| The small heat shock protein p26 aids development of encysting Artemia embryos, prevents spontaneous diapause termination and protects against stress. | |
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MedLine Citation:
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PMID: 22952748 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Artemia franciscana embryos enter diapause as encysted gastrulae, a physiological state of metabolic dormancy and enhanced stress resistance. The objective of this study was to use RNAi to investigate the function of p26, an abundant, diapause-specific small heat shock protein, in the development and behavior of encysted Artemia embryos (cysts). RNAi methodology was developed where injection of Artemia females with dsRNA specifically eliminated p26 from cysts. p26 mRNA and protein knock down were, respectively, confirmed by RT-PCR and immuno-probing of western blots. ArHsp21 and ArHsp22, diapause-related small heat shock proteins in Artemia cysts sharing a conserved α-crystallin domain with p26, were unaffected by injection of females with dsRNA for p26, demonstrating the specificity of protein knock down. Elimination of p26 delayed cyst release from females demonstrating that this molecular chaperone influences the development of diapause-destined embryos. Although development was slowed the metabolic activities of cysts either containing or lacking p26 were similar. p26 inhibited diapause termination after prolonged incubation of cysts in sea water perhaps by a direct effect on termination or indirectly because p26 is necessary for the preservation of diapause maintenance. Cyst diapause was however, terminated by desiccation and freezing, a procedure leading to high mortality within cyst populations lacking p26 and indicating the protein is required for stress tolerance. Cysts lacking p26 were also less resistant to heat shock. This is the first in vivo study to show that knock down of a small heat shock protein slows the development of diapause-destined embryos, suggesting a role for p26 in the developmental process. The same small heat shock protein prevents spontaneous termination of diapause and provides stress protection to encysted embryos. |
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Authors:
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Allison M King; Thomas H MacRae |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2012-08-27 |
Journal Detail:
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Title: PloS one Volume: 7 ISSN: 1932-6203 ISO Abbreviation: PLoS ONE Publication Date: 2012 |
Date Detail:
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Created Date: 2012-09-06 Completed Date: 2013-02-19 Revised Date: 2013-03-08 |
Medline Journal Info:
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Nlm Unique ID: 101285081 Medline TA: PLoS One Country: United States |
Other Details:
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Languages: eng Pagination: e43723 Citation Subset: IM |
Affiliation:
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Department of Biology, Dalhousie University, Halifax, Nova Scotia, Canada. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Animals Artemia / embryology*, metabolism, physiology* Embryo, Nonmammalian / embryology*, metabolism*, physiology Female Gene Knockdown Techniques Heat-Shock Proteins / deficiency, genetics, metabolism* Injections RNA, Double-Stranded / genetics RNA, Messenger / genetics, metabolism Stress, Physiological* |
| Chemical | |
Reg. No./Substance:
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0/Heat-Shock Proteins; 0/RNA, Double-Stranded; 0/RNA, Messenger; 0/p26 chaperone protein, Artemia franciscana |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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