The induction of gene activity in drosophila by heat shock

Ashburner, Michael; Bonner, J. Jose

doi:10.1016/0092-8674(79)90150-8

Cited by 1,294 publications

(583 citation statements)

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“…To analyze which of the 11 D. melanogaster small HSPs are heat‐inducible, we heat‐shocked Drosophila S2 cells at 38 °C for 30 min and analyzed the small HSP mRNA levels by qPCR. As controls, we measured the mRNA levels of HSC70‐4 and HSC70‐5, two constitutively expressed genes not responsive to heat shock (Ashburner & Bonner, 1979; Ish‐Horowicz et al ., 1979), and HSP70Aa, a highly heat‐inducible gene (Fig. 1A).…”

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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“…Their induction requires a brief hyperthermic treatment (5-10 min at 45°C) and their synthesis is maximal after a 2 h "development" at 37°C. Whilst the function of HSP is still a matter of speculation, it has been suggested that they might be concerned with the "maintenance" or "repair" of cellular homeo-stasis after the initial hyperthermic treatment (Ashburner & Bonner, 1979 Labelling of cells with L-35S-methionine.-Half a million cells were allowed to grow overnight in the bottom of glass scintillation vials as described previously . Hyperthermia was administered by immersion of the vial in a water bath at the appropriate temperature.…”

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confidence: 99%

Hyperthermia and the heat-shock proteins of HeLa cells

Burdon¹,

Slater²,

McMahon³

et al. 1982

Br J Cancer

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Summary.-When HeLa cells are subject to hyperthermia, the synthesis of specific heat-shock proteins (HSP) is induced under a variety of thermal conditions. HSP synthesis does not occur at temperatures above 43°C but requires return to a culture temperature of 37°C. Maximal induction appears to be achieved if a brief hyperthermia treatment (10 min, 45°-46°C) is followed by 2 h "development" at 37°C. The induction process requires transcription but not DNA replication, and general cell metabolism is probably also required, as induction does not occur if the heat-treated cells are returned to 40 (rather than 37°C) for development.A small proportion of the HSPs of 72-74 Kd are found in nuclei, but do not appear to bind to DNA. The bulk of these proteins, as well as those at 100 Kd, are cytoplasmic, but none are preferentially associated with mitochondria.

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“…These proteins are made in response to a variety of environmental stresses including heat, anoxia and various chemical and mechanical stresses (Ashburner & Bonner, 1979). It has been suggested that hsp may perform a function which is essential to cell survival following certain kinds of stress (Loomis & Wheeler, 1980;Ashburner & Bonner, 1979;Guttman et al, 1980).…”

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confidence: 99%