Chemical proteomic analysis of the potential toxicological mechanisms of microcystin-RR in zebrafish (Danio rerio) liver
文献类型:期刊论文
作者 | Tuo, Xun1,2,3; Chen, Jun1; Zhao, Sujuan1,3; Xie, Ping1 |
刊名 | ENVIRONMENTAL TOXICOLOGY
![]() |
出版日期 | 2016-10-01 |
卷号 | 31期号:10页码:1206-1216 |
关键词 | microcystin-RR chemical proteomics toxicological mechanisms zebrafish liver |
ISSN号 | 1520-4081 |
DOI | 10.1002/tox.22128 |
通讯作者 | Xie, Ping(xieping@ihb.ac.cn) |
英文摘要 | Microcystins (MCs) are common toxins produced by freshwater cyanobacteria, and they represent a potential health risk to aquatic organisms and animals, including humans. Specific inhibition of protein phosphatases 1 and 2A is considered the typical mechanism of MCs toxicity, but the exact mechanism has not been fully elucidated. To further our understanding of the toxicological mechanisms induced by MCs, this study is the first to use a chemical proteomic approach to screen proteins that exhibit special interactions with MC-arginine-arginine (MC-RR) from zebrafish (Danio rerio) liver. Seventeen proteins were identified via affinity blocking test. Integration of the results of previous studies and this study revealed that these proteins play a crucial role in various toxic phenomena of liver induced by MCs, such as the disruption of cytoskeleton assembly, oxidative stress, and metabolic disorder. Moreover, in addition to inhibition of protein phosphate activity, the overall toxicity of MCs was simultaneously modulated by the distribution of MCs in cells and their interactions with other target proteins. These results provide new insight into the mechanisms of hepatotoxicity induced by MCs. (c) 2015 Wiley Periodicals, Inc. Environ Toxicol 31: 1206-1216, 2016. |
WOS关键词 | TANDEM MASS-SPECTROMETRY ; AFFINITY-CHROMATOGRAPHY ; RAT HEPATOCYTES ; INTERMEDIATE-FILAMENTS ; PROTEIN PHOSPHATASES ; PROTEOLYTIC-ENZYMES ; CELLULAR-RESPONSES ; SERINE PROTEASES ; MOUSE-LIVER ; FISH LIVER |
资助项目 | National Natural Science Foundation of China[31322013] ; National Natural Science Foundation of China[31070457] |
WOS研究方向 | Environmental Sciences & Ecology ; Toxicology ; Water Resources |
语种 | 英语 |
WOS记录号 | WOS:000383611900005 |
出版者 | WILEY-BLACKWELL |
资助机构 | National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Natural Science Foundation of China |
源URL | [http://ir.ihb.ac.cn/handle/342005/34137] ![]() |
专题 | 水生生物研究所_水环境工程研究中心_期刊论文 |
通讯作者 | Xie, Ping |
作者单位 | 1.Chinese Acad Sci, Inst Hydrobiol, State Key Lab Freshwater Ecol & Biotechnol, Donghu Expt Stn Lake Ecosyst, Donghu South Rd 7, Wuhan 430072, Peoples R China 2.Nanchang Univ, Basic Chem Expt Ctr, Nanchang 330031, Jiangxi, Peoples R China 3.Univ Chinese Acad Sci, Beijing 100049, Peoples R China |
推荐引用方式 GB/T 7714 | Tuo, Xun,Chen, Jun,Zhao, Sujuan,et al. Chemical proteomic analysis of the potential toxicological mechanisms of microcystin-RR in zebrafish (Danio rerio) liver[J]. ENVIRONMENTAL TOXICOLOGY,2016,31(10):1206-1216. |
APA | Tuo, Xun,Chen, Jun,Zhao, Sujuan,&Xie, Ping.(2016).Chemical proteomic analysis of the potential toxicological mechanisms of microcystin-RR in zebrafish (Danio rerio) liver.ENVIRONMENTAL TOXICOLOGY,31(10),1206-1216. |
MLA | Tuo, Xun,et al."Chemical proteomic analysis of the potential toxicological mechanisms of microcystin-RR in zebrafish (Danio rerio) liver".ENVIRONMENTAL TOXICOLOGY 31.10(2016):1206-1216. |
入库方式: OAI收割
来源:水生生物研究所
浏览0
下载0
收藏0
其他版本
除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。