Department of Chemical Engineering, Tulane University, Boggs Center Rm. 300, 70118, New Orleans, LA, USA.
Cytotechnology. 1995 Jan;17(2):91-101. doi: 10.1007/BF00749396.
In this study, we compare stress protein induction in anoxic and hyperthermicSpodoptera frugiperda cells. Anoxia transiently induces a cluster of heat shock proteins at 71 and 72 kDa. This is a subset of a larger group of stress proteins induced by heat shock. Several heat shock proteins reported in this study were previously undetected inS. frugiperda. With these additional proteins, the stress response of hyperthermicS. frugiperda closely resembles that ofDrosophila melanogaster. Prior investigations of stress protein induction during oxygen deprivation focused on mammalian cells. In sharp contrast to these cells, anoxicS. frugiperda cells neither induce glucose-regulated proteins nor suppress the heat shock family of 71/72 kDa proteins. These findings provide insight into the virtually unexplored area of stress protein induction in anoxic insect cells. In addition, they help to explain the effects of oxygen deprivation on heterologous protein yield from virally infected insect cells and to develop an oxygenregulated promoter for stably transformed insect cells.
在这项研究中，我们比较了缺氧和高温条件下 Spodoptera frugiperda 细胞中应激蛋白的诱导情况。缺氧会短暂诱导一组 71 和 72 kDa 的热休克蛋白。这是热休克诱导的更大应激蛋白组的一个子集。本研究中报道的几种热休克蛋白以前在 Spodoptera frugiperda 中未被检测到。有了这些额外的蛋白质，高温下 Spodoptera frugiperda 的应激反应与 Drosophila melanogaster 非常相似。以前关于缺氧条件下应激蛋白诱导的研究主要集中在哺乳动物细胞上。与这些细胞形成鲜明对比的是，缺氧的 Spodoptera frugiperda 细胞既不诱导葡萄糖调节蛋白，也不抑制 71/72 kDa 的热休克蛋白家族。这些发现为我们深入了解缺氧昆虫细胞中应激蛋白诱导的这一几乎未被探索的领域提供了线索。此外，它们有助于解释缺氧对病毒感染的昆虫细胞中外源蛋白产量的影响，并开发用于稳定转化的昆虫细胞的氧调控启动子。
