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Mass Spectrometric Analyses of Organophosphate Insecticide Oxon Protein Adducts
OBJECTIVE: Organophosphate (OP) insecticides continue to be used to control insect pests. Acute and chronic exposures to OP insecticides have been documented to cause adverse health effects, but few OP-adducted proteins have been correlated with these illnesses at the molecular level. Our aim was to...
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Formato: | Texto |
Lenguaje: | English |
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National Institute of Environmental Health Sciences
2010
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2831953/ https://www.ncbi.nlm.nih.gov/pubmed/20056576 http://dx.doi.org/10.1289/ehp.0900824 |
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author | Thompson, Charles M. Prins, John M. George, Kathleen M. |
author_facet | Thompson, Charles M. Prins, John M. George, Kathleen M. |
author_sort | Thompson, Charles M. |
collection | PubMed |
description | OBJECTIVE: Organophosphate (OP) insecticides continue to be used to control insect pests. Acute and chronic exposures to OP insecticides have been documented to cause adverse health effects, but few OP-adducted proteins have been correlated with these illnesses at the molecular level. Our aim was to review the literature covering the current state of the art in mass spectrometry (MS) used to identify OP protein biomarkers. DATA SOURCES AND EXTRACTION: We identified general and specific research reports related to OP insecticides, OP toxicity, OP structure, and protein MS by searching PubMed and Chemical Abstracts for articles published before December 2008. DATA SYNTHESIS: A number of OP-based insecticides share common structural elements that result in predictable OP–protein adducts. The resultant OP–protein adducts show an increase in molecular mass that can be identified by MS and correlated with the OP agent. Customized OP-containing probes have also been used to tag and identify protein targets that can be identified by MS. CONCLUSIONS: MS is a useful and emerging tool for the identification of proteins that are modified by activated organophosphate insecticides. MS can characterize the structure of the OP adduct and also the specific amino acid residue that forms the key bond with the OP. Each protein that is modified in a unique way by an OP represents a unique molecular biomarker that with further research can lead to new correlations with exposure. |
format | Text |
id | pubmed-2831953 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | National Institute of Environmental Health Sciences |
record_format | MEDLINE/PubMed |
spelling | pubmed-28319532010-03-16 Mass Spectrometric Analyses of Organophosphate Insecticide Oxon Protein Adducts Thompson, Charles M. Prins, John M. George, Kathleen M. Environ Health Perspect Review OBJECTIVE: Organophosphate (OP) insecticides continue to be used to control insect pests. Acute and chronic exposures to OP insecticides have been documented to cause adverse health effects, but few OP-adducted proteins have been correlated with these illnesses at the molecular level. Our aim was to review the literature covering the current state of the art in mass spectrometry (MS) used to identify OP protein biomarkers. DATA SOURCES AND EXTRACTION: We identified general and specific research reports related to OP insecticides, OP toxicity, OP structure, and protein MS by searching PubMed and Chemical Abstracts for articles published before December 2008. DATA SYNTHESIS: A number of OP-based insecticides share common structural elements that result in predictable OP–protein adducts. The resultant OP–protein adducts show an increase in molecular mass that can be identified by MS and correlated with the OP agent. Customized OP-containing probes have also been used to tag and identify protein targets that can be identified by MS. CONCLUSIONS: MS is a useful and emerging tool for the identification of proteins that are modified by activated organophosphate insecticides. MS can characterize the structure of the OP adduct and also the specific amino acid residue that forms the key bond with the OP. Each protein that is modified in a unique way by an OP represents a unique molecular biomarker that with further research can lead to new correlations with exposure. National Institute of Environmental Health Sciences 2010-01 2009-07-29 /pmc/articles/PMC2831953/ /pubmed/20056576 http://dx.doi.org/10.1289/ehp.0900824 Text en http://creativecommons.org/publicdomain/mark/1.0/ Publication of EHP lies in the public domain and is therefore without copyright. All text from EHP may be reprinted freely. Use of materials published in EHP should be acknowledged (for example, ?Reproduced with permission from Environmental Health Perspectives?); pertinent reference information should be provided for the article from which the material was reproduced. Articles from EHP, especially the News section, may contain photographs or illustrations copyrighted by other commercial organizations or individuals that may not be used without obtaining prior approval from the holder of the copyright. |
spellingShingle | Review Thompson, Charles M. Prins, John M. George, Kathleen M. Mass Spectrometric Analyses of Organophosphate Insecticide Oxon Protein Adducts |
title | Mass Spectrometric Analyses of Organophosphate Insecticide Oxon Protein Adducts |
title_full | Mass Spectrometric Analyses of Organophosphate Insecticide Oxon Protein Adducts |
title_fullStr | Mass Spectrometric Analyses of Organophosphate Insecticide Oxon Protein Adducts |
title_full_unstemmed | Mass Spectrometric Analyses of Organophosphate Insecticide Oxon Protein Adducts |
title_short | Mass Spectrometric Analyses of Organophosphate Insecticide Oxon Protein Adducts |
title_sort | mass spectrometric analyses of organophosphate insecticide oxon protein adducts |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2831953/ https://www.ncbi.nlm.nih.gov/pubmed/20056576 http://dx.doi.org/10.1289/ehp.0900824 |
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