Gabai V L, Kabakov A E
Medical Radiology Research Center, Obninsk, Russian Federation.
FEBS Lett. 1993 Aug 2;327(3):247-50. doi: 10.1016/0014-5793(93)80997-9.
Heat shock (44 degrees C for 10 min) or ATP depletion by an uncoupler (CCCP for 20 min) is shown to result in stimulation of hsp68/70 synthesis in Ehrlich tumor cells. After 3 h of recovery, the cells become thermotolerant. Surprisingly, repeated ATP depletion caused by CCCP or rotenone (a respiratory inhibitor) treatment, had a much lower effect on cell viability. Both induction of tolerance to energy deprivation and hsp68/70 synthesis were totally suppressed by cycloheximide, an inhibitor of cytosolic protein synthesis. In tolerant cells, rotenone still induced ATP depletion; however, protein aggregation (the rise in Triton-insoluble proteins) was inhibited in these cells. It is suggested that cellular chaperones (e.g. hsp70) are involved in the protection of ischemic cells from necrosis, preventing protein aggregation under ATP deficiency.
热休克（44摄氏度，持续10分钟）或通过解偶联剂（羰基氰-间氯苯腙，CCCP，持续20分钟）消耗ATP，已被证明会导致艾氏腹水瘤细胞中hsp68/70合成的刺激。恢复3小时后，细胞变得耐热。令人惊讶的是，由CCCP或鱼藤酮（一种呼吸抑制剂）处理引起的反复ATP消耗，对细胞活力的影响要低得多。对能量剥夺的耐受性诱导和hsp68/70合成均被环己酰亚胺（一种胞质蛋白合成抑制剂）完全抑制。在耐受细胞中，鱼藤酮仍会诱导ATP消耗；然而，这些细胞中的蛋白质聚集（Triton不溶性蛋白质的增加）受到抑制。有人提出，细胞伴侣（如hsp70）参与保护缺血细胞免于坏死，在ATP缺乏时防止蛋白质聚集。
