低氧环境下蛋白质糖基化参与免疫反应机制的研究进展

Research progress of mechanism of protein glycosylation in the immune reaction under hypoxia

背景:糖基化作为蛋白质重要的翻译后修饰之一而广泛的存在与生物体内,其合成过程显著受到细胞所处环境的影响。目的:通过对细菌、病毒及肿瘤所形成的低氧微环境下蛋白质糖基化参与免疫反应的研究做一总结,以探讨高原低氧时蛋白质糖基化参与免疫反应的机制,方法:以"proteinglycosylation,immunereaction,hypoxia"为检索词,检索PubMed数据1988年1月至2019年1月与细菌、病毒及肿瘤所致的糖基化对免疫反应影响相关的文献。按照纳入排除标准,对最终选入的61篇文献进行探讨。结果与结论:近年研究发现,低氧可导致机体或细胞的糖基化过程改变,并可导致蛋白的生物学活性发生变化。蛋白的糖基化修饰在病毒的传染、病毒颗粒的形成及其发生免疫逃避的过程中都扮演着重要角色。在肿瘤细胞的进展过程中,由于氧缺乏及糖摄取的增加导致了糖酵解的发生,而血葡萄糖浓度的升高诱发了蛋白非酶催化的糖基化或糖化,并导致了晚期糖基化产物的蓄积。高原环境作为首要的环境因素缺氧是机体发生损伤的基础,可导致一系列疾病的发生,而在此之中是否涉及糖基化的改变还有待进一步证实。

BACKGROUND: As one of the important post-translation modifications, the protein glycosylation inhere in the biosome extensively, and its synthetize process is influenced by the surroundings of the cells. OBJECTIVE: To summarize the study on the protein glycosylation with the immune reaction under hypoxia developed in the bacteria, virus and tumors infecting, so as to discuss the mechanism of the protein glycosylation with the immune reaction in the plateau hypoxia. METHODS: PubMed database between January 1988 and January 2019 was retrieved for relevant articles on the effect of glycosylation induced by bacteria, virus and tumors. The keywords were "protein glycosylation, immune reaction, hypoxia". Finally 61 articles eligible for inclusion and exclusion criteria were included for result analysis. RESULTS AND CONCLUSION: In recent years, hypoxia has been shown to cause the changes of glycosylation in organism or cells, and moreover can change the biologic activity of protein. Protein glycosylation modification plays an important role in the virus infection, virus particle formation and immune escape. Lack of oxygen and increased sugar intake lead to glycolysis in the progress of tumor cells, and elevated blood glucose levels induce non-enzymatic glycosylation or saccharification, further resulting in the accumulation of advanced glycosylation product. Plateau environment of oxygen is the basis of airframe damage, can lead to a series of diseases, and whether glycosylation change is involved needs to be investigated in depth.