title: Histological, digestive, metabolic, hormonal and some immune factor responses in Atlantic salmon, Salmo salar L., fed genetically modified soybeans.
abstract: The paper reports the second and final part of an experiment aiming to study physiological and health-related effects of genetically modified (GM) soybean meal (SBM) type Roundup Ready soybean (RRS) in diets for post-smolt Atlantic salmon. For 3 months salmon were fed diets containing 172 g kg(-1) full-fat SBM from RRS (GM-soy) or an unmodified, non-isogenic line (nGM-soy), or a reference diet with fishmeal as the sole protein source (FM). Slight differences in anti-nutrient levels were observed between the GM and nGM-soy. Histological changes were observed only in the distal intestine of the soy-fed fish. The incidence of moderate inflammation was higher in the GM-soy group (9 of 10 sampled fish) compared with the nGM-soy group (7 of 10). However, no differences in the concomitant decreases in activities of digestive enzymes located in the brush border (leucine aminopeptidase and maltase) and apical cytoplasm (acid phosphatase) of enterocytes or in the number of major histocompatibility complex class II+ cells, lysozyme activity, or total IgM of the distal intestine were observed. GM compared with nGM-soy fed fish had higher head kidney lysozyme (11,856 vs. 10,456 units g(-1) tissue) and a tendency towards higher acid phosphatase (0.45 vs. 0.39 micromol h(-1) kg(-1) body mass in whole tissue) activities, respectively. Plasma insulin and thyroxin levels, and hepatic fructose-1,6-bisphosphatase and ethoxyresorufin-O-deethylase activities were not significantly affected. It is not possible, however, to conclude whether the differences in responses to GM-soy were due to the genetic modification or to differences in soy cultivars in the soy-containing diets. Results from studies using non-modified, parental line soybeans as the control group are necessary to evaluate whether genetic modification of soybeans in diets poses any risk to farmed Atlantic salmon.
authors.affiliation: Aquaculture Protein Centre, CoE, Norway. anne.mckellep@veths.no
authors.forename: A M
authors.initials: AM
authors.lastname: Bakke-McKellep
authors.forename: E O
authors.initials: EO
authors.lastname: Koppang
authors.forename: G
authors.initials: G
authors.lastname: Gunnes
authors.forename: M
authors.initials: M
authors.lastname: Sanden
authors.forename: G-I
authors.initials: GI
authors.lastname: Hemre
authors.forename: T
authors.initials: T
authors.lastname: Landsverk
authors.forename: A
authors.initials: A
authors.lastname: Krogdahl
mesh_terms: D000821:Animal Feed / Q000032:analysis; D000818:Animals; D017756:Aquaculture / Q000379:methods; D019363:Cytochrome P-450 CYP1A1 / Q000032:analysis; D004032:Diet / Q000662:veterinary*; D030841:Food, Genetically Modified; D005802:Genes, MHC Class II / Q000502:physiology; D000949:Histocompatibility Antigens Class II / Q000032:analysis; D007075:Immunoglobulin M / Q000032:analysis; D007150:Immunohistochemistry / Q000662:veterinary; D008099:Liver / Q000201:enzymology; D009113:Muramidase / Q000032:analysis; D020317:Salmo salar / Q000033:anatomy & histology / Q000502:physiology*; D013025:Glycine max
chemical_list: D000949:Histocompatibility Antigens Class II; D007075:Immunoglobulin M; D019363:Cytochrome P-450 CYP1A1; D009113:Muramidase