Jang E B
USDA-ARS, Tropical Fruit and Vegetable Research Laboratory, Hilo, Hawaii 96720.
Arch Insect Biochem Physiol. 1992;19(2):93-103. doi: 10.1002/arch.940190203.
Heat shock proteins (hsps) were identified in a cell line from the Mediterranean fruit fly, Ceratitis capitata Wiedemann (Diptera: Tephritidae) exposed to elevated temperatures. Cells produced three hsps (Mr 87,000, 69,000, and 34,000) in response to a temperature shift from 26 degrees C to 37 degrees C (30-60 min) with a concomitant decrease in synthesis of most other cellular proteins. Synthesis of low Mr hsps was not evident. The heat shock response is triggered within 30 min at temperatures from 33 degrees C to 41 degrees C. At temperatures greater than 41 degrees C protein synthesis was shut down. Within 2-3 h after return to 26 degrees C, synthesis of proteins repressed at the higher temperatures resumed production while the major hsps disappear. Heat shock proteins were not produced in the presence of actinomycin D. Evaluations on the role of hsps in conferring thermotolerance to the cells showed an increase in cell viability in heat-shocked cells over non-heat-shocked cells (after 3 and 10 days) when subsequently placed at 45 degrees C for 1 h, a normally lethal temperature. Heat shock alone had little effect on subsequent cell viability or growth at 26 degrees C. These results suggest that hsps produced by these cells may aid in the maintenance of cell integrity and thus play a transitory role in thermotolerance.
在地中海实蝇(Ceratitis capitata Wiedemann,双翅目:实蝇科)的一个细胞系中,研究人员鉴定出了热休克蛋白(hsps),该细胞系被置于高温环境中。当温度从26摄氏度转变为37摄氏度(30 - 60分钟)时,细胞产生了三种热休克蛋白(分子量分别为87,000、69,000和34,000),与此同时,大多数其他细胞蛋白的合成减少。低分子量热休克蛋白的合成并不明显。在33摄氏度至41摄氏度的温度下,30分钟内即可触发热休克反应。当温度高于41摄氏度时,蛋白质合成停止。回到26摄氏度后的2 - 3小时内,在较高温度下受到抑制的蛋白质合成恢复,而主要的热休克蛋白消失。在放线菌素D存在的情况下,不会产生热休克蛋白。对热休克蛋白赋予细胞耐热性作用的评估表明,热休克细胞在随后置于45摄氏度(通常为致死温度)1小时后(3天和10天后),其细胞活力比未受热休克处理的细胞有所增加。单独的热休克对随后在26摄氏度下的细胞活力或生长几乎没有影响。这些结果表明,这些细胞产生的热休克蛋白可能有助于维持细胞完整性,从而在耐热性方面发挥短暂作用。