S-Mercuration of cellular proteins by methylmercury and its toxicological implications

• Kanda Hironori

  Doctoral Program in Biomedical Sciences, Graduate School of Comprehensive Human Sciences, University of Tsukuba

• Shinkai Yasuhiro

  Environmental Biology Laboratory, Faculty of Medicine, University of Tsukuba

• Kumagai Yoshito

  Environmental Biology Laboratory, Faculty of Medicine, University of Tsukuba

書誌事項

タイトル別名

• <i>S</i>-Mercuration of cellular proteins by methylmercury and its toxicological implications

抄録

The accumulation of methylmercury (MeHg) through the daily consumption of large predatory fish poses potential health risks. MeHg has been found to cause Minamata disease, but the full nature of MeHg toxicity remains unclear. Because of its chemical properties, MeHg covalently binds to cellular proteins through their reactive thiols, referred to as S-mercuration, resulting in the formation of protein adducts. In this review, we summarize how the S-mercuration of cellular proteins could be involved in the major mechanisms that have been suggested to underlie MeHg toxicity. Additionally, we introduce our attempts to identify cases of S-mercuration for the research to reveal the true nature of MeHg toxicity.

収録刊行物

• Ｔｈｅ　Ｊｏｕｒｎａｌ　ｏｆ　Ｔｏｘｉｃｏｌｏｇｉｃａｌ　Ｓｃｉｅｎｃｅｓ

  Ｔｈｅ　Ｊｏｕｒｎａｌ　ｏｆ　Ｔｏｘｉｃｏｌｏｇｉｃａｌ　Ｓｃｉｅｎｃｅｓ 39 (5), 687-700, 2014

  一般社団法人　日本毒性学会

キーワード

• Methylmercury
• Cysteine
• Thiol
• Covalent binding
• Protein

詳細情報

• CRID: 1390001204905792128
• NII論文ID: 130004690955
• NII書誌ID: AN00002808
• DOI: 10.2131/jts.39.687
• COI: 1:STN:280:DC%2BC2M7jsFOitA%3D%3D
• ISSN: 18803989
• ISSN: 03881350
• NDL書誌ID: 025850759
• PubMed: 25242398
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I025850759
• Web Site: https://www.jstage.jst.go.jp/article/jts/39/5/39_687/_pdf
• Web Site: https://search.jamas.or.jp/link/ui/2015134679
• 本文言語コード: en
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