沙蜥的辐射防护蛋白dsup(损伤抑制因子)可抵抗高剂量的电离辐射

M. Zarubin, A.F. Nizamieva, S.I. Alexeev, S. Mitrofanov, Y.E. Gorshkova, E.V. Kravchenko
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引用次数: 0

摘要

在不同种类的生物和人类细胞培养过程中,沙蜥特有的Dsup蛋白能增强对辐射和氧化应激的抵抗力。然而,Dsup 蛋白本身在电离辐射作用下的稳定性仍不清楚,这对于评估其辐射防护潜力和了解该蛋白在高剂量辐射条件下的分子作用机制非常重要。本研究首次通过小角 X 射线散射(SAXS)和变性条件下的聚丙烯酰胺凝胶蛋白质电泳(SDS-PAGE)研究了 Dsup 蛋白在γ 射线辐照后的辐射降解情况,结果表明,与对照组牛血清白蛋白相比,Dsup 蛋白的空间和结构特征即使在高剂量辐射(5 kGy 和 10 kGy)下也几乎保持不变,这表明其具有很高的辐射稳定性。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
RADIOPROTECTIVE PROTEIN OF TARDIGRADE DSUP (DAMAGE SUPPRESSOR) IS RESISTANT TO HIGH DOSES OF IONIZING RADIATION
The unique Dsup protein of the tardigrade Ramazzottiusvarieornatus increases resistance to radiation and oxidative stress in various species of organisms and in human cell culture. According to modeling data,Dsup forms a complex with DNA with an intermolecular distance of ∼4˚A, as a result of which DNA is lessdamaged by reactive oxygen species formed during exposure to radiation.However, the stability of the Dsupprotein itself under the in uence of ionizing radiation remains unclear, which is important for assessing its radioprotective potential and understanding the molecular mechanisms of the action of this protein under conditions of high doses of radiation. In this work, the radiation degradation of the Dsup protein after γ-ray irradiation by small-angle X-ray scattering (SAXS) and protein electrophoresis in polyacrylamide gel under denaturing conditions (SDS-PAGE) was studied for the rst time.It has been shown that, in contrast to the control bovine serum albumin, the spatial and structural characteristics of the Dsup protein remain almost unchanged even when exposed to high doses of radiation (5 and 10 kGy), which suggests its high radiation stability.
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