Marine Biotechnology

, Volume 12, Issue 3, pp 273–281 | Cite as

Proteomic Profiling of Liver from Atlantic Salmon (Salmo salar) Fed Genetically Modified Soy Compared to the Near-Isogenic non-GM Line

  • Nini H. SissenerEmail author
  • Samuel A. M. Martin
  • Phillip Cash
  • Ernst M. Hevrøy
  • Monica Sanden
  • Gro-Ingunn Hemre
original Article


The aim of this study was to investigate potential differences in liver protein expression of Atlantic salmon fed genetically modified (GM) Roundup Ready® soy at a high inclusion level (25% inclusion, constituting 21% of crude protein in the diet) for 7 months or a compositionally similar non-GM diet. The liver was selected as the target organ due to its importance in the general metabolism, and 2D gel electrophoresis used as a screening tool. Samples from 12 individual fish from each diet group were evaluated. Of a total of 781 analysed protein spots, only 36 were significantly different by ANOVA (p < 0.05) in abundance between the diet groups. All these spots had low fold differences (1.2–1.6) and high false discovery rate (q = 0.44), indicating minor differences in liver protein synthesis between fish fed GM and non-GM soy. Additionally, low fold differences were observed. Four protein spots were analyzed by liquid chromatography tandem mass spectrometry and identified using a combination of online searches in NCBI and searches in an inhouse database containing salmonid expressed sequence tags and contigs. Follow-up on these proteins by real-time polymerase chain reaction did not identify differences at the transcriptional level.


Atlantic salmon Biotechnology Genetic modification Liver Roundup Ready® soybean 



We would like to thank the Monsanto Company (St. Louis, MO, USA) for supplying the RRS® as well as the near-isogenic maternal soybeans. We would also like to thank Ivar Helge Matre for technical assistance and Lise Dyrhovden for care of the fish during the feeding trial. Further, many thanks to Evelyn Argo and Elizabeth C. Stewart at the Aberdeen Proteome Facility for much appreciated help with the gels and protein identifications, respectively. The project was supported by the Norwegian Research Council, grant no. 172151. Work carried out at Aberdeen Proteome Facility is supported in part by a grant from the BBSRC.

Supplementary material

10126_2009_9214_MOESM1_ESM.doc (68 kb)
Table 1 Protein identifications; matching peptides obtained when searching the NCBI and the EST/contig databases, respectively. When several matches are made to the same amino acid sequence, only the one with the highest ion score is given in the table. O@M oxidation of methionine. (DOC 67 kb)


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Copyright information

© Springer Science+Business Media, LLC 2009

Authors and Affiliations

  • Nini H. Sissener
    • 1
    Email author
  • Samuel A. M. Martin
    • 2
  • Phillip Cash
    • 3
  • Ernst M. Hevrøy
    • 1
  • Monica Sanden
    • 1
  • Gro-Ingunn Hemre
    • 1
  1. 1.National Institute of Seafood and Nutrition Research (NIFES)BergenNorway
  2. 2.School of Biological SciencesUniversity of AberdeenAberdeenUK
  3. 3.Division of Applied Medicine, School of Medical SciencesUniversity of AberdeenAberdeenUK

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