Changes in Liver Proteome Expression of Senegalese Sole (Solea senegalensis) in Response to Repeated Handling Stress

Publication: Research - peer-reviewJournal article – Annual report year: 2012

Standard

Changes in Liver Proteome Expression of Senegalese Sole (Solea senegalensis) in Response to Repeated Handling Stress. / Cordeiro, O. D.; Silva, Tomé Santos; Alves, R. N.; Costas, B.; Wulff, Tune; Richard, N.; Vareilles, M. de; Conceição, L. E. C.; Rodrigues, P. M.

In: Marine Biotechnology, Vol. 14, No. 6, 2012, p. 714-729.

Publication: Research - peer-reviewJournal article – Annual report year: 2012

Harvard

Cordeiro, OD, Silva, TS, Alves, RN, Costas, B, Wulff, T, Richard, N, Vareilles, MD, Conceição, LEC & Rodrigues, PM 2012, 'Changes in Liver Proteome Expression of Senegalese Sole (Solea senegalensis) in Response to Repeated Handling Stress' Marine Biotechnology, vol 14, no. 6, pp. 714-729., 10.1007/s10126-012-9437-4

APA

CBE

Cordeiro OD, Silva TS, Alves RN, Costas B, Wulff T, Richard N, Vareilles MD, Conceição LEC, Rodrigues PM. 2012. Changes in Liver Proteome Expression of Senegalese Sole (Solea senegalensis) in Response to Repeated Handling Stress. Marine Biotechnology. 14(6):714-729. Available from: 10.1007/s10126-012-9437-4

MLA

Vancouver

Author

Cordeiro, O. D.; Silva, Tomé Santos; Alves, R. N.; Costas, B.; Wulff, Tune; Richard, N.; Vareilles, M. de; Conceição, L. E. C.; Rodrigues, P. M. / Changes in Liver Proteome Expression of Senegalese Sole (Solea senegalensis) in Response to Repeated Handling Stress.

In: Marine Biotechnology, Vol. 14, No. 6, 2012, p. 714-729.

Publication: Research - peer-reviewJournal article – Annual report year: 2012

Bibtex

@article{c3934127cc864e0e975b4618bc5ea67c,
title = "Changes in Liver Proteome Expression of Senegalese Sole (Solea senegalensis) in Response to Repeated Handling Stress",
keywords = "Solea senegalensis, Chronic stress, Liver proteome, Fish welfare, Aquaculture",
publisher = "Springer New York LLC",
author = "Cordeiro, {O. D.} and Silva, {Tomé Santos} and Alves, {R. N.} and B. Costas and Tune Wulff and N. Richard and Vareilles, {M. de} and Conceição, {L. E. C.} and Rodrigues, {P. M.}",
year = "2012",
doi = "10.1007/s10126-012-9437-4",
volume = "14",
number = "6",
pages = "714--729",
journal = "Marine Biotechnology",
issn = "1436-2228",

}

RIS

TY - JOUR

T1 - Changes in Liver Proteome Expression of Senegalese Sole (Solea senegalensis) in Response to Repeated Handling Stress

A1 - Cordeiro,O. D.

A1 - Silva,Tomé Santos

A1 - Alves,R. N.

A1 - Costas,B.

A1 - Wulff,Tune

A1 - Richard,N.

A1 - Vareilles,M. de

A1 - Conceição,L. E. C.

A1 - Rodrigues,P. M.

AU - Cordeiro,O. D.

AU - Silva,Tomé Santos

AU - Alves,R. N.

AU - Costas,B.

AU - Wulff,Tune

AU - Richard,N.

AU - Vareilles,M. de

AU - Conceição,L. E. C.

AU - Rodrigues,P. M.

PB - Springer New York LLC

PY - 2012

Y1 - 2012

N2 - The Senegalese sole, a high-value flatfish, is a good candidate for aquaculture production. Nevertheless, there are still issues regarding this species’ sensitivity to stress in captivity. We aimed to characterize the hepatic proteome expression for this species in response to repeated handling and identify potential molecular markers that indicate a physiological response to chronic stress. Two groups of fish were reared in duplicate for 28 days, one of them weekly exposed to handling stress (including hypoxia) for 3 min, and the other left undisturbed. Two-dimensional electrophoresis enabled the detection of 287 spots significantly affected by repeated handling stress (Wilcoxon–Mann–Whitney U test, p < 0.05), 33 of which could be reliably identified by peptide mass spectrometry. Chronic exposure to stress seems to have affected protein synthesis, folding and turnover (40S ribosomal protein S12, cathepsin B, disulfide-isomerase A3 precursor, cell-division cycle 48, and five distinct heat shock proteins), amino acid metabolism, urea cycle and methylation/folate pathways (methionine adenosyltransferase I α, phenylalanine hydroxylase, mitochondrial agmatinase, serine hydroxymethyltransferase, 3-hydroxyanthranilate 3,4-dioxygenase, and betaine homocysteine methyltransferase), cytoskeletal (40S ribosomal protein SA, α-actin, β-actin, α-tubulin, and cytokeratin K18), aldehyde detoxification (aldehyde dehydrogenase 4A1 family and aldehyde dehydrogenase 7A1 family), carbohydrate metabolism and energy homeostasis (fatty acid-binding protein, enolase 3, enolase 1, phosphoglycerate kinase, glyceraldehyde-3-phosphate dehydrogenase, aconitase 1, mitochondrial ATP synthase α-subunit, and electron-transfer flavoprotein α polypeptide), iron and selenium homeostasis (transferrin and selenium binding protein 1), steroid hormone metabolism (3-oxo-5-β-steroid 4-dehydrogenase), and purine salvage (hypoxanthine phosphoribosyltransferase). Further characterization is required to fully assess the potential of these markers for the monitoring of fish stress response to chronic stressors of aquaculture environment.

AB - The Senegalese sole, a high-value flatfish, is a good candidate for aquaculture production. Nevertheless, there are still issues regarding this species’ sensitivity to stress in captivity. We aimed to characterize the hepatic proteome expression for this species in response to repeated handling and identify potential molecular markers that indicate a physiological response to chronic stress. Two groups of fish were reared in duplicate for 28 days, one of them weekly exposed to handling stress (including hypoxia) for 3 min, and the other left undisturbed. Two-dimensional electrophoresis enabled the detection of 287 spots significantly affected by repeated handling stress (Wilcoxon–Mann–Whitney U test, p < 0.05), 33 of which could be reliably identified by peptide mass spectrometry. Chronic exposure to stress seems to have affected protein synthesis, folding and turnover (40S ribosomal protein S12, cathepsin B, disulfide-isomerase A3 precursor, cell-division cycle 48, and five distinct heat shock proteins), amino acid metabolism, urea cycle and methylation/folate pathways (methionine adenosyltransferase I α, phenylalanine hydroxylase, mitochondrial agmatinase, serine hydroxymethyltransferase, 3-hydroxyanthranilate 3,4-dioxygenase, and betaine homocysteine methyltransferase), cytoskeletal (40S ribosomal protein SA, α-actin, β-actin, α-tubulin, and cytokeratin K18), aldehyde detoxification (aldehyde dehydrogenase 4A1 family and aldehyde dehydrogenase 7A1 family), carbohydrate metabolism and energy homeostasis (fatty acid-binding protein, enolase 3, enolase 1, phosphoglycerate kinase, glyceraldehyde-3-phosphate dehydrogenase, aconitase 1, mitochondrial ATP synthase α-subunit, and electron-transfer flavoprotein α polypeptide), iron and selenium homeostasis (transferrin and selenium binding protein 1), steroid hormone metabolism (3-oxo-5-β-steroid 4-dehydrogenase), and purine salvage (hypoxanthine phosphoribosyltransferase). Further characterization is required to fully assess the potential of these markers for the monitoring of fish stress response to chronic stressors of aquaculture environment.

KW - Solea senegalensis

KW - Chronic stress

KW - Liver proteome

KW - Fish welfare

KW - Aquaculture

U2 - 10.1007/s10126-012-9437-4

DO - 10.1007/s10126-012-9437-4

JO - Marine Biotechnology

JF - Marine Biotechnology

SN - 1436-2228

IS - 6

VL - 14

SP - 714

EP - 729

ER -