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DC Field | Value | Language |
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dc.contributor.author | Muñoz-Torrero López-Ibarra, Diego | - |
dc.contributor.author | Schopfer, Lawrence M. | - |
dc.contributor.author | Lockridge, Oksana | - |
dc.date.accessioned | 2023-02-22T11:55:29Z | - |
dc.date.available | 2023-02-22T11:55:29Z | - |
dc.date.issued | 2023 | - |
dc.identifier.issn | 0893-228X | - |
dc.identifier.uri | http://hdl.handle.net/2445/193966 | - |
dc.description.abstract | Chronic low-dose exposure to organophosphorus (OP) toxicants is correlated with an increase in the risk of impaired cognition and neurodegenerative diseases. A mechanism to explain this relationship is needed. We suggest that the formation of organophosphate-induced high-molecular-weight protein aggregates that disrupt cell function may be the missing link. It has been demonstrated that such aggregation can be promoted by OP-labeled lysine. Alternatively, OP-labeled glutamate may be the initiator. To test this hypothesis, we treated MAP-rich tubulin Sus scrofa and human transglutaminase with chlorpyrifos oxon. Trypsin-digested proteins were subjected to liquid chromatography−tandem mass spectrometry followed by Protein Prospector searches to identify diethyl phosphate adducts and cross-linked peptides. We report the presence of diethyl phosphate adducts on the side chains of glutamate, lysine, and tyrosine, as well as cross-links between glutamate and lysine. Glutamate-lysine cross-linking could be initiated either by diethyl phosphate-activated glutamate or by diethyl phosphate-activated lysine to form stable isopeptide bonds between and within proteins. It was concluded that organophosphate-induced high-molecular-weight protein aggregates could promote brain dysfunction. | - |
dc.format.extent | 10 p. | - |
dc.format.mimetype | application/pdf | - |
dc.language.iso | eng | - |
dc.publisher | American Chemical Society | - |
dc.relation.isformatof | Reproducció del document publicat a: https://doi.org/10.1021/acs.chemrestox.2c00333 | - |
dc.relation.ispartof | Chemical Research in Toxicology, 2023, vol. 36, num. 1, p. 112-121 | - |
dc.relation.uri | https://doi.org/10.1021/acs.chemrestox.2c00333 | - |
dc.rights | cc by-nc-nd (c) Diego Muñoz-Torrero López-Ibarra, et al., 2023 | - |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/3.0/es/ | * |
dc.source | Articles publicats en revistes (Farmacologia, Toxicologia i Química Terapèutica) | - |
dc.subject.classification | Malalties neurodegeneratives | - |
dc.subject.classification | Pèptids | - |
dc.subject.classification | Proteïnes | - |
dc.subject.classification | Àcids nucleics | - |
dc.subject.other | Neurodegenerative Diseases | - |
dc.subject.other | Peptides | - |
dc.subject.other | Proteins | - |
dc.subject.other | Nucleic acids | - |
dc.title | Chlorpyrifos oxon activates glutamate and lysine for protein cross-linking | - |
dc.type | info:eu-repo/semantics/article | - |
dc.type | info:eu-repo/semantics/publishedVersion | - |
dc.identifier.idgrec | 728358 | - |
dc.date.updated | 2023-02-22T11:55:29Z | - |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | - |
Appears in Collections: | Articles publicats en revistes (Farmacologia, Toxicologia i Química Terapèutica) |
Files in This Item:
File | Description | Size | Format | |
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728358.pdf | 4.23 MB | Adobe PDF | View/Open |
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