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Protein-Binding Patterns Drive the Transport of Mercury in Plasma and Red Blood Cells in Rats

文献类型： 外文期刊

作者： Yuan, Min 1 ; Li, Yiling 1 ; Liu, Yingqiu 1 ; Tian, Haozhong 1 ; He, Bin 1 ; Liu, Lihong 1 ; Yin, Yongguang 1 ; Shi, Jianbo 1 ; Hu, Ligang 1 ; Jiang, Guibin 1 ;

作者机构： 1.Chinese Acad Sci, Res Ctr Ecoenvironm Sci, State Key Lab Environm Chem & Ecotoxicol, Beijing 100085, Peoples R China

2.Chinese Acad Fishery Sci, Yellow Sea Fisheries Res Inst, State Key Lab Mariculture Biobreeding & Sustainabl, Qingdao 266071, Peoples R China

3.Univ Chinese Acad Sci, Coll Resources & Environm, Beijing 100049, Peoples R China

4.Jianghan Univ, Sch Environm & Hlth, Wuhan 430056, Peoples R China

5.Univ Chinese Acad Sci, Hangzhou Inst Adv Study, Sch Environm, Hangzhou 310000, Peoples R China

关键词： mercury; protein-binding patterns; plasma; red blood cells

期刊名称：ENVIRONMENTAL SCIENCE & TECHNOLOGY （ 影响因子：11.3； 五年影响因子：12.4 ）

ISSN： 0013-936X

年卷期： 2025 年 59 卷 31 期

页码：

收录情况： SCI

摘要： The fate of metals within biological systems is determined by their associated binding partners, specifically protein ligands. However, the mechanisms by which these protein targets regulate the transport of metal pollutants remain unclear. Here, protein-binding patterns were identified as drivers of the transport of mercuric compounds (methylmercury and inorganic mercury) in the bloodstream. We systematically investigated the transport of mercury (Hg) in rats following oral administration and analyzed the time-resolved patterns of Hg-binding proteins in the blood. Our findings demonstrated that Hg was differentially distributed between plasma and red blood cells (RBCs) over time, suggesting distinct transport pathways mediated by specific protein interactions. Methylmercury (MeHg) preferentially bound to hemoglobin and carbonic anhydrase in RBCs, together accounting for more than 97% of protein-bound MeHg. This selective binding retained MeHg within the RBCs and significantly prolonged its circulation time. In contrast, inorganic mercury (HgCl2) displayed a broader and more diverse protein-binding pattern. In RBCs, it bound primarily to hemoglobin and galectin-5, whereas in plasma, albumin and glutathione peroxidase 3 (Gpx3) were identified as its major binding partners. These protein-binding patterns drive the differential biological fates of mercury. The higher ratio of MeHg to proteins in RBCs resulted in a longer vascular circulation lifetime of MeHg in blood, leading to the prolonged transfer of MeHg from the blood to the brain. Conversely, the higher plasma protein binding of HgCl2 facilitated its partitioning from the blood into tissues such as the kidney and liver, where it could be rapidly cleared and excreted. In summary, Hg-binding proteins play a crucial role in regulating their retention in the blood and their subsequent transfer to tissues.

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