02736nas a2200265   4500008004600000245010700046210006900153300001400222490000800236520184900244653001602093653003202109653001202141653002302153653001602176653002402192653001802216653004502234653003602279653003902315100002302354700002102377700002202398856005002420       Submitted                   eng d     00aDesiccation and rehydration elicit distinct heat shock protein transcript responses in flesh fly pupae0 aDesiccation and rehydration elicit distinct heat shock protein t  a963 - 9710 v2073 aHeat shock proteins (Hsps) are a ubiquitous component of the cellular response to stress in both prokaryotic and eukaryotic organisms, but their role and function during desiccation stress in terrestrial arthropods has received limited attention. Molecular responses to rehydration are arguably as important as those to desiccation in maintaining cellular integrity and enzyme activity, but the role of Hsps during stress recovery is poorly understood and has never been addressed with respect to rehydration in insects. This study identifies distinct differences in the Hsp response to desiccation and rehydration in the flesh fly Sarcophaga crassipalpis, as well as differences in the desiccation responses of diapausing and nondiapausing pupae. In nondiapausing pupae, the expression of two inducible Hsps (Hsp23 and Hsp70) is upregulated by desiccation, but the water loss threshold for Hsp expression changes at different rates of dehydration. Continued desiccation results in the prolonged expression of both Hsp23 and Hsp70, which may contribute to the delayed adult eclosion noted in samples desiccated for more than 3 days at &lt;5% relative humidity/25 degrees C. In diapausing pupae, hsp23 and hsp70 transcripts are already highly expressed and are not further upregulated by desiccation stress. Both of the constitutive Hsps investigated, Hsp90 and Hsc70, were unresponsive to desiccation in both nondiapausing and diapausing pupae. However, both Hsp90 and Hsc70 were upregulated upon rehydration in nondiapausing and diapausing pupae. These results indicate distinct roles for the different Hsps during desiccation stress and rehydration/stress recovery. The response to desiccation recovery (rehydration) is similar to the Hsp response to cold recovery identified in S. crassipalpis: Hsp90 and Hsc70 are upregulated in both cases.10a*Body Water10a*Gene Expression Regulation10aAnimals10aBlotting, Northern10aDesiccation10aDiptera/*physiology10aFluid Therapy10aHeat-Shock Proteins/genetics/*metabolism10aHibernation/genetics/physiology10aRNA, Messenger/genetics/metabolism1 aHayward, S., A. L.1 aRinehart, J., P.1 aDenlinger, D., L.  uhttps://sarcophagidae.myspecies.info/node/76402638nas a2200313   4500008004600000245014100046210006900187300001400256490000700270520155500277653001201832653002101844653002401865653002001889653005801909653002401967653003801991653003402029653005102063653002002114653001202134653001702146100002302163700002102186700002402207700002102231700002202252856005002274       Submitted                   eng d     00aTemporal expression patterns of diapause-associated genes in flesh fly pupae from the onset of diapause through post-diapause quiescence0 aTemporal expression patterns of diapauseassociated genes in fles  a631 - 6400 v513 aDistinct differences in the temporal expression patterns of genes associated with pupal diapause were noted in the flesh fly, Sarcophaga crassipalpis. The first change observed was a decline in expression of the gene encoding heat shock protein 90 (hsp90) 2 days after pupariation (1 day before the pupa reaches the phanerocephalic stage characteristic of diapause). In contrast, hsp23 and hsp70 transcripts were undetectable in nondiapause samples and d1-d4 diapause-programmed pupae, but were up-regulated just after the start of diapause, 5 days after pupariation. An increase of glycerol content in diapausing pupae was also noted at the start of diapause. The gene encoding proliferating cell nuclear antigen (pcna) was diapause down-regulated, and this occurred in two phases, with the first decline in expression 7 days after pupariation and a second decline in the level of expression on day 14. For pupae held at 20 degrees C for 20 days and transferred to 10 degrees C, diapause ended after 90-100 days at the lower temperature. However, pupae remained in a state of post-diapause quiescence (d100-d150) and sustained diapause-like hsp and pcna expression patterns until adult development was initiated. Glycerol concentrations and survival declined during the post-diapause phase. This study suggests a distinct sequence in the pattern of gene expression at the onset of diapause, but the genes we have monitored do not contribute to the switch to covert developmental potential at the transition from diapause to post-diapause quiescence.10aAnimals10aCold Temperature10aDiptera/*physiology10aDown-Regulation10aGene Expression Regulation, Developmental/*physiology10aGlycerol/metabolism10aHeat-Shock Proteins/*biosynthesis10aInsect Proteins/*biosynthesis10aProliferating Cell Nuclear Antigen/*metabolism10aPupa/physiology10aSeasons10aTime Factors1 aHayward, S., A. L.1 aPavlides, S., C.1 aTammariello, S., P.1 aRinehart, J., P.1 aDenlinger, D., L.  uhttps://sarcophagidae.myspecies.info/node/647