Regulation of heat shock gene induction and expression during Drosophila development

Michaud, Sébastien; Marín, Raquel; Tanguay, Robert M.

doi:10.1007/pl00000572

Cited by 110 publications

(78 citation statements)

References 110 publications

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“…The four classical small HSPs (HSP22, HSP23, HSP26, and HSP27) were all highly induced after a heat shock (Fig. 1B), consistent with previous findings (Marin et al ., 1996; Michaud et al ., 1997). Apart from CG14207 and CG13133, all the other small HSPs were also found to be heat‐inducible (Fig.…”

Section: Resultsmentioning

confidence: 99%

Specific protein homeostatic functions of small heat‐shock proteins increase lifespan

et al. 2015

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SummaryDuring aging, oxidized, misfolded, and aggregated proteins accumulate in cells, while the capacity to deal with protein damage declines severely. To cope with the toxicity of damaged proteins, cells rely on protein quality control networks, in particular proteins belonging to the family of heat‐shock proteins (HSPs). As safeguards of the cellular proteome, HSPs assist in protein folding and prevent accumulation of damaged, misfolded proteins. Here, we compared the capacity of all Drosophila melanogaster small HSP family members for their ability to assist in refolding stress‐denatured substrates and/or to prevent aggregation of disease‐associated misfolded proteins. We identified CG14207 as a novel and potent small HSP member that exclusively assisted in HSP70‐dependent refolding of stress‐denatured proteins. Furthermore, we report that HSP67BC, which has no role in protein refolding, was the most effective small HSP preventing toxic protein aggregation in an HSP70‐independent manner. Importantly, overexpression of both CG14207 and HSP67BC in Drosophila leads to a mild increase in lifespan, demonstrating that increased levels of functionally diverse small HSPs can promote longevity in vivo.

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Section: Resultsmentioning

confidence: 99%

Specific protein homeostatic functions of small heat‐shock proteins increase lifespan

et al. 2015

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“…For example, a Hsp60 expression increase was observed in heart failure (Lin et al 2007;Wang et al 2010). It is known that Hsp27 is usually expressed in heart muscle tissues under normal conditions where its function can be modified by different cell mechanisms operating either on their expression or their structure depending on cellular localization (Michaud et al 1997;Anastasiya et al 2005). However, several studies have indicated that overexpression of Hsp27 protects cardiac myocytes against ischemic injury (Yamboliev et al 2000;Vander Heide 2002).…”

Section: Introductionmentioning

confidence: 99%

The role of heat shock proteins in inflammatory injury induced by cold stress in chicken hearts

Zhao

Zhang

Wang

et al. 2013

Cell Stress and Chaperones

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The aim of this study was to investigate the effects of cold stress on the expression levels of heat shock proteins (Hsps90, 70, 60, 40, and 27) and inflammatory factors (iNOS, COX-2, NF-κB, TNF-α, and PTGEs) and oxidative indexes in hearts of chickens. Two hundred forty 15-day-old male chickens were randomly divided into 12 groups and kept at the temperature of 12±1°C for acute and chronic cold stress. There were one control group and five treatment groups for acute cold stress, three control groups, and three treatment groups for chronic cold stress. After cold stress, malondialdehyde level increased in chicken heart; the activity of superoxide dismutase and glutathione peroxidase in the heart first increased and then decreased. The inflammatory factors mRNA levels were increased in cold stress groups relative to control groups. The histopathological analysis showed that heart tissues were seriously injured in the cold stress group. Additionally, the mRNA levels of Hsps (70, 60, 40, and 27) increased significantly (P<0.05) in the cold stress groups relative to the corresponding control group. Meanwhile, the mRNA level and protein expression of Hsp90 decreased significantly (P<0.05) in the stress group, and showed a gradually decreasing tendency. These results suggested that the levels of inflammatory factors and Hsps expression levels in heart tissues can be influenced by cold stress. Hsps commonly played an important role in the protection of the heart after cold stress.

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“…The sequences which regulate the tissue-specific expression and the heat shock expression of D. melanogaster hsp26 have been shown to be located in different parts of the promoter. Three regions involved in spermatocyte-specific expression are identified downstream from −352, whereas the ovarian expression is dependent on the region (−522 to −352) (Cohen and Meselson 1985;Frank et al 1992;Michaud et al 1997).…”

Section: Discussionmentioning

confidence: 99%

“…The sHsps have many different functions, both under stress and under non-stress conditions (Mestril et al 1986;Michaud et al 1997;Michaud and Tanguay 2003). Under stress conditions they have chaperone functions, protect the cytoskeleton and modulate the apoptotic process.…”

Section: Introductionmentioning

confidence: 99%

“…In D. melanogaster, the regulation of each of the shsps has been thoroughly investigated, either using promoter deletions to locate important regulator regions (Cohen and Meselson 1985;Riddihough and Pelham 1986;Frank et al 1992;Michaud et al 1997), or regulation by known tissue specific transcription factors (Michaud and Tanguay 2003) or search for consensus transcription factor binding sites. The expression after heat shock is regulated by the heat shock factor (HSF) binding to the heat shock element (HSE) and HSE have been found in the promoter of most hsp genes (Mestril et al 1986;Sandaltzopoulos et al 1995;Riddihough and Pelham 1986).…”

Section: Introductionmentioning

confidence: 99%

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Characterization of the shsp genes in Drosophila buzzatii and association between the frequency of Valine mutations in hsp23 and climatic variables along a longitudinal gradient in Australia

Frydenberg

Barker

Loeschcke

2010

Cell Stress and Chaperones

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The small heat shock gene (shsp) cluster of Drosophila buzzatii was sequenced and the gene order and DNA sequence were compared with those of the shsps in Drosophila melanogaster. The D. buzzatii shsp cluster contains an inversion and a duplication of hsp26. A phylogenetic tree was constructed based on hsp26 genes from several Drosophila species of the Sophophora and Drosophila subgenera. The tree shows first a separation of the Sophophora and the Drosophila subgenera and then the Drosophila subgenus is divided into the Hawaiian Drosophila and the repleta/virilis groups. Only the latter contain a duplicated hsp26. Comparing the gene organisation of the shsp cluster shows that all the Drosophila subgenus species contain the inversion. Putative heat shock elements (HSE) were found in the promoters of all the shsp and putative regulator elements for tissue specific expression were found in the promoter of hsp23, hsp27 and one of the hsp26 genes. hsp23 was found to be polymorphic for four non-synonymous changes that all lead to exchange of a Valine. The duplicated hsp26 gene in D. buzzatii (phsp26) was polymorphic for two non-synonymous changes. The allele frequencies of these variants were determined in nine D. buzzatii populations covering most of its distribution in Australia using high-resolution melting curves. The allele frequencies of one of the hsp23 variants showed a significant linear regression with longitude and the pooled frequency of the four Valine changes of hsp23 in the nine populations showed a significant linear regression with longitude and with a composite measure of climatic variables.

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Regulation of heat shock gene induction and expression during Drosophila development

Cited by 110 publications

References 110 publications

Specific protein homeostatic functions of small heat‐shock proteins increase lifespan

Specific protein homeostatic functions of small heat‐shock proteins increase lifespan

The role of heat shock proteins in inflammatory injury induced by cold stress in chicken hearts

Characterization of the shsp genes in Drosophila buzzatii and association between the frequency of Valine mutations in hsp23 and climatic variables along a longitudinal gradient in Australia

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