Comparative petroleum hydrocarbons levels and biochemical responses in mussels from hydrothermal vents (Bathymodiolus azoricus) and coastal environments (Mytilus galloprovincialis).
Aliphatic hydrocarbons and PAHs in the whole soft tissues of Bathymodiolus azoricus from three Mid-Atlantic Ridge hydrothermal vents (Menez-Gwen, Lucky Strike and Rainbow), and Mytilus galloprovincialis from three contaminated coastal sites in South Portugal were analysed, and its effects on the digestive gland microsomes mixed-function oxygenase system (MFO) were assessed. Aliphatic hydrocarbons levels were present in the same magnitude in both coastal and hydrothermal environments, while the UCM (unresolved complex mixture) for coastal mussels were higher than in vent mussels. In general, significantly higher PAHs concentrations were found in coastal mussels, compared to B. azoricus where low molecular weight PAHs (2-3 rings) represented the majority of PAHs contrarily to what was observed in M. galloprovincialis. The MFO components were present in both mussel species, and were detected in vent mussels for the first time. However this system seems to have different roles in species from these contrasting environments. In coastal mussels MFO responded to hydrocarbon contamination while response in hydrothermal organisms appeared to be related mainly to endogenous factors.
Serafim
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A
CIMA, Faculty of Marine and Environmental Sciences, University of Algarve, Campus de Gambelas, Faro, Portugal. aserafim@ualg.pt
Lopes
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B
Company
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R
Ferreira
A M
AM
Bebianno
M J
MJ
D000818:Animals; D001267:Atlantic Ocean; D049872:Bivalvia / Q000737:chemistry* / Q000187:drug effects*; D004064:Digestive System / Q000187:drug effects / Q000201:enzymology; D006838:Hydrocarbons / Q000737:chemistry / Q000378:metabolism* / Q000633:toxicity*; D006899:Mixed Function Oxygenases / Q000187:drug effects; D049878:Mytilus / Q000737:chemistry* / Q000187:drug effects*; D010578:Petroleum / Q000633:toxicity*; D011174:Portugal
D006838:Hydrocarbons; D010578:Petroleum; D006899:Mixed Function Oxygenases