The acquisition of thermal tolerance in larvae of Calpodes ethlius (Lepidoptera) and the in situ and in vitro synthesis of heat-shock proteins

Abstract

Larvae of Calpodes ethlius (Lepidoptera) reared at 22 degrees C die after 1 h at 45 degrees C, but they acquire the ability to tolerate 1 h at 45 degrees C if they are first exposed to 37 degrees C for 1 or 2 h. Incubation of intact larvae at 37 degrees C for 1 h induces the new and (or) enhanced synthesis of a similar family of polypeptides (relative masses (MrS) approximately 22 000) in all tissues examined (silk gland, fat body, wing discs, central nervous system, and muscle). When these same tissues are cultured at 37 degrees C for 1 h, the new and (or) enhanced synthesis of at least 5 polypeptides (MrS approximately 95 000, 81 000, 74 000, 26 000, and 22 000) is evident. The more dramatic response elicited from cultured tissues by heat shock results, presumably, from the added stress of dissection. The new and (or) enhanced synthesis of polypeptides with MrS of approximately 22 000 by tissues of intact larvae, incubated at 37 degrees C for 1 h, may be related to the acquisition of thermal tolerance by similarly treated larvae. These results suggest that the induced synthesis of these polypeptides is an integral part of a ubiquitous molecular mechanism involved in the development of thermal tolerance.

Temperature ranges over which rainbow trout fibroblasts survive and synthesize heat‐shock proteins

“…These are polypeptides whose synthesis is induced andlor enhanced by a variety of stressors, which include heat and heavy metals (Schlesinger et al, 1982;Nover, 1984;Atkinson and Walden, 1985). Little is known about their function, but hsps appear to be involved in the development of thermotolerance (Li and Werb, 1982;Dean and Atkinson, 1983) and may be part of a general protective mechanism for cells under physiological and environmental stress (Currie and White, 1981;Schlesinger et al, 1982). For vertebrates, stress proteins have been studied primarily with cells in culture.…”

Accumulation of Heat Shock Proteins in Field-Grown Cotton

“…Studies with mammalian cells (13), yeast (24), Drosophila (25), Calpodes (10), and Dictyostelium (23) have demonstrated that exposure to elevated, sublethal temperatures induces a transient thermoresistance, which protects them from a second exposure at typically lethal temperatures. A correlation between the development of thermotolerance and the synthesis of HSPs has been reported, although the mechanisms underlying the thermotolerance remain unknown (19,21).…”

Synthesis and secretion of immunoglobulin G by lymphocytes from cultured mouse spleen cells is not affected by heat shock

“…Considerable evidence suggests that the HS response (i.e., synthesis of HSPs) may act as a universal and fundamental mechanism for cell protection during periods of diverse environmental stress. This evidence includes the wide variety of stresses capable of inducing HSP synthesis (Subjeck and Shyy, 1986), the conservation through evolution of the HS genes and the consensus sequences required for their transcription (Craig, 1985;Pelham, 19851, the correlation of HSP synthesis with the protection that mild heat treatment or chemical-stress offer to cells (Li and Laszlo, 1985) or animals (Dean and Atkinson, 1983) subsequently exposed to lethal temperatures (thermotolerance), and the correlation of HSP synthesis resulting from mild heat pretreatment with protection from phenocopy induction (Mitchell et al, 1979). In many cell types, enhanced HSP synthesis by heat-shocked cells appears to be accompanied by the depressed synthesis of many normally synthesized polypeptides, as a result of preferential transcription of the HS genes (Ashburner and Bonner, 1979;Lindquist and DiDomenico, 19851, the preferential selection and translation of the HS mRNAs, and the sequestering of preexisting mRNAs translated prior to the HS treatment (Lindquist and DiDomenico, 1985;Craig, 1985).…”