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The Scientific World Journal
Volume 2014, Article ID 360153, 7 pages
Research Article

Arsenic Modulates Posttranslational S-Nitrosylation and Translational Proteome in Keratinocytes

1Department of Biomedical Science and Environmental Biology, College of Life Science, Kaohsiung Medical University, Kaohsiung 80708, Taiwan
2Department of Biological Sciences, National Sun Yat-sen University, Kaohsiung 80424, Taiwan
3Department of Biotechnology, College of Life Science, No. 100, Shihchuan 1st Rd., Sanming District, Kaohsiung Medical University, Kaohsiung 80708, Taiwan
4Department of Dermatology, Kaohsiung Medical University Hospital and Kaohsiung Medical University College of Medicine, Kaohsiung 80708, Taiwan
5Department of Anesthesiology, Mackay Memorial Hospital, Taipei 10449, Taiwan
6Departments of Laboratory Medicine, Chang Gung Memorial Hospital-Kaohsiung Medical Center, Kaohsiung 83301, Taiwan

Received 12 June 2014; Accepted 18 June 2014; Published 8 July 2014

Academic Editor: Hsueh-Wei Chang

Copyright © 2014 Bin Huang et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Arsenic is a class I human carcinogen (such as inducing skin cancer) by its prominent chemical interaction with protein thio (-SH) group. Therefore, arsenic may compromise protein S-nitrosylation by competing the -SH binding activity. In the present study, we aimed to understand the influence of arsenic on protein S-nitrosylation and the following proteomic changes. By using primary human skin keratinocyte, we found that arsenic treatment decreased the level of protein S-nitrosylation. This was coincident to the decent expressions of endothelial nitric oxide synthase (eNOS) and inducible nitric oxide synthase (iNOS). By using LC-MS/MS, around twenty S-nitrosoproteins were detected in the biotin-switched eluent. With the interest that arsenic not only regulates posttranslational S-nitrosylation but also separately affects protein’s translation expression, we performed two-dimensional gel electrophoresis and found that 8 proteins were significantly decreased during arsenic treatment. Whether these decreased proteins are the consequence of protein S-nitrosylation will be further investigated. Taken together, these results provide a finding that arsenic can deplete the binding activity of NO and therefore reduce protein S-nitrosylation.