Proteomic responses to hypoxia at different temperatures in the Great Scallop (Pecten maximus)

Laboratoire des Sciences de l’Environnement Marin, LEMAR UMR 6539 CNRS/UBO/IRD/Ifremer, Université de Bretagne Occidentale, Institut Universitaire Européen de la Mer, Plouzané, France
Department of Comparative Biomedicine and Food Science, University of Padova, Padova, Italy
DOI
10.7287/peerj.preprints.736v1
Subject Areas
Aquaculture, Fisheries and Fish Science, Ecology, Environmental Sciences, Marine Biology, Molecular Biology
Keywords
Proteomic, Hypoxia, Temperature, Bivalves, Non-model, Marine Biology
Copyright
© 2014 Artigaud et al.
Licence
This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, reproduction and adaptation in any medium and for any purpose provided that it is properly attributed. For attribution, the original author(s), title, publication source (PeerJ PrePrints) and either DOI or URL of the article must be cited.
Cite this article
Artigaud SS, Lacroix CC, Richard JJ, Flye-Sainte-Marie J, Bargelloni LL, Pichereau V. 2014. Proteomic responses to hypoxia at different temperatures in the Great Scallop (Pecten maximus) PeerJ PrePrints 2:e736v1

Abstract

Hypoxia and hyperthermia are two connected consequences of the ongoing global change that constitute major threats for coastal marine organisms. In the present study, we used a proteomic approach to characterize the changes induced by hypoxia in individuals of the great scallop, Pecten maximus, subjected to three different temperatures, i.e. 10°C, 18°C and 25°C. We did not observe any significant change induced by hypoxia in animals acclimated at 10°C. Contrastingly at 18°C and 25°C, 16 and 11 protein spots were differentially accumulated between normoxia and hypoxia, respectively. Moreover, biochemical data, i.e. octopine dehydrogenase activity and arginine assays suggests that animals grown at 25°C switched their metabolism towards anaerobic metabolism when exposed to either normoxia or hypoxia, suggesting that this temperature is out of the scallops’ optimal thermal window. In all, 11 proteins could be unambiguously identified by mass spectrometry, involved in protein modifications and signaling (e.g. CK2, TBK1), metabolism (e.g. ENO3) or cytoskeleton (GSN). The potential roles of these proteins in the thermal-dependent response of scallops to hypoxia are discussed.

Author Comment

This is a submission to PeerJ for peer review.