Gene expression analysis during heat shock in Drosophila melanogaster KC167 cells and 3rd instar dp cn bw larvae
Ontology highlight
ABSTRACT:
INSTRUMENT(S): NimbleGen Drosophila melanogaster 385K Array
ORGANISM(S): Drosophila melanogaster
SUBMITTER: 
Zak Razak
PROVIDER: GSE19745 | GEO | 2011-01-05
SECONDARY ACCESSION(S): PRJNA123997
REPOSITORIES: GEO
Similar Datasets
Project description:Gene expression analysis of Drosophila melanogaster 3rd instar hsf4 cn bw larvae, under heat shock and non-heat shock conditions (room temperature) using Nimblegen arrrays (GPL8443) Overall design: total RNA recovered from heat shocked or non-heat shocked (room temperature) samples in hsf4 larvae, 3 biological replicates for each treatment
2011-01-05 | GSE22332 | GEO
Project description:Expression analysis of Heat Shock in Drosophila melanogaster KC167 Cells and 3rd instar dpcnbw larvae, and room temperature expression levels using Nimblegen arrrays (GPL8443) A 12 chip study using total RNA recovered from Heat shocked or non-heat shocked (room temperature) samples in either cells or larvae, 3 technical replicates for each treatment
2011-01-05 | E-GEOD-19745 | ArrayExpress
Project description:Autophagy is a physiological mechanism that can be activated under stress conditions. However, the role of autophagy during oocyte maturation has been poorly investigated. Therefore, this study characterized the role of autophagy on developmental competence and gene expression of bovine oocytes exposed to heat shock (HS). Cumulus-oocyte-complexes (COCs) were matured at Control (38.5 °C) and HS (41 °C) temperatures in the presence of 0 and 10 mM 3-methyladenine (3MA; autophagy inhibitor). Western blotting analysis revealed that HS increased autophagy marker LC3-II/LC3-I ratio in oocytes. However, there was no effect of temperature for oocytes matured with 3MA. On cumulus cells, 3MA reduced LC3-II/LC3-I ratio regardless of temperature. Inhibition of autophagy during IVM of heat-shocked oocytes (3MA-41 °C) reduced cleavage and blastocyst rates compared to standard in vitro matured heat-shocked oocytes (IVM-41 °C). Therefore, the magnitude of HS detrimental effects was greater in the presence of autophagy inhibitor. Oocyte maturation under 3MA-41 °C reduced mRNA abundance for genes related to energy metabolism (MTIF3), heat shock response (HSF1), and oocyte maturation (HAS2 and GREM1). In conclusion, autophagy is a stress response induced on heat shocked oocytes. Inhibition of autophagy modulated key functional processes rendering the oocyte more susceptible to the deleterious effects of heat shock.
2020-01-01 | S-EPMC7426922 | BioStudies
Project description:ecdysone treated KC167 cells during Heat Shock and at Room Temperature Overall design: 2-colour microarray desgin using 9 spotted oligonucleotide microarrays printed at the Canadian Drosophila Microarray Centre. Total RNA from Ecdysone treated KC167 cells were compared to Total RNA from an EtOH (the solvent for ecdysone) control sample pool.
2011-08-17 | GSE23824 | GEO
Project description:Securing economically and ecologically significant molluscs, as our oceans warm due to climate change, is a global priority. South eastern Australia receives warm water in a strengthening East Australia Current and so resident species are vulnerable to elevated temperature and marine heat waves. This study tested whether prior exposure to elevated temperature can enhance resilience of oysters to ocean warming. Two Australian species, the flat oyster, Ostrea angasi, and the Sydney rock oyster, Saccostrea glomerata, were obtained as adults and "heat shocked" by exposure to a dose of warm water in the laboratory. Oysters were then transferred to elevated seawater temperature conditions where the thermal outfall from power generation was used as a proxy to investigate the impacts of ocean warming. Shell growth, condition index, lipid content and survival of flat oysters and condition of Sydney rock oysters were all significantly reduced by elevated seawater temperature in the field. Flat oysters grew faster than Sydney rock oysters at ambient temperature, but their growth and survival was more sensitive to elevated temperature. "Stress inoculation" by heat shock did little to ameliorate the negative effects of increased temperature, although the survival of heat-shocked flat oysters was greater than non-heat shocked oysters. Further investigations are required to determine if early exposure to heat stress can enhance resilience of oysters to ocean warming.
2020-01-01 | S-EPMC7147797 | BioStudies
Project description:In order to survive in extreme environments, organisms need to develop special adaptations both on physiological and molecular levels. The sleeping chironomid Polypedilum vanderplanki, inhabiting temporary water pools in semi-arid regions of Africa, is the only insect to have evolutionarily acquired the ability to withstand prolonged complete desiccation at larval stage, entering a state called anhydrobiosis. Even after years in a dry state, larvae are able to revive within a short period of time, completely restoring metabolism. Because of the possible involvement of stress proteins in the preservation of biomolecules during the anhydrobiosis of the sleeping chironomid, we have analyzed the expression of genes encoding six heat shock proteins (Pv-hsp90, Pv-hsp70, Pv-hsc70, Pv-hsp60, Pv-hsp20, and Pv-p23) and one heat shock factor (Pv-hsf1) in dehydrating, rehydrating, and heat-shocked larvae. All examined genes were significantly up-regulated in the larvae upon dehydration and several patterns of expression were detected. Gene transcript of Pv-hsf1 was up-regulated within 8 h of desiccation, followed by large shock proteins expression reaching peak at 24-48 h of desiccation. Heat-shock-responsive Pv-hsp70 and Pv-hsp60 showed a two-peak expression: in dehydrating and rehydrating larvae. Both small alpha-crystallin heat shock proteins (sHSP) transcripts were accumulated in the desiccated larvae, but showed different expression profiles. Both sHSP-coding genes were found to be heat-inducible, and Pv-hsp20 was up-regulated in the larvae at the early stage of desiccation. In contrast, expression of the second transcript, corresponding to Pv-p23, was limited to the late stages of desiccation, suggesting possible involvement of this protein in the glass-state formation in anhydrobiotic larvae. We discuss possible roles of proteins encoded by these stress genes during the different stages of anhydrobiosis in P. vanderplanki.
2011-01-01 | S-EPMC3024092 | BioStudies
Project description:Heat shock, sudden change in temperature, triggers various responses in cells for protecting the cells from such a severe circumstance. Here we investigated gene silencing mediated by endogenous microRNAs (miRNAs) in mammalian cells exposed to a mild hyperthermia, by means of miRNA activity assay using a luciferase reporter gene as well as miRNA expression analysis using a DNA microarray. Our findings indicated that the gene silencing activities involving miRNAs were enhanced without increasing in their expression levels under heat-stress conditions. Additionally, the gene silencing activity appeared to be independent of the cytoprotective action involving heat shock proteins that are immediately activated in heat-shocked cells and that function as molecular chaperons for restoring heat-denatured proteins to normal proteins. Our current findings suggested the possibility that gene silencing involving endogenous miRNAs might play a subsidiary role in heat-shocked cells for an aggressive inhibition of the expression of heat-denatured proteins.
2014-01-01 | S-EPMC4113354 | BioStudies
Project description:Temperature-induced changes in thermotolerance and protein composition were examined in heat-shocked cells and high-temperature-grown cells of the extremely thermophilic bacterium Rhodothermus obamensis. The survival at temperatures superoptimal for growth (90 and 95 degrees C) was enhanced in both heat-shocked cells and high-temperature-grown cells relative to that of cells grown at optimal temperatures. In a comparison of protein composition using two-dimensional gel electrophoresis, putative heat shock proteins (HSPs) and high-temperature growth-specific proteins (HGPs) were detected. N-terminal amino acid sequence analysis revealed that the putative HSPs were quite similar to the ATP-binding subunits of ABC transporters and the HGPs were proteins corresponding to domains II and III of elongation factor Tu. These results suggested that this extreme thermophile has developed temperature-induced responses that include increased survival under hyperthermal conditions, changes in protein composition, and also the production of novel HSPs.
1998-01-01 | S-EPMC107234 | BioStudies
Project description:When organisms are exposed to an increase in temperature, they undergo a heat shock response (HSR) regulated by the transcription factor heat shock factor 1 (HSF-1). The heat shock response includes the rapid changes in gene expression initiated by binding of HSF-1 to response elements in the promoters of heat shock genes. Heat shock proteins function as molecular chaperones to protect proteins during periods of elevated temperature and other stress. During infection, hookworm infective third stage larvae (L3) undergo a temperature shift from ambient to host temperature. This increased temperature is required for the resumption of feeding and activation of L3, but whether this increase initiates a heat shock response is unknown. To investigate the role of the heat shock in hookworm L3 activation and parasitic development, we identified and characterized the expression profile of several components of the heat shock response in the hookworm Ancylostoma caninum. We cloned DNAs encoding an hsp70 family member (Aca-hsp-1) and an hsp90 family member (Aca-daf-21). Exposure to a heat shock of 42°C for one hour caused significant up-regulation of both genes, which slowly returned to near baseline levels following one hour attenuation at 22°C. Neither gene was up-regulated in response to host temperature (37°C). Conversely, levels of hsf-1 remained unchanged during heat shock, but increased in response to incubation at 37°C. During activation, both hsp-1 and daf-21 are down regulated early, although daf-21 levels increase significantly in non-activated control larvae after 12h, and slightly in activated larvae by 24h incubation. The heat shock response modulators celastrol and KNK437 were tested for their effects on gene expression during heat shock and activation. Pre-incubation with celastrol, an HSP90 inhibitor that promotes heat shock gene expression, slightly up-regulated expression of both hsp-1 and daf-21 during heat shock. KNK437, an inhibitor of heat shock protein expression, slightly down regulated both genes under similar conditions. Both modulators inhibited activation-associated feeding, but neither had an effect on hsp-1 levels in activated L3 at 16h. Both celastrol and KNK437 prevent the up-regulation of daf-21 and hsf-1 seen in non-activated control larvae during activation, and significantly down regulated expression of the HSF-1 negative regulator Aca-hsb-1 in activated larvae. Expression levels of heat shock response factors were examined in developing Ancylostoma ceylanicum larvae recovered from infected hosts and found to differ significantly from the expression profile of activated L3, suggesting that feeding during in vitro activation is regulated differently than parasitic development. Our results indicate that a classical heat shock response is not induced at host temperature and is suppressed during larval recovery and parasitic development in the host, but a partial heat shock response is induced after extended incubation at host temperature in the absence of a developmental signal, possibly to protect against heat stress.
2015-01-01 | S-EPMC4605861 | BioStudies
Project description:Whole-genome analysis of heat shock factor binding sites in Drosophila melanogaster. Heat shock factor IP DNA from non-shock (room temperature) Kc 167 cells compared to whole cell extract on Agilent 2x244k tiling arrays. Overall design: Heat Shock Factor IP vs whole cell extract from non-shock (room temperature) Kc cells.
2011-01-05 | GSE22335 | GEO