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dc.contributor.authorSlade, Peter G.
dc.contributor.authorWilliams, Michelle V.
dc.contributor.authorBrahmbhatt, Viral
dc.contributor.authorWishnok, John S.
dc.contributor.authorWishnok, John S.
dc.contributor.authorDash, Ajit
dc.contributor.authorTannenbaum, Steven Robert
dc.date.accessioned2011-11-02T20:21:05Z
dc.date.available2011-11-02T20:21:05Z
dc.date.issued2010-02
dc.date.submitted2009-08
dc.identifier.issn0893-228X
dc.identifier.issn1520-5010
dc.identifier.urihttp://hdl.handle.net/1721.1/66897
dc.description.abstractThe hydroperoxide of linoleic acid (13-HPODE) degrades to 9,12-dioxo-10(E)-dodecenoic acid (DODE), which readily modifies proteins. This study identified the major proteins in MCF7 cells modified by DODE. To reduce false positives, three methods were used to identify DODE-modified proteins. First, cells were treated with a synthetically biotinylated 13-HPODE (13-HPODE-biotin). Modified proteins were enriched by neutravidin affinity and identified by two-dimensional liquid chromatography−tandem mass spectrometry (2D LC-MS/MS). Second, cells were treated with native 13-HPODE. Protein carbonyls were biotinylated with an aldehyde reactive probe, and modified proteins were enriched by neutravidin affinity and identified by 2D LC-MS/MS. Third, using a newly developed DODE antibody, DODE-modified proteins were located by 2D sodium dodecyl sulfate−polyacrylamide gel electrophoresis and Western blot and identified by in-gel digestion and LC-MS/MS. Analysis of the proteins characterized by all three methods revealed a significant overlap and identified 32 primary proteins modified by DODE in MCF7 cells. These results demonstrated the feasibility for the cellular formation of DODE protein−carbonyl adducts that may be future indicators of oxidative stress.en_US
dc.description.sponsorshipHarvard University--MIT Division of Health Sciences and Technologyen_US
dc.description.sponsorshipUnited States. National Institutes of Health (NCI Program Project Grant CA26731)en_US
dc.description.sponsorshipNational Institute of Environmental Health Sciences (Grant P30 ES002109)en_US
dc.language.isoen_US
dc.publisherAmerican Chemical Societyen_US
dc.relation.isversionofhttp://dx.doi.org/10.1021/tx9002808en_US
dc.rightsCreative Commons Attribution-Noncommercial-Share Alike 3.0en_US
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/3.0/en_US
dc.sourcePubMed Centralen_US
dc.titleProteins Modified by the Lipid Peroxidation Aldehyde 9,12-Dioxo-10(E)-dodecenoic Acid in MCF7 Breast Cancer Cellsen_US
dc.typeArticleen_US
dc.identifier.citationSlade, Peter G. et al. “Proteins Modified by the Lipid Peroxidation Aldehyde 9,12-Dioxo-10(E)-dodecenoic Acid in MCF7 Breast Cancer Cells.” Chemical Research in Toxicology 23 (2010): 557-567. Web. 2 Nov. 2011.en_US
dc.contributor.departmentMassachusetts Institute of Technology. Department of Biological Engineeringen_US
dc.contributor.departmentMassachusetts Institute of Technology. Department of Chemistryen_US
dc.contributor.approverTannenbaum, Steven R.
dc.contributor.mitauthorSlade, Peter G.
dc.contributor.mitauthorWilliams, Michelle V.
dc.contributor.mitauthorBrahmbhatt, Viral
dc.contributor.mitauthorWishnok, John S.
dc.contributor.mitauthorWishnok, John S.
dc.contributor.mitauthorDash, Ajit
dc.contributor.mitauthorTannenbaum, Steven Robert
dc.relation.journalChemical Research in Toxicologyen_US
dc.eprint.versionAuthor's final manuscripten_US
dc.type.urihttp://purl.org/eprint/type/JournalArticleen_US
eprint.statushttp://purl.org/eprint/status/PeerRevieweden_US
dspace.orderedauthorsSlade, Peter G.; Williams, Michelle V.; Brahmbhatt, Viral; Dash, Ajit; Wishnok, John S.; Tannenbaum, Steven R.en
dc.identifier.orcidhttps://orcid.org/0000-0002-2325-552X
mit.licenseOPEN_ACCESS_POLICYen_US


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