(Tables 1,2) Polar bear (Ursus maritimus), beluga whale (Delphinapterus leucas) and ringed seal (Pusa hispida) liver microsomal protein content and EROD activity

The present study assessed and compared the oxidative and reductive biotransformation of brominated flame retardants, including established polybrominated diphenyl ethers (PBDEs) and emerging decabromodiphenyl ethane (DBDPE) using an in vitro system based on liver microsomes from various arctic marine-feeding mammals: polar bear (Ursus maritimus), beluga whale (Delphinapterus leucas), and ringed seal (Pusa hispida), and in laboratory rat as a mammalian model species. Greater depletion of fully brominated BDE209 (14-25% of 30pmol) and DBDPE (44-74% of 90pmol) occurred in individuals from all species relative to depletion of lower brominated PBDEs (BDEs 99,100, and 154; 0-3% of 30pmol). No evidence of simply debrominated metabolites was observed. Investigation of phenolic metabolites in rat and polar bear revealed formation of two phenolic, likely multiply debrominated, DBDPE metabolites in polar bear and one phenolic BDE154 metabolite in polar bear and rat microsomes. For BDE209 and DBDPE, observed metabolite concentrations were low to nondetectable, despite substantial parent depletion. These findings suggested possible underestimation of the ecosystem burden of total-BDE209, as well as its transformation products, and a need for research to identify and characterize the persistence and toxicity of major BDE209 metabolites. Similar cause for concern may exist regarding DBDPE, given similarities of physicochemical and environmental behavior to BDE209, current evidence of biotransformation, and increasing use of DBDPE as a replacement for BDE209.

Seawater carbonate chemistry and protein sports of barnicle Balanus amphitrite during experiments, 2011

The majority of benthic marine invertebrates have a complex life cycle, during which the pelagic larvae select a suitable substrate, attach to it, and then metamorphose into benthic adults. Anthropogenic ocean acidification (OA) is postulated to affect larval metamorphic success through an altered protein expression pattern (proteome structure) and post-translational modifications. To test this hypothesis, larvae of an economically and ecologically important barnacle species Balanus amphitrite, were cultured from nauplius to the cyprid stage in the present (control) and in the projected elevated concentrations of CO2 for the year 2100 (the OA treatment). Cyprid response to OA was analyzed at the total proteome level as well as two protein post-translational modification (phosphorylation and glycosylation) levels using a 2-DE based proteomic approach. The cyprid proteome showed OA-driven changes. Proteins that were differentially up or down regulated by OA come from three major groups, namely those related to energy-metabolism, respiration, and molecular chaperones, illustrating a potential strategy that the barnacle larvae may employ to tolerate OA stress. The differentially expressed proteins were tentatively identified as OA-responsive, effectively creating unique protein expression signatures for OA scenario of 2100. This study showed the promise of using a sentinel and non-model species to examine the impact of OA at the proteome level.