Jeyachandran Sivakamavalli, Chellapandian Hethesh, Park Kiyun, Kwak Ihn-Sil
Lab in Biotechnology & Biosignal Transduction, Department of Orthodontics, Saveetha Dental College & Hospitals, Saveetha Institute of Medical and Technical Sciences (SIMATS), Saveetha University, Chennai 600077, Tamil Nadu, India.
Fisheries Science Institute, Chonnam National University, Yeosu 59626, Republic of Korea.
Antioxidants (Basel). 2023 Jul 18;12(7):1444. doi: 10.3390/antiox12071444.
Heat shock proteins (HSPs) encompass both extrinsic chaperones and stress proteins. These proteins, with molecular weights ranging from 14 to 120 kDa, are conserved across all living organisms and are expressed in response to stress. The upregulation of specific genes triggers the synthesis of HSPs, facilitated by the interaction between heat shock factors and gene promoter regions. Notably, HSPs function as chaperones or helper molecules in various cellular processes involving lipids and proteins, and their upregulation is not limited to heat-induced stress but also occurs in response to anoxia, acidosis, hypoxia, toxins, ischemia, protein breakdown, and microbial infection. HSPs play a vital role in regulating protein synthesis in cells. They assist in the folding and assembly of other cellular proteins, primarily through HSP families such as HSP70 and HSP90. Additionally, the process of the folding, translocation, and aggregation of proteins is governed by the dynamic partitioning facilitated by HSPs throughout the cell. Beyond their involvement in protein metabolism, HSPs also exert a significant influence on apoptosis, the immune system, and various characteristics of inflammation. The immunity of aquatic organisms, including shrimp, fish, and shellfish, relies heavily on the development of inflammation, as well as non-specific and specific immune responses to viral and bacterial infections. Recent advancements in aquatic research have demonstrated that the HSP levels in populations of fish, shrimp, and shellfish can be increased through non-traumatic means such as water or oral administration of HSP stimulants, exogenous HSPs, and heat induction. These methods have proven useful in reducing physical stress and trauma, while also facilitating sustainable husbandry practices such as vaccination and transportation, thereby offering health benefits. Hence, the present review discusses the importance of HSPs in different tissues in aquatic organisms (fish, shrimp), and their expression levels during pathogen invasion; this gives new insights into the significance of HSPs in invertebrates.
热休克蛋白(HSPs)包括外在伴侣蛋白和应激蛋白。这些蛋白质分子量在14至120 kDa之间,在所有生物中都保守存在,并在应激反应时表达。热休克因子与基因启动子区域之间的相互作用促进了特定基因的上调,从而触发热休克蛋白的合成。值得注意的是,热休克蛋白在涉及脂质和蛋白质的各种细胞过程中作为伴侣蛋白或辅助分子发挥作用,其上调不仅限于热诱导应激,还会在缺氧、酸中毒、低氧、毒素、缺血、蛋白质分解和微生物感染等情况下发生。热休克蛋白在调节细胞内蛋白质合成中起着至关重要的作用。它们主要通过HSP70和HSP90等热休克蛋白家族协助其他细胞蛋白质的折叠和组装。此外,蛋白质的折叠、转运和聚集过程受热休克蛋白在整个细胞中促进的动态分配控制。除了参与蛋白质代谢外,热休克蛋白还对细胞凋亡、免疫系统和炎症的各种特征产生重大影响。包括虾、鱼和贝类在内的水生生物的免疫力很大程度上依赖于炎症的发展以及对病毒和细菌感染的非特异性和特异性免疫反应。水生研究的最新进展表明,通过非创伤性手段,如水或口服热休克蛋白刺激剂、外源性热休克蛋白和热诱导,可以提高鱼、虾和贝类群体中的热休克蛋白水平。这些方法已被证明有助于减轻身体压力和创伤,同时也促进了疫苗接种和运输等可持续养殖实践,从而带来健康益处。因此,本综述讨论了热休克蛋白在水生生物(鱼、虾)不同组织中的重要性,以及它们在病原体入侵期间的表达水平;这为热休克蛋白在无脊椎动物中的重要性提供了新的见解。