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Bibliographie de l'Institut Maurice-Lamontagne

Poissons / Squalius cephalus / Mullet, Meunier, Chevaine, Cabot truité, Chavasson

MALTAIS, D., R.L. ROY, C.M. COUILLARD, 2010. Hybrid ELISAs for vitellogenins of the endangered Copper Redhorse (Moxostoma hubbsi) and the Shorthead Redhorse (Moxostoma macrolepidotum (Cypriniformes, catostomidae). Ecotoxicol. Environ. Saf., 73(5): 883-892.

[Résumé disponible seulement en anglais]
The shorthead redhorse (sr) Moxostoma macrolepidotum is endemic in North America, while in Canada the copper redhorse (cr) Moxostoma hubbsi is classified as endangered. A commercial heterologous carp vitellogenin (VTG) sandwich ELISA underestimates VTGs in these species. Hybrid ELISAs, using anti-carp VTG antibodies and purified sr- and cr-VTGs as standards, were validated to measure VTGs in plasma and surface mucus of redhorse species. The hybrid ELISAs showed good precision, sensitivity and accuracy. Following induction with β-estradiol 3-benzoate (E2B), levels of plasma VTG (mean ± SEM) in male sr increased from 2.7 ± 1.5 μg/ml to 16.5±2.2 mg/ml. In immature cr, plasma VTG increased to 70.1±13.8 mg/ml after induction, from an initial value of 37.7±51.0 μg/ml. Levels of VTG in mucus from E2B-injected fish were highly correlated (p<0.0001) with levels in plasma, but not in a non-induced mature female. Hybrid assays are a good compromise between homologous and heterologous assays, especially for small-bodied or endangered fish species. The performance of the hybrid assays strongly suggests they could be used to determine exposure of these species to estrogenic contaminants and contribute to restoration efforts of the copper redhorse. Crown Copyright ©2010 Elsevier Inc.

MALTAIS, D., R.L. ROY, 2009. Purification and partial characterization of vitellogenin from shorthead redhorse (Moxostoma macrolepidotum)and copper redhorse (Moxostoma hubbsi) and detection in plasma and mucus with a heterologous antibody. Fish. Physiol. Biochem., 35: 241-254 .

[Résumé disponible seulement en anglais]
Vitellogenin (VTG), the egg yolk precursor protein, was purified from plasma of estradiol-3- benzoate (E2B)-treated male shorthead redhorse (Moxostoma macrolepidotum) and immature copper redhorse (Moxostoma hubbsi) by a two-step chromatographic procedure without precipitation. Intact VTGs appeared as dimers with apparent molecular masses, determined by gel filtration, of ˜425 kDa (copper redhorse) and ˜450 kDa (shorthead redhorse). In native polyacrylamide gel electrophoresis (PAGE), dimeric redhorse VTGs appeared as a 520 kDa band. Both VTGs were reduced to a single monomer of ˜150 kDa in sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) under reducing and nonreducing conditions, indicating that monomers are not linked by disulfide bonds in the dimer form. The purified proteins were characterized as phospholipoglycoproteins. Isoelectric focusing of both VTGs revealed components with isoelectric points ranging from 5.3 to 6.0, suggesting charge heterogeneity. The amino acid composition of both VTGs contains a high proportion of nonpolar amino acids and was similar to those of other teleosts. An antibody developed against carp (Cyprinus carpio) VTG showed cross-reactivity with VTG from both redhorse species. Using this antibody, VTG was detected in plasma and surface mucus of E2B-treated redhorse. This is the most extensive report on purification and characterization of vitellogenin from catostomidid species.©2009 Springer