstract
Heat shock proteins (HSPs), also known as stress proteins and extrinsic chaperones, are a suite of highly conserved proteins of varying molecular weight (c. 16-100 kDa) produced in all cellular organisms when they are exposed to stress. They develop following up-regulation of specific genes, whose transcription is mediated by the interaction of heat shock factors with heat shock elements in gene promoter regions. HSPs function as helper molecules or chaperones for all protein and lipid metabolic activities of the cell, and it is now recognized that the up-regulation in response to stress is universal to all cells and not restricted to heat stress. Thus, other stressors such as anoxia, ischaemia, toxins, protein degradation, hypoxia, acidosis and microbial damage will also lead to their up-regulation. They play a fundamental role in the regulation of normal protein synthesis within the cell. HSP families, such as HSP90 and HSP70, are critical to the folding and assembly of other cellular proteins and are also involved in regulation of kinetic partitioning between folding, translocation and aggregation within the cell. HSPs also have a wider role in relation to the function of the immune system, apoptosis and various facets of the inflammatory process. In aquatic animals, they have been shown to play an important role in health, in relation to the host response to environmental pollutants, to food toxins and in particular in the development of inflammation and the specific and non-specific immune responses to bacterial and viral infections in both finfish and shrimp. With the recent development of non-traumatic methods for enhancing HSP levels in fish and shrimp populations via heat, via provision of exogenous HSPs or by oral or water administration of HSP stimulants, they have also, in addition to the health effects, been demonstrated to be valuable in contributing to reducing trauma and physical stress in relation to husbandry events such as transportation and vaccination.
Keywords
ARTEMIA-FRANCISCANA LARVAE, SALMO-SALAR L., ATLANTIC SALMON, STRESS-PROTEINS, GENE-EXPRESSION, RAINBOW-TROUT, MOLECULAR CHAPERONES, IMMUNE-RESPONSE, SOYBEAN-MEAL, TRANSCRIPTION FACTORS, chaperone, fish, heat shock cognate, heat shock protein, HSP, shellfish

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Citation

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Chicago
Roberts, RJ, C Agius, C Saliba, Peter Bossier, and YY Sung. 2010. “Heat Shock Proteins (chaperones) in Fish and Shellfish and Their Potential Role in Relation to Fish Health: a Review.” Journal of Fish Diseases 33 (10): 789–801.
APA
Roberts, R., Agius, C., Saliba, C., Bossier, P., & Sung, Y. (2010). Heat shock proteins (chaperones) in fish and shellfish and their potential role in relation to fish health: a review. JOURNAL OF FISH DISEASES, 33(10), 789–801.
Vancouver
1.
Roberts R, Agius C, Saliba C, Bossier P, Sung Y. Heat shock proteins (chaperones) in fish and shellfish and their potential role in relation to fish health: a review. JOURNAL OF FISH DISEASES. 2010;33(10):789–801.
MLA
Roberts, RJ, C Agius, C Saliba, et al. “Heat Shock Proteins (chaperones) in Fish and Shellfish and Their Potential Role in Relation to Fish Health: a Review.” JOURNAL OF FISH DISEASES 33.10 (2010): 789–801. Print.
@article{1896631,
  abstract     = {Heat shock proteins (HSPs), also known as stress proteins and extrinsic chaperones, are a suite of highly conserved proteins of varying molecular weight (c. 16-100 kDa) produced in all cellular organisms when they are exposed to stress. They develop following up-regulation of specific genes, whose transcription is mediated by the interaction of heat shock factors with heat shock elements in gene promoter regions. HSPs function as helper molecules or chaperones for all protein and lipid metabolic activities of the cell, and it is now recognized that the up-regulation in response to stress is universal to all cells and not restricted to heat stress. Thus, other stressors such as anoxia, ischaemia, toxins, protein degradation, hypoxia, acidosis and microbial damage will also lead to their up-regulation. They play a fundamental role in the regulation of normal protein synthesis within the cell. HSP families, such as HSP90 and HSP70, are critical to the folding and assembly of other cellular proteins and are also involved in regulation of kinetic partitioning between folding, translocation and aggregation within the cell. HSPs also have a wider role in relation to the function of the immune system, apoptosis and various facets of the inflammatory process. In aquatic animals, they have been shown to play an important role in health, in relation to the host response to environmental pollutants, to food toxins and in particular in the development of inflammation and the specific and non-specific immune responses to bacterial and viral infections in both finfish and shrimp. With the recent development of non-traumatic methods for enhancing HSP levels in fish and shrimp populations via heat, via provision of exogenous HSPs or by oral or water administration of HSP stimulants, they have also, in addition to the health effects, been demonstrated to be valuable in contributing to reducing trauma and physical stress in relation to husbandry events such as transportation and vaccination.},
  author       = {Roberts, RJ and Agius, C and Saliba, C and Bossier, Peter and Sung, YY},
  issn         = {0140-7775},
  journal      = {JOURNAL OF FISH DISEASES},
  keyword      = {ARTEMIA-FRANCISCANA LARVAE,SALMO-SALAR L.,ATLANTIC SALMON,STRESS-PROTEINS,GENE-EXPRESSION,RAINBOW-TROUT,MOLECULAR CHAPERONES,IMMUNE-RESPONSE,SOYBEAN-MEAL,TRANSCRIPTION FACTORS,chaperone,fish,heat shock cognate,heat shock protein,HSP,shellfish},
  language     = {eng},
  number       = {10},
  pages        = {789--801},
  title        = {Heat shock proteins (chaperones) in fish and shellfish and their potential role in relation to fish health: a review},
  url          = {http://dx.doi.org/10.1111/j.1365-2761.2010.01183.x},
  volume       = {33},
  year         = {2010},
}

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