Dataset Information

Upregulation of heat-shock proteins in larvae, but not adults, of the flesh fly during hot summer days.

ABSTRACT: Heat-shock proteins (HSPs) are highly expressed when organisms are exposed to thermal stresses. The HSPs are considered to play significant roles in thermal adaptation because they function as molecular chaperones facilitating proper protein synthesis. The expression of HSPs under field conditions, however, has not been evaluated much, and their importance, based on the ecological contexts in nature, is still unclear. We investigated this aspect in the larvae and adults of the flesh fly, Sarcophaga similis. These larvae spend their larval life in the carrion or faeces of vertebrates; therefore, they are less mobile and are occasionally exposed to high temperature. In contrast, the adults of this species can fly and, therefore, they are highly mobile. Massive transcription of Hsps was detected both in the larvae and adults in a laboratory heat-shock experiment. The larvae in the field showed no or less Hsp production on thermally mild days, whereas considerable upregulation of Hsp expression was detected on days with high temperature. The adults can also be exposed to thermal stress as high as 40 °C or higher in the field. However, most of the flies showed no or less Hsp expression. The observations in the experimental cage under field conditions revealed behavioural thermoregulation of adults through microhabitat selection. The present study demonstrates ontogenetic alteration of the strategy to overcome thermal stress in an insect; in the field, less mobile larvae use physiological protection against heat (HSP production), whereas highly mobile adults avoid the stress behaviourally (through microhabitat selection).

SUBMITTER: Harada E

PROVIDER: S-EPMC5655370 | biostudies-literature | 2017 Nov

REPOSITORIES: biostudies-literature

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Upregulation of heat-shock proteins in larvae, but not adults, of the flesh fly during hot summer days.

Harada Eri E Goto Shin G SG

Cell stress & chaperones 20170608 6

Heat-shock proteins (HSPs) are highly expressed when organisms are exposed to thermal stresses. The HSPs are considered to play significant roles in thermal adaptation because they function as molecular chaperones facilitating proper protein synthesis. The expression of HSPs under field conditions, however, has not been evaluated much, and their importance, based on the ecological contexts in nature, is still unclear. We investigated this aspect in the larvae and adults of the flesh fly, Sarcoph ...[more]

PMID: 28597340

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Project description:OBJECTIVE:Present study explores the effect of hot summer period on the glycolytic rate of early post-mortem meat quality of Ghungroo and Large White Yorkshire (LWY) pig and comparative adaptability to high temperature between above breeds by shifting the expression of stress related genes like mono-carboxylate transporters (MCTs) and heat shock proteins (HSPs). METHODS:Healthy pigs of two different breeds, viz., LYW and Ghungroo (20 from each) were maintained during hot summer period (May to June) with a mean temperature of about 38°C. The pigs were slaughtered and meat samples from the longissimus dorsi (LD) muscles were analyzed for pH, glycogen and lactate content and mRNA expression. Following 24 h of chilling, LD muscle was also taken from the carcasses to evaluate protein solubility and different meat quality measurements. RESULTS:LWY exhibited significantly (p<0.01) higher plasma cortisol and lactate dehydrogenase concentration than Ghungroo indicating their higher sensitivity to high temperature. LD muscle from LWY pigs revealed lower initial and ultimate pH values and higher drip loss compared to Ghungroo, indicating a faster rate of pH fall. LD muscle of Ghungroo had significantly lower lactate content at 45 min postmortem indicating normal postmortem glycolysis and much slower glycolytic rate at early postmortem. LD muscle of LWY showed rapid postmortem glycolysis, higher drip loss and higher degrees of protein denaturation. Ghungroo exhibited slightly better water holding capacity, lower cooking loss and higher protein solubility. All HSPs (HSP27, HSP70, and HSP90) and MCTs (MCT1, MCT2, and MCT4) in the LD muscle of pigs inclined to increase more in Ghungroo than LWY when exposed to high temperature. CONCLUSION:Effect of high temperature on the variation of HSPs and MCTs may play a crucial role in thermal tolerance and adaptation to different climatic conditions, pH regulation, muscle acidification, drip loss, protein denaturation and also in postmortem meat quality development.

Project description:It is known from earlier studies that the heat shock (HS) response in Malpighian tubules (MTs) of Drosophila larvae is different from that in other tissues because instead of the Hsp70 and other common heat shock proteins, Hsp64 and certain other new proteins are induced immediately after HS. In the present study, we examined the kinetics of the synthesis of Hsp70 and Hsp64 immediately after HS and during recovery from HS by 35S-methionine labeling and Western blotting. In addition, we also examined the transcriptional activity of hsp70 genes in larval MT cells at different times after HS by in situ hybridization and Northern blotting. The HS-induced synthesis of Hsp64 ceased by 1 hour of recovery from the HS when synthesis of the Hsp70 commenced. Our results revealed that the induced synthesis of Hsp64 immediately after HS was dependent on new transcription. Although the levels of Hsp70 in MT cells rapidly increased after its synthesis began during recovery, the levels of Hsp64 remained unaltered irrespective of its new synthesis occurring during or after HS. Inhibition of new Hsp64 synthesis by transcriptional or translational inhibitors also did not affect the total amount of this protein in MTs. The Hsp64 polypeptides synthesized in response to HS are degraded rapidly. Apparently, the cells in MTs maintain a balance between new synthesis of Hsp64 and its turnover so that under all conditions a more or less constant level of this protein is maintained. Although the Hsp70 synthesis started only after 1 hour of recovery, the hsp70 genes were transcriptionally activated immediately after HS and they continued to transcribe till at least 4 hours after the HS. The hsp70 transcripts in MT cells that recovered for 2 hours or longer did not contain the 3' untranslated regions (UTRs), which may allow their longer stability and translatability at normal temperature. Synthesis of Hsp70 during recovery period was dependent on continuing transcription. Assessment of the beta-galactosidase activity in 2 transgenic lines carrying the LacZ reporter gene under hsp70 promoter and different lengths of the 5'UTR suggested that the delayed translation of hsp70 transcripts in MTs is probably regulated by some elements in the 5'UTR.

Dataset Information

Upregulation of heat-shock proteins in larvae, but not adults, of the flesh fly during hot summer days.

Publications

Upregulation of heat-shock proteins in larvae, but not adults, of the flesh fly during hot summer days.

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