Proteomics in the liver of gilthead sea bream (Sparus aurata) to elucidate the cellular response induced by the intake of maslinic acid.

Maslinic acid (MA) is a pentacyclic triterpene used as a feed additive to stimulate growth, protein-turnover rates, and hyperplasia in fish. To further our understanding of cellular mechanisms underlying the action of MA, we have used 2-DE coupled with MS to identify proteins differentially expressed in the livers of juvenile gilthead sea bream (Sparus aurata) grown under fish-farm conditions and fed with a 100 mg/kg MA-enriched diet (MA(100)). After the comparison of the protein profiles from MA(100) fed fish and from control, 49 protein spots were found to be altered in abundance (≥2-fold). Analysis by MALDI-TOF/TOF allowed the unambiguous identification of 29 spots, corresponding to 19 different proteins. These proteins were: phosphoglucomutase, phosphoglucose isomerase, S-adenosyl methionine-dependent methyltransferase class I, aldehyde dehydrogenase, catalase, 6-phosphogluconate dehydrogenase, fumarylacetoacetate hydrolase, 4-hydroxyphenylpyruvic dioxygenase, methylmalonate-semialdehyde dehydrogenase, lysozyme, urate oxidase, elongation factor 2, 60 kDa heat-shock protein, 58 kDa glucose-regulated protein, cytokeratin E7, type-II keratin, intermediate filament proteins, 17-β-hydroxysteroid dehydrogenase type 4, and kinase suppressor of Ras1. Western blot analysis of kinase suppressor of Ras1, glucose 6-phosphate dehydrogenase, elongation factor 2, 60 kDa heat-shock protein, and catalase supported the proteome evidence. Based on the changes found in the protein-expression levels of these proteins, we proposed a cellular-signalling pathway to explain the hepatic-cell response to the intake of a diet containing MA.
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