Tomanek Lars
California Polytechnic State University, Department of Biological Sciences, Center for Coastal Marine Studies, Environmental Proteomics Laboratory, 1 Grand Ave., San Luis Obispo, CA 93407-0401, USA
J Exp Biol. 2015 Jun;218(Pt 12):1867-79. doi: 10.1242/jeb.116475.
Environmental (acute and chronic temperature, osmotic, hypoxic and pH) stress challenges the cellular redox balance and can lead to the increased production of reactive oxygen species (ROS). This review provides an overview of the reactions producing and scavenging ROS in the mitochondria, endoplasmic reticulum (ER) and peroxisome. It then compares these reactions with the findings of a number of studies investigating the proteomic responses of marine organisms to environmentally induced oxidative stress. These responses indicate that the thioredoxin-peroxiredoxin system is possibly more frequently recruited to scavenge H2O2 than the glutathione system. Isoforms of superoxide dismutase (SOD) are not ubiquitously induced in parallel, suggesting that SOD scavenging activity is sometimes sufficient. The glutathione system plays an important role in some organisms and probably also contributes to protecting protein thiols during environmental stress. Synthesis pathways of cysteine and selenocysteine, building blocks for glutathione and glutathione peroxidase, also play an important role in scavenging ROS during stress. The increased abundance of glutaredoxin and DyP-type peroxidase suggests a need for regulating the deglutathionylation of proteins and scavenging of peroxynitrite. Reducing equivalents for these scavenging reactions are generated by proteins of the pentose phosphate pathway and by NADP-dependent isocitrate dehydrogenase. Furthermore, proteins representing reactions of the tricarboxylic acid cycle and the electron transport system generating NADH and ROS, including those of complex I, II and III, are frequently reduced in abundance with stress. Protein maturation in the ER likely represents another source of ROS during environmental stress, as indicated by simultaneous changes in ER chaperones and antioxidant proteins. Although there are still too few proteomic analyses of non-model organisms exposed to environmental stress for a general pattern to emerge, hyposaline and low pH stress show different responses from temperature and hypoxic stress. Furthermore, comparisons of closely related congeners differing in stress tolerance start to provide insights into biochemical processes contributing to adaptive differences, but more of these comparisons are needed to draw general conclusions. To fully take advantage of a systems approach, studies with longer time courses, including several tissues and more species comparisons are needed.
环境(急性和慢性温度、渗透压、缺氧和pH值)应激会挑战细胞的氧化还原平衡,并可能导致活性氧(ROS)生成增加。本综述概述了线粒体、内质网(ER)和过氧化物酶体中产生和清除ROS的反应。然后将这些反应与一些研究的结果进行比较,这些研究调查了海洋生物对环境诱导的氧化应激的蛋白质组学反应。这些反应表明,与谷胱甘肽系统相比,硫氧还蛋白-过氧化物酶系统可能更频繁地被用于清除H2O2。超氧化物歧化酶(SOD)的同工型并非总是同时被诱导,这表明SOD的清除活性有时就足够了。谷胱甘肽系统在一些生物中起重要作用,并且可能在环境应激期间也有助于保护蛋白质硫醇。半胱氨酸和硒代半胱氨酸的合成途径是谷胱甘肽和谷胱甘肽过氧化物酶的组成部分,在应激期间清除ROS方面也起重要作用。谷氧还蛋白和DyP型过氧化物酶丰度的增加表明需要调节蛋白质的去谷胱甘肽化和清除过氧亚硝酸盐。这些清除反应的还原当量由磷酸戊糖途径的蛋白质和NADP依赖性异柠檬酸脱氢酶产生。此外,代表三羧酸循环和电子传递系统反应产生NADH和ROS(包括复合体I、II和III的反应)的蛋白质,其丰度在应激时经常降低。内质网中的蛋白质成熟可能是环境应激期间ROS的另一个来源,内质网伴侣蛋白和抗氧化蛋白的同时变化表明了这一点。尽管对于非模式生物暴露于环境应激的蛋白质组学分析仍然太少,尚未形成普遍模式,但低盐度和低pH值应激显示出与温度和缺氧应激不同的反应。此外,对胁迫耐受性不同的近缘同属生物进行比较,开始为有助于适应性差异的生化过程提供见解,但需要更多这样的比较才能得出一般性结论。为了充分利用系统方法,需要进行更长时间的研究,包括多个组织和更多物种比较。