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Arsenic Modulates Posttranslational S-Nitrosylation and Translational Proteome in Keratinocytes

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 ars...

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Autores principales: Huang, Bin, Chiang, Kuo-Hao, Yu, Hsin-Su, Chen, Ying-Lun, You, Huey-Ling, Liao, Wei-Ting
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4119667/
https://www.ncbi.nlm.nih.gov/pubmed/25110733
http://dx.doi.org/10.1155/2014/360153
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author Huang, Bin
Chiang, Kuo-Hao
Yu, Hsin-Su
Chen, Ying-Lun
You, Huey-Ling
Liao, Wei-Ting
author_facet Huang, Bin
Chiang, Kuo-Hao
Yu, Hsin-Su
Chen, Ying-Lun
You, Huey-Ling
Liao, Wei-Ting
author_sort Huang, Bin
collection PubMed
description 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.
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spelling pubmed-41196672014-08-10 Arsenic Modulates Posttranslational S-Nitrosylation and Translational Proteome in Keratinocytes Huang, Bin Chiang, Kuo-Hao Yu, Hsin-Su Chen, Ying-Lun You, Huey-Ling Liao, Wei-Ting ScientificWorldJournal Research Article 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. Hindawi Publishing Corporation 2014 2014-07-08 /pmc/articles/PMC4119667/ /pubmed/25110733 http://dx.doi.org/10.1155/2014/360153 Text en Copyright © 2014 Bin Huang et al. https://creativecommons.org/licenses/by/3.0/ 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.
spellingShingle Research Article
Huang, Bin
Chiang, Kuo-Hao
Yu, Hsin-Su
Chen, Ying-Lun
You, Huey-Ling
Liao, Wei-Ting
Arsenic Modulates Posttranslational S-Nitrosylation and Translational Proteome in Keratinocytes
title Arsenic Modulates Posttranslational S-Nitrosylation and Translational Proteome in Keratinocytes
title_full Arsenic Modulates Posttranslational S-Nitrosylation and Translational Proteome in Keratinocytes
title_fullStr Arsenic Modulates Posttranslational S-Nitrosylation and Translational Proteome in Keratinocytes
title_full_unstemmed Arsenic Modulates Posttranslational S-Nitrosylation and Translational Proteome in Keratinocytes
title_short Arsenic Modulates Posttranslational S-Nitrosylation and Translational Proteome in Keratinocytes
title_sort arsenic modulates posttranslational s-nitrosylation and translational proteome in keratinocytes
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4119667/
https://www.ncbi.nlm.nih.gov/pubmed/25110733
http://dx.doi.org/10.1155/2014/360153
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