T. Agusa, T. Kunito, S. Tanabe, M. Pourkazemi, and D. G. Aubrey, Concentrations of trace elements in muscle of sturgeons in the Caspian Sea, Marine Pollution Bulletin, vol.49, issue.9-10, pp.789-800, 2004.
DOI : 10.1016/j.marpolbul.2004.06.008

I. Apraiz, J. Mi, and S. Cristobal, Identification of Proteomic Signatures of Exposure to Marine Pollutants in Mussels (Mytilus edulis), Molecular & Cellular Proteomics, vol.5, issue.7, pp.1274-1285, 2006.
DOI : 10.1074/mcp.M500333-MCP200

E. Baatrup and K. B. Doving, Histochemical demonstration of mercury in the olfactory system of salmon (Salmo salar L.) following treatments with dietary methylmercuric chloride and dissolved mercuric chloride, Ecotoxicology and Environmental Safety, vol.20, issue.3, pp.277-289, 1990.
DOI : 10.1016/0147-6513(90)90007-R

O. A. Barski, V. Z. Papusha, G. R. Kunkel, and K. H. Gabbay, Regulation of aldehyde reductase expression by STAF and CHOP, Genomics, vol.83, issue.1, pp.119-129, 2004.
DOI : 10.1016/S0888-7543(03)00213-1

G. Benaim and A. Villalobo, Phosphorylation of calmodulin, European Journal of Biochemistry, vol.60, issue.15, pp.3619-3631, 2002.
DOI : 10.1046/j.1432-1033.2002.03038.x

M. H. Berntssen, A. Aatland, and R. D. Handy, Chronic dietary mercury exposure causes oxidative stress, brain lesions, and altered behaviour in Atlantic salmon (Salmo salar) parr, Aquatic Toxicology, vol.65, issue.1, pp.55-72, 2003.
DOI : 10.1016/S0166-445X(03)00104-8

R. Billard and G. Lecointre, Biology and conservation of sturgeon and paddlefish, Reviews in Fish Biology and Fisheries, vol.10, issue.4, pp.355-392, 2001.
DOI : 10.1023/A:1012231526151

D. Bonacker, T. Stoiber, M. Wang, K. J. Bohm, I. Prots et al., Genotoxicity of inorganic mercury salts based on disturbed microtubule function, Archives of Toxicology, vol.64, issue.10, pp.575-583, 2004.
DOI : 10.1007/s00204-004-0578-8

M. M. Bradford, A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Analytical Biochemistry, vol.72, issue.1-2, pp.248-254, 1976.
DOI : 10.1016/0003-2697(76)90527-3

G. Candiano, M. Bruschi, L. Musante, L. Santucci, G. M. Ghiggeri et al., Blue silver: A very sensitive colloidal Coomassie G-250 staining for proteome analysis, ELECTROPHORESIS, vol.25, issue.9, pp.1327-1333, 2004.
DOI : 10.1002/elps.200305844

O. Carnevali and F. Maradonna, Exposure to xenobiotic compounds: looking for new biomarkers, General and Comparative Endocrinology, vol.131, issue.3, pp.203-208, 2003.
DOI : 10.1016/S0016-6480(03)00105-9

P. A. Coulombe, X. Tong, S. Mazzalupo, Z. Wang, and P. Wong, Great promises yet to be fulfilled: Defining keratin intermediate filament function in vivo, European Journal of Cell Biology, vol.83, issue.11-12, pp.735-746, 2004.
DOI : 10.1078/0171-9335-00443

A. J. Edgar and J. M. Polak, Cloning and Tissue Distribution of Three Murine ??/?? Hydrolase Fold Protein cDNAs, Biochemical and Biophysical Research Communications, vol.292, issue.3, pp.617-625, 2002.
DOI : 10.1006/bbrc.2002.6692

H. Esterbauer, K. H. Cheeseman, M. U. Dianzani, G. Poli, and T. F. Slater, in rat liver microsomes, Biochemical Journal, vol.208, issue.1, pp.129-140, 1982.
DOI : 10.1042/bj2080129

P. R. Gardner, I. Raineri, L. B. Epstein, and C. W. White, Superoxide Radical and Iron Modulate Aconitase Activity in Mammalian Cells, Journal of Biological Chemistry, vol.270, issue.22, pp.13399-13405, 1995.
DOI : 10.1074/jbc.270.22.13399

R. Gardner, S. Kazi, and E. M. Ellis, Detoxication of the environmental pollutant acrolein by a rat liver aldo-keto reductase, Toxicology Letters, vol.148, issue.1-2, pp.65-72, 2004.
DOI : 10.1016/j.toxlet.2003.12.056

S. Gasso, R. M. Cristofol, G. Selema, R. Rosa, E. Rodriguez-farre et al., pathway blockers differentially protect against methylmercury and mercuric chloride neurotoxicity, Journal of Neuroscience Research, vol.17, issue.1, pp.135-145, 2001.
DOI : 10.1002/jnr.1205

I. Gavidia, P. Perez-bermudez, and H. U. Seitz, leaves, European Journal of Biochemistry, vol.4, issue.12, pp.2842-2850, 2002.
DOI : 10.1046/j.1432-1033.2002.02931.x

E. Godfroid, M. Geuskens, T. Dupressoir, I. Parent, and C. Szpirer, Cytokeratins are exposed on the outer surface of established human mammary-carcinoma cells, 1991.

E. J. Gribble, S. W. Hong, and E. M. Faustman, The magnitude of methylmercury-induced cytotoxicity and cell cycle arrest is p53-dependent, Birth Defects Research Part A: Clinical and Molecular Teratology, vol.19, issue.182, pp.29-38, 2005.
DOI : 10.1002/bdra.20104

I. Hajimohammadreza, A. W. Probert, L. L. Coughenour, S. A. Borosky, F. W. Marcoux et al., A specific inhibitor of calcium/calmodulin-dependent protein kinase-II provides neuroprotection against NMDA-and hypoxia/hypoglycemia-induced cell death, J. Neurosci, vol.15, pp.4093-4101, 1995.

H. H. Harris, I. J. Pickering, and G. N. George, The Chemical Form of Mercury in Fish, Science, vol.301, issue.5637, 1203.
DOI : 10.1126/science.1085941

D. Hyndman, D. R. Bauman, V. V. Heredia, and T. M. Penning, The aldo-keto reductase superfamily homepage, Chemico-Biological Interactions, vol.143, issue.144, pp.143-144, 2003.
DOI : 10.1016/S0009-2797(02)00193-X

C. Jacob, M. Courbot, F. Martin, A. Brun, and M. Chalot, Transcriptomic responses to cadmium in the ectomycorrhizal fungus Paxillus involutus, FEBS Letters, vol.3, issue.3, pp.423-427, 2004.
DOI : 10.1016/j.febslet.2004.09.028

R. A. Keates and B. Yott, Inhibition of microtubule polymerization by micromolar concentrations of mercury(II), Biochemistry and Cell Biology, vol.62, issue.9, pp.814-818, 1984.
DOI : 10.1139/o84-103

R. P. Khodorevskaya, G. F. Dovgopol, O. L. Zhuravleva, and A. D. Vlasenko, Present status of commercial stocks of sturgeons in the Caspian Sea basin, Environ. Biol. Fishes, vol.48, pp.209-220, 1997.
DOI : 10.1007/0-306-46854-9_11

S. H. Kim and R. P. Sharma, Cytotoxicity of inorganic mercury in murine T and B lymphoma cell lines: involvement of reactive oxygen species, Ca2+ homeostasis, and cytokine gene expression, Toxicology in Vitro, vol.17, issue.4, pp.385-395, 2003.
DOI : 10.1016/S0887-2333(03)00040-7

D. Li, A. Hinshelwood, R. Gardner, G. Mcgarvie, and E. M. Ellis, Mouse aldo-keto reductase AKR7A5 protects V79 cells against 4-hydroxynonenal-induced apoptosis, Toxicology, vol.226, issue.2-3, pp.172-180, 2006.
DOI : 10.1016/j.tox.2006.06.013

T. L. Limke and W. D. Atchison, Acute Exposure to Methylmercury Opens the Mitochondrial Permeability Transition Pore in Rat Cerebellar Granule Cells, Toxicology and Applied Pharmacology, vol.178, issue.1, pp.52-61, 2002.
DOI : 10.1006/taap.2001.9327

W. Maret, C. A. Yetman, and L. Jiang, Enzyme regulation by reversible zinc inhibition: glycerol phosphate dehydrogenase as an example, Chemico-Biological Interactions, vol.130, issue.132, pp.130-132, 2001.
DOI : 10.1016/S0009-2797(00)00243-X

K. Miura, M. Inokawa, and N. Imura, Effects of methylmercury and some metal ions on microtubule networks in mouse glioma cells and in vitro tubulin polymerization, Toxicology and Applied Pharmacology, vol.73, issue.2, pp.218-231, 1984.
DOI : 10.1016/0041-008X(84)90327-2

Y. Miura, M. Kano, K. Abe, S. Urano, S. Suzuki et al., Age-dependent variations of cell response to oxidative stress: Proteomic approach to protein expression and phosphorylation, ELECTROPHORESIS, vol.262, issue.14, pp.2786-2796, 2005.
DOI : 10.1002/elps.200500172

M. Nardini and B. W. Dijkstra, ??/?? Hydrolase fold enzymes: the family keeps growing, Current Opinion in Structural Biology, vol.9, issue.6, pp.732-737, 1999.
DOI : 10.1016/S0959-440X(99)00037-8

D. L. Ollis, E. Cheah, M. Cygler, B. Dijkstra, F. Frolow et al., hydrolase fold, "Protein Engineering, Design and Selection", vol.5, issue.3, pp.197-211, 1992.
DOI : 10.1093/protein/5.3.197

X. S. Puente and C. Lopez-otin, Cloning and expression analysis of a novel human serine hydrolase with sequence similarity to prokaryotic enzymes involved in the degradation of aromatic compounds, J. Biol. Chem, vol.270, pp.12926-12932, 1995.

X. S. Puente and C. Lopez-otin, The PLEES proteins: a family of structurally related enzymes widely distributed from bacteria to humans, Biochemical Journal, vol.322, issue.3, pp.947-949, 1997.
DOI : 10.1042/bj3220947

H. L. Rittner, V. Hafner, P. A. Klimiuk, L. I. Szweda, J. J. Goronzy et al., Aldose reductase functions as a detoxification system for lipid peroxidation products in vasculitis, Journal of Clinical Investigation, vol.103, issue.7, pp.1007-1013, 1999.
DOI : 10.1172/JCI4711

A. Sarmento, L. Guilhermino, and A. Afonso, Mercury chloride effects on the function and cellular integrity of sea bass (Dicentrarchus labrax) head kidney macrophages, Fish & Shellfish Immunology, vol.17, issue.5, pp.489-498, 2004.
DOI : 10.1016/j.fsi.2004.05.004

F. Silvestre, J. F. Dierick, V. Dumont, M. Dieu, M. Raes et al., Differential protein expression profiles in anterior gills of Eriocheir sinensis during acclimation to cadmium, Aquatic Toxicology, vol.76, issue.1, pp.46-58, 2006.
DOI : 10.1016/j.aquatox.2005.09.006

C. Skak and E. Baatrup, Quantitative and histochemical demonstration of mercury deposits in the inner ear of trout, Salmo trutta, exposed to dietary methylmercury and dissolved mercuric chloride, Aquatic Toxicology, vol.25, issue.1-2, pp.55-70, 1993.
DOI : 10.1016/0166-445X(93)90020-2

W. K. Son, D. Y. Lee, S. H. Lee, W. A. Joo, and C. W. Kim, Analysis of proteins expressed in rat plasma exposed to dioxin using 2-dimensional gel electrophoresis, PROTEOMICS, vol.3, issue.12, pp.2393-2401, 2003.
DOI : 10.1002/pmic.200300605

S. Srivastava, A. Chandra, N. H. Ansari, S. K. Srivastava, and A. Bhatnagar, Identification of cardiac oxidoreductase(s) involved in the metabolism of the lipid peroxidation-derived aldehyde-4-hydroxynonenal, Biochemical Journal, vol.329, issue.3, pp.469-475, 1998.
DOI : 10.1042/bj3290469

A. Tabuchi, K. Funaji, J. Nakatsubo, M. Fukuchi, T. Tsuchiya et al., Inactivation of aconitase during the apoptosis of mouse cerebellar granule neurons induced by a deprivation of membrane depolarization, Journal of Neuroscience Research, vol.94, issue.4, pp.504-515, 2003.
DOI : 10.1002/jnr.10505

R. Thier, D. Bonacker, T. Stoiber, K. J. Bohm, M. Wang et al., Interaction of metal salts with cytoskeletal motor protein systems, Toxicology Letters, vol.140, issue.141, pp.140-141, 2003.
DOI : 10.1016/S0378-4274(02)00502-7

P. J. Vig, R. Nath, and D. Desaiah, Metal inhibition of calmodulin activity in monkey brain, Journal of Applied Toxicology, vol.8, issue.5, pp.313-316, 1989.
DOI : 10.1002/jat.2550090506

S. Yee and B. H. Choi, Oxidative stress in neurotoxic effects of methylmercury poisoning, Neurotoxicology, vol.17, pp.17-26, 1996.

M. Yole, M. Wickstrom, and B. Blakley, Cell death and cytotoxic effects in YAC-1 lymphoma cells following exposure to various forms of mercury, Toxicology, vol.231, issue.1, pp.40-57, 2007.
DOI : 10.1016/j.tox.2006.11.062

J. L. Yoo and D. M. Janz, Tissue-Specific HSP70 Levels and Reproductive Physiological Responses in Fishes Inhabiting a Metal-Contaminated Creek, Archives of Environmental Contamination and Toxicology, vol.45, issue.1, pp.110-120, 2003.
DOI : 10.1007/s00244-002-0109-7

Q. Zhang and D. E. Riechers, Proteomic characterization of herbicide safener-induced proteins in the coleoptile ofTriticum tauschii seedlings, PROTEOMICS, vol.4, issue.7, pp.2058-2071, 2004.
DOI : 10.1002/pmic.200300733

W. Zheng, M. Aschner, and J. F. Ghersi-egea, Brain barrier systems: a new frontier in metal neurotoxicological research, Toxicology and Applied Pharmacology, vol.192, issue.1, pp.1-11, 2003.
DOI : 10.1016/S0041-008X(03)00251-5

J. Y. Zhu, H. Q. Huang, X. D. Bao, Q. M. Lin, and Z. Cai, Acute toxicity profile of cadmium revealed by proteomics in brain tissue of Paralichthys olivaceus: Potential role of transferrin in cadmium toxicity, Aquatic Toxicology, vol.78, issue.2, pp.127-135, 2006.
DOI : 10.1016/j.aquatox.2006.02.010