首页 | 本学科首页   官方微博 | 高级检索  
   检索      


Post-translational modifications in MeHg-induced neurotoxicity
Authors:Tao Ke  Filipe Marques Gonçalves  Cinara Ludvig Gonçalves  Alessandra Antunes dos Santos  João BT Rocha  Marcelo Farina  Anatoly Skalny  Aristidis Tsatsakis  Aaron B Bowman  Michael Aschner
Institution:1. Department of Molecular Pharmacology, Albert Einstein College of Medicine, Bronx, NY 10461, United States;2. Departamento de Bioquímica e Biologia Molecular, Centro de Ciências Naturais e Exatas, Universidade Federal de Santa Maria, 97105900 Santa Maria, RS, Brazil;3. Departamento de Bioquímica, Centro de Ciências Biológicas, Universidade Federal de Santa Catarina, 88040900 Florianópolis, SC, Brazil;4. Yaroslavl State University, Sovetskaya St., 14, Yaroslavl 150000, Russia;5. Center of Toxicology Science & Research, Medical School, University of Crete, Heraklion, Crete, Greece;6. School of Health Sciences, Purdue University, West Lafayette, IN, United States;7. Peoples'' Friendship University of Russia (RUDN University), Miklukho-Maklaya St., 6, Moscow 105064, Russia;8. Orenburg State University, Pobedy Ave., 13, Orenburg 460352, Russia
Abstract:Mercury (Hg) exposure remains a major public health concern due to its widespread distribution in the environment. Organic mercurials, such as MeHg, have been extensively investigated especially because of their congenital effects. In this context, studies on the molecular mechanism of MeHg-induced neurotoxicity are pivotal to the understanding of its toxic effects and the development of preventive measures. Post-translational modifications (PTMs) of proteins, such as phosphorylation, ubiquitination, and acetylation are essential for the proper function of proteins and play important roles in the regulation of cellular homeostasis. The rapid and transient nature of many PTMs allows efficient signal transduction in response to stress. This review summarizes the current knowledge of PTMs in MeHg-induced neurotoxicity, including the most commonly PTMs, as well as PTMs induced by oxidative stress and PTMs of antioxidant proteins. Though PTMs represent an important molecular mechanism for maintaining cellular homeostasis and are involved in the neurotoxic effects of MeHg, we are far from understanding the complete picture on their role, and further research is warranted to increase our knowledge of PTMs in MeHg-induced neurotoxicity.
Keywords:Corresponding authors at: 1300 Morris Park Avenue  Forchheimer Building  Room 209  Bronx  NY 10461  United States    Hg  mercury  EtHg  ethylmercury  MeHg  methylmercury  FMD  Fetal Minamata disease  CGC  cerebellar granule cells  ROS  reactive oxygen species  PTMs  post-translational modifications  OXPHOS  oxidative phosphorylation  ETC  electron transport chain  AIF  apoptosis inducing factor  NMDA  AD  Alzheimer's disease  HATs  histone acetylases  HDACs  histone deacetylases  MAPKs  mitogen-activated protein kinases  PKA  protein kinase A  PKC  protein kinase C  ERK1/2  extracellular signal-regulated kinases  JNKs  c?Jun N-terminal kinases  LTP  long term potentiation  cAMP  5′?cyclic?adenosine monophosphate  ACs  adenylyl cyclases  DUBs  deubiquitinases  UCH?L1  ubiquitin carboxy-terminal hydrolase L1  UBE2L3  ubiquitin conjugating enzyme E2L3  BDNF  brain-derived neurotrophic factor  GR  glutathione reductase  GPxs  glutathione peroxidases  SODs  superoxide dismutases  ER  endoplasmic reticulum  ApoE  apolipoprotein E  CGNs  cerebellar granule neurons  hNPCs  human neural progenitor cells  MALDI-TOF/MS  matrix-assisted laser desorption and ionization time-of-flight mass spectrometry  GSH  glutathione  GSTs  GCL  glutamate cysteine ligase  NF-H  high molecular weight neurofilament subunit  TrxR  thioredoxin reductase  ASK?1  apoptosis signaling kinase 1  Nrf2  nuclear factor erythroid 2–related factor 2  Keap1  Kelch-like ECH-associated protein 1  PDI  protein disulfide isomerase  NO  nitrogen monoxide  Post-translational modification  Methylmercury  Neurotoxicity
本文献已被 ScienceDirect 等数据库收录!
设为首页 | 免责声明 | 关于勤云 | 加入收藏

Copyright©北京勤云科技发展有限公司  京ICP备09084417号