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Glyphosate does not substitute for glycine in proteins of actively dividing mammalian cells

Authors
  • Antoniou, Michael N.1
  • Nicolas, Armel2, 3
  • Mesnage, Robin1
  • Biserni, Martina1
  • Rao, Francesco V.2, 4
  • Martin, Cristina Vazquez2
  • 1 King’s College London, Guy’s Hospital, Department of Medical and Molecular Genetics, Faculty of Life Sciences & Medicine, Gene Expression and Therapy Group, 8th Floor, Tower Wing, Great Maze Pond, London, SE1 9RT, UK , London (United Kingdom)
  • 2 DC Biosciences, James Lindsay Place, Dundee, DD1 5JJ, UK , Dundee (United Kingdom)
  • 3 IST Austria Proteomics Service, Lab Building East, Am Campus 1, Klosterneuburg, 3400, Austria , Klosterneuburg (Austria)
  • 4 Platinum Informatics Ltd., Unit 8, The Vision Building, 20 Greenmarket, Dundee, DD1 4QB, UK , Dundee (United Kingdom)
Type
Published Article
Journal
BMC Research Notes
Publisher
Springer (Biomed Central Ltd.)
Publication Date
Aug 08, 2019
Volume
12
Issue
1
Identifiers
DOI: 10.1186/s13104-019-4534-3
Source
Springer Nature
Keywords
License
Green

Abstract

ObjectivesGlyphosate (N-phosphonomethyl glycine) and its commercial herbicide formulations have been shown to exert toxicity via various mechanisms. It has been asserted that glyphosate substitutes for glycine in polypeptide chains leading to protein misfolding and toxicity. However, as no direct evidence exists for glycine to glyphosate substitution in proteins, including in mammalian organisms, we tested this claim by conducting a proteomics analysis of MDA-MB-231 human breast cancer cells grown in the presence of 100 mg/L glyphosate for 6 days. Protein extracts from three treated and three untreated cell cultures were analysed as one TMT-6plex labelled sample, to highlight a specific pattern (+/+/+/−/−/−) of reporter intensities for peptides bearing true glyphosate treatment induced-post translational modifications as well as allowing an investigation of the total proteome.ResultsComparative statistical analysis of global proteome changes between glyphosate treated and non-treated samples did not show significant differences. Crucially, filtering of data to focus analysis on peptides potentially bearing glycine for glyphosate replacement revealed that the TMT reporter intensity pattern of all candidates showed conclusively that they are all false discoveries, with none displaying the expected TMT pattern for such a substitution. Thus, the assertion that glyphosate substitutes for glycine in protein polypeptide chains is incorrect.

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