dc.contributor.author | Slade, Peter G. | |
dc.contributor.author | Williams, Michelle V. | |
dc.contributor.author | Brahmbhatt, Viral | |
dc.contributor.author | Wishnok, John S. | |
dc.contributor.author | Wishnok, John S. | |
dc.contributor.author | Dash, Ajit | |
dc.contributor.author | Tannenbaum, Steven Robert | |
dc.date.accessioned | 2011-11-02T20:21:05Z | |
dc.date.available | 2011-11-02T20:21:05Z | |
dc.date.issued | 2010-02 | |
dc.date.submitted | 2009-08 | |
dc.identifier.issn | 0893-228X | |
dc.identifier.issn | 1520-5010 | |
dc.identifier.uri | http://hdl.handle.net/1721.1/66897 | |
dc.description.abstract | The 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.sponsorship | Harvard University--MIT Division of Health Sciences and Technology | en_US |
dc.description.sponsorship | United States. National Institutes of Health (NCI Program Project Grant CA26731) | en_US |
dc.description.sponsorship | National Institute of Environmental Health Sciences (Grant P30 ES002109) | en_US |
dc.language.iso | en_US | |
dc.publisher | American Chemical Society | en_US |
dc.relation.isversionof | http://dx.doi.org/10.1021/tx9002808 | en_US |
dc.rights | Creative Commons Attribution-Noncommercial-Share Alike 3.0 | en_US |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-sa/3.0/ | en_US |
dc.source | PubMed Central | en_US |
dc.title | Proteins Modified by the Lipid Peroxidation Aldehyde 9,12-Dioxo-10(E)-dodecenoic Acid in MCF7 Breast Cancer Cells | en_US |
dc.type | Article | en_US |
dc.identifier.citation | Slade, 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.department | Massachusetts Institute of Technology. Department of Biological Engineering | en_US |
dc.contributor.department | Massachusetts Institute of Technology. Department of Chemistry | en_US |
dc.contributor.approver | Tannenbaum, Steven R. | |
dc.contributor.mitauthor | Slade, Peter G. | |
dc.contributor.mitauthor | Williams, Michelle V. | |
dc.contributor.mitauthor | Brahmbhatt, Viral | |
dc.contributor.mitauthor | Wishnok, John S. | |
dc.contributor.mitauthor | Wishnok, John S. | |
dc.contributor.mitauthor | Dash, Ajit | |
dc.contributor.mitauthor | Tannenbaum, Steven Robert | |
dc.relation.journal | Chemical Research in Toxicology | en_US |
dc.eprint.version | Author's final manuscript | en_US |
dc.type.uri | http://purl.org/eprint/type/JournalArticle | en_US |
eprint.status | http://purl.org/eprint/status/PeerReviewed | en_US |
dspace.orderedauthors | Slade, Peter G.; Williams, Michelle V.; Brahmbhatt, Viral; Dash, Ajit; Wishnok, John S.; Tannenbaum, Steven R. | en |
dc.identifier.orcid | https://orcid.org/0000-0002-2325-552X | |
mit.license | OPEN_ACCESS_POLICY | en_US |
mit.metadata.status | Complete | |