Heat shock protein synthesis can be induced during recovery from cold treatment of Drosophila melanogaster larvae. Survival of larvae after a cold treatment is dramatically improved by a mild heat shock just before the cold shock. The conditions which induce tolerance to cold are similar to those which confer tolerance to heat.Heat shock proteins are a group of proteins which are universally expressed in response to heat, heavy metals, and a variety of chemical treatments (1, 5, 10, 11). The major heat shock proteins synthesized in bacteria, plants, and mammals show a high degree of sequence homology (1, 5). These proteins are also synthesized during some periods in normal development.Transient resistance to killing by heat stress has been observed to be induced in many organisms by an initial exposure to a sublethal heat treatment (2, 7, 11). We have shown that conditions which induce thermotolerance in Drosophila melanogaster also induce the synthesis of heat shock proteins (7), and this correlation has been repeated many times in a variety of systems (1,5). Because of this and the universality of the response, it has been suggested that heat shock proteins play a role in protecting cells from damage caused by these stresses. The precise function of the heat shock proteins as well their role in stress protection are still uncertain.We show here that heat shock proteins are synthesized during recovery from prolonged exposure to cold in the absence of heat shock and that a mild heat treatment of the same kind which protects against death from heat shock also prevents death from exposure to cold.Induction of heat shock proteins by cold treatment. Drosophila larvae recovering from cold treatments of more than 8 h at 0°C synthesized the same set of heat shock or stress proteins that are made in response to heat shock (7, 9, 12). Figure 1 shows the proteins synthesized in larval salivary glands during recovery from 14 h at 0°C. Salivary glands were dissected from cold-shocked larvae that had been allowed to recover for 0, 10, 20, 30, or 40 min at 25°C. The salivary glands were labeled for 30 min with ['5S] methionine, and the proteins were separated on sodium dodecyl sulfate-polyacrylamide gels as described previously (8). An untreated 25°C control is shown in Fig. 1, lane C, as is a typical heat shock pattern from animals heated to 37°C (lane H). Clearly, all the major heat shock proteins appeared in the 20-min sample. The strongest heat shock protein synthesis patterns were seen not during the 30 min immediately following the cold treatment, but rather when larvae were allowed to recover for 30 or 40 min before being labeled. This suggests that the induction of the heat shock proteins may be a response to the shift from 0 to 25°C rather than a response to the 0°C treatment itself. We are currently doing * Corresponding author.RNA blots to determine directly the levels of hsp70 mRNA present at 0°C and during the recovery at 25°C.Experiments designed to evaluate the effects of different durations of cold treatments ...
Heat shock protein synthesis can be induced during recovery from cold treatment of Drosophila melanogaster larvae. Survival of larvae after a cold treatment is dramatically improved by a mild heat shock just before the cold shock. The conditions which induce tolerance to cold are similar to those which confer tolerance to heat.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.
hi@scite.ai
10624 S. Eastern Ave., Ste. A-614
Henderson, NV 89052, USA
Copyright © 2024 scite LLC. All rights reserved.
Made with 💙 for researchers
Part of the Research Solutions Family.