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

© 2010 Blackwell Publishing Ltd.

Détails bibliographiques
Publié dans:Journal of fish diseases. - 1998. - 33(2010), 10 vom: 15. Okt., Seite 789-801
Auteur principal: Roberts, R J (Auteur)
Autres auteurs: Agius, C, Saliba, C, Bossier, P, Sung, Y Y
Format: Article en ligne
Langue:English
Publié: 2010
Accès à la collection:Journal of fish diseases
Sujets:Journal Article Review Heat-Shock Proteins
LEADER 01000caa a22002652c 4500
001 NLM200018329
003 DE-627
005 20250211201133.0
007 cr uuu---uuuuu
008 231223s2010 xx |||||o 00| ||eng c
024 7 |a 10.1111/j.1365-2761.2010.01183.x  |2 doi 
028 5 2 |a pubmed25n0667.xml 
035 |a (DE-627)NLM200018329 
035 |a (NLM)20678104 
040 |a DE-627  |b ger  |c DE-627  |e rakwb 
041 |a eng 
100 1 |a Roberts, R J  |e verfasserin  |4 aut 
245 1 0 |a Heat shock proteins (chaperones) in fish and shellfish and their potential role in relation to fish health  |b a review 
264 1 |c 2010 
336 |a Text  |b txt  |2 rdacontent 
337 |a ƒaComputermedien  |b c  |2 rdamedia 
338 |a ƒa Online-Ressource  |b cr  |2 rdacarrier 
500 |a Date Completed 24.01.2011 
500 |a Date Revised 30.09.2020 
500 |a published: Print 
500 |a Citation Status MEDLINE 
520 |a © 2010 Blackwell Publishing Ltd. 
520 |a 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 
650 4 |a Journal Article 
650 4 |a Review 
650 7 |a Heat-Shock Proteins  |2 NLM 
700 1 |a Agius, C  |e verfasserin  |4 aut 
700 1 |a Saliba, C  |e verfasserin  |4 aut 
700 1 |a Bossier, P  |e verfasserin  |4 aut 
700 1 |a Sung, Y Y  |e verfasserin  |4 aut 
773 0 8 |i Enthalten in  |t Journal of fish diseases  |d 1998  |g 33(2010), 10 vom: 15. Okt., Seite 789-801  |w (DE-627)NLM098166034  |x 1365-2761  |7 nnas 
773 1 8 |g volume:33  |g year:2010  |g number:10  |g day:15  |g month:10  |g pages:789-801 
856 4 0 |u http://dx.doi.org/10.1111/j.1365-2761.2010.01183.x  |3 Volltext 
912 |a GBV_USEFLAG_A 
912 |a SYSFLAG_A 
912 |a GBV_NLM 
912 |a GBV_ILN_350 
951 |a AR 
952 |d 33  |j 2010  |e 10  |b 15  |c 10  |h 789-801