| Direct binding of sulfur mustard and chloroethyl ethyl sulphide to human cell membrane-associated proteins; implications for sulfur mustard pathology. | |
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MedLine Citation:
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PMID: 20004628 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Sulfur mustard (SM) is a potent vesicating agent that produces debilitating blisters and ulcerating lesions on the skin which are characteristically slow to heal. There are currently no specific medical countermeasures to prevent SM-induced vesication and therefore SM remains a major military threat. To investigate the mechanism by which SM causes these injuries we aimed to identify the cellular proteins that are important in the vesicant response and pathology of SM. Membrane and membrane-associated proteins that are targets for direct binding by SM were compared to targets directly bound by CEES (chloroethylethylsulphide). As CEES is a less potent blistering agent compared to SM, it was hypothesised that differences in the binding of these two mustards could reveal key proteins directly involved in the mustard vesicant response. Human cellular membranes fractionated from HaCaT cells were exposed to (14)C-SM or (14)C-CEES and the membrane proteins to which SM or CEES bound were separated by 2D gel electrophoresis, located by fluorography and subsequently identified using mass spectrometry. A number of proteins were identified that were differentially labelled by SM and CEES. Actin, annexin A2 and keratin 9 were labelled with SM at a higher intensity than was seen with the same concentration of CEES. Therefore results from these studies suggest that SM binding to these proteins could contribute to the complex pathology seen following SM exposure. |
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Authors:
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N M Sayer; R Whiting; A C Green; K Anderson; J Jenner; C D Lindsay |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2009-11-18 |
Journal Detail:
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Title: Journal of chromatography. B, Analytical technologies in the biomedical and life sciences Volume: 878 ISSN: 1873-376X ISO Abbreviation: J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. Publication Date: 2010 May |
Date Detail:
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Created Date: 2010-04-27 Completed Date: 2010-08-10 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 101139554 Medline TA: J Chromatogr B Analyt Technol Biomed Life Sci Country: Netherlands |
Other Details:
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Languages: eng Pagination: 1426-32 Citation Subset: IM |
Copyright Information:
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Crown Copyright (c) 2009. Published by Elsevier B.V. All rights reserved. |
Affiliation:
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Biomedical Sciences, Defence Science and Technology Laboratory, Salisbury, Wiltshire SP4 OJQ, United Kingdom. nsayer@dstl.gov.uk |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Actins
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chemistry,
metabolism* Annexin A2 / chemistry, metabolism Carbon Isotopes / chemistry, metabolism Cell Fractionation Cell Line, Transformed Chemical Warfare Agents / chemistry, metabolism Electrophoresis, Gel, Two-Dimensional Humans Membrane Proteins / chemistry, metabolism* Mustard Gas / analogs & derivatives*, chemistry, metabolism* Peptide Fragments / chemistry, metabolism Peptide Mapping / methods* Protein Binding |
| Chemical | |
Reg. No./Substance:
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0/ANXA2 protein, human; 0/Actins; 0/Annexin A2; 0/Carbon Isotopes; 0/Chemical Warfare Agents; 0/Membrane Proteins; 0/Peptide Fragments; 505-60-2/Mustard Gas; 693-07-2/2-chloroethyl ethyl sulfide |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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