Villeneuve Tania S, Ma Xiaocui, Sun Yu, Oulton Mindy M, Oliver Ann E, MacRae Thomas H
Department of Biology, Dalhousie University, Halifax, NS B3H 4J1 Canada.
Cell Stress Chaperones. 2006 Spring;11(1):71-80. doi: 10.1379/csc-154r.1.
p26, an abundantly expressed small heat shock protein, is thought to establish stress resistance in oviparously developing embryos of the crustacean Artemia franciscana by preventing irreversible protein denaturation, but it might also promote survival by inhibiting apoptosis. To test this possibility, stably transfected mammalian cells producing p26 were generated and their ability to resist apoptosis induction determined. Examination of immunofluorescently stained transfected 293H cells by confocal microscopy demonstrated p26 is diffusely distributed in the cytoplasm with a minor amount of the protein in nuclei. As shown by immunoprobing of Western blots, p26 constituted approximately 0.6% of soluble cell protein. p26 localization and quantity were unchanged during prolonged culture, and the protein had no apparent ill effects on transfected cells. Molecular sieve chromatography in Sepharose 6B revealed p26 oligomers of about 20 monomers, with a second fraction occurring as larger aggregates. A similar pattern was observed in sucrose gradients, but overall oligomer size was smaller. Mammalian cells containing p26 were more thermotolerant than cells transfected with the expression vector only, and as measured by annexin V labeling, Hoescht 33342 nuclear staining and procaspase-3 activation, transfected cells effectively resisted apoptosis induction by heat and staurosporine. The ability to confer thermotolerance and limit heat-induced apoptosis is important because Artemia embryos are frequently exposed to high temperature in their natural habitat. p26 also blocked apoptosis in transfected cells during drying and rehydration, findings with direct relevance to Artemia life history characteristics because desiccation terminates cyst diapause. Thus, in addition to functioning as a molecular chaperone, p26 inhibits apoptosis, an activity shared by other small heat shock proteins and with the potential to play an important role during Artemia embryo development.
p26是一种大量表达的小热休克蛋白,人们认为它通过防止蛋白质不可逆变性,在卤虫的卵生发育胚胎中建立应激抗性,但它也可能通过抑制细胞凋亡来促进存活。为了验证这种可能性,我们构建了稳定转染产生p26的哺乳动物细胞,并测定了它们抵抗凋亡诱导的能力。通过共聚焦显微镜检查免疫荧光染色的转染293H细胞发现,p26在细胞质中呈弥漫性分布,少量蛋白存在于细胞核中。蛋白质印迹免疫检测显示,p26约占可溶性细胞蛋白的0.6%。在长时间培养过程中,p26的定位和数量没有变化,并且该蛋白对转染细胞没有明显的不良影响。在琼脂糖6B中进行分子筛层析显示,p26形成了约20个单体的寡聚体,还有一部分以更大的聚集体形式存在。在蔗糖梯度中也观察到了类似的模式,但总体寡聚体尺寸较小。含有p26的哺乳动物细胞比仅转染表达载体的细胞具有更高的耐热性,并且通过膜联蛋白V标记、Hoechst 33342核染色和前半胱天冬酶-3激活检测发现,转染细胞能有效抵抗热和星形孢菌素诱导的细胞凋亡。赋予耐热性和限制热诱导凋亡的能力很重要,因为卤虫胚胎在其自然栖息地经常暴露于高温环境。在干燥和复水过程中,p26也能阻止转染细胞的凋亡,这些发现与卤虫的生活史特征直接相关,因为干燥会终止卵囊滞育。因此,除了作为分子伴侣发挥作用外,p26还能抑制细胞凋亡,这是其他小热休克蛋白共有的活性,并且可能在卤虫胚胎发育过程中发挥重要作用。