Biomarkers in Natural Fish Populations Indicate Adverse Biological Effects of Offshore Oil Production

Despite the growing awareness of the necessity of a sustainable development, the global economy continues to depend largely on the consumption of non-renewable energy resources. One such energy resource is fossil oil extracted from the seabed at offshore oil platforms. This type of oil production causes continuous environmental pollution from drilling waste, discharge of large amounts of produced water, and accidental spills.Samples from natural populations of haddock (Melanogrammus aeglefinus) and Atlantic cod (Gadus morhua) in two North Sea areas with extensive oil production were investigated. Exposure to and uptake of polycyclic aromatic hydrocarbons (PAHs) were demonstrated, and biomarker analyses revealed adverse biological effects, including induction of biotransformation enzymes, oxidative stress, altered fatty acid composition, and genotoxicity. Genotoxicity was reflected by a hepatic DNA adduct pattern typical for exposure to a mixture of PAHs. Control material was collected from a North Sea area without oil production and from remote Icelandic waters. The difference between the two control areas indicates significant background pollution in the North Sea.It is most remarkable to obtain biomarker responses in natural fish populations in the open sea that are similar to the biomarker responses in fish from highly polluted areas close to a point source. Risk assessment of various threats to the marine fish populations in the North Sea, such as overfishing, global warming, and eutrophication, should also take into account the ecologically relevant impact of offshore oil production

Hydrophobic molecules in lecithin-water systems. I. Formation of reversed hexagonal phases at high and low water contents.

The system dioleoylphosphatidylcholine (DOPC)-n-dodecane-2H2O was investigated with different nuclear magnetic resonance (NMR) techniques: (a) a tentative phase diagram was determined by 2H- and 31P-NMR, (b) translational diffusion coefficients were determined for the three components with the pulsed magnetic field gradient NMR technique, and (c) order parameters for perdeuterated n-dodecane were obtained by 2H-NMR. n-Dodecane induces the formation of reversed hexagonal (HII) phases at low and high water concentrations, and cubic phases at low water contents. The translational diffusion coefficients of n-dodecane in a cubic phase with 6 mol water per mol DOPC, and in an HII phase with 48 mol water per mol DOPC, were just approximately 2.5 times lower than in pure dodecane. Perdeuterated dodecane gave large quadrupole splittings in a lamellar phase, much smaller in an HII phase at low water contents, and a narrow single peak in an HII phase at high water contents. This latter observation indicates that a large fraction of the dodecane molecules is located in separate regions between the water cylinders. Our results support the model given by Gruner concerning the aggregation of membrane lipids in the presence of hydrophobic molecules

Total lipids with short and long acyl chains from Acholeplasma form nonlamellar phases.

The cell-wall-less bacterium Acholeplasma laidlawii A-EF22 synthesizes eight glycerolipids. Some of them form lamellar phases, whereas others are able to form normal or reversed nonlamellar phases. In this study we examined the phase properties of total lipid extracts with limiting average acyl chain lengths of 15 and 19 carbon atoms. The temperature at which these extracts formed reversed hexagonal (HII) phases differed by 5-10 degreesC when the water contents were 20-30 wt%. Thus the cells adjust the ratio between lamellar-forming and nonlamellar-forming lipids to the acyl chain lengths. Because short acyl chains generally increase the potential of lipids to form bilayers, it was judged interesting to determine which of the A. laidlawii A lipids are able to form reversed nonlamellar phases with short acyl chains. The two candidates with this ability are monoacyldiglucosyldiacylglycerol (MADGlcDAG) and monoglucosyldiacylglycerol. The average acyl chain lengths were 14.7 and 15.1 carbon atoms, and the degrees of acyl chain unsaturation were 32 and 46 mol%, respectively. The only liquid crystalline phase formed by MADGlcDAG is an HII phase. Monoglucosyldiacylglycerol forms reversed cubic (Ia3d) and HII phases at high temperatures. Thus, even when the organism is grown with short fatty acids, it synthesizes two lipids that have the capacity to maintain the nonlamellar tendency of the lipid bilayer. MADGlcDAG in particular contributes very powerfully to this tendency

Interaction of phosphatidylserine synthase from E. coli with lipid bilayers: coupled plasmon-waveguide resonance spectroscopy studies.

The interaction of phosphatidylserine (PS) synthase from Escherichia coli with lipid membranes was studied with a recently developed variant of the surface plasmon resonance technique, referred to as coupled plasmon-waveguide resonance spectroscopy. The features of the new technique are increased sensitivity and spectral resolution, and a unique ability to directly measure the structural anisotropy of lipid and proteolipid films. Solid-supported lipid bilayers with the following compositions were used: 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC); POPC-1-palmitoyl-2-oleoyl-sn-glycero-3-phosphate (POPA) (80:20, mol/mol); POPC-POPA (60:40, mol/mol); and POPC-1-palmitoyl-2-oleoyl-sn-glycero-3-[phospho-rac-(1-glycerol)] (POPG) (75:25, mol/mol). Addition of either POPA or POPG to a POPC bilayer causes a considerable increase of both the bilayer thickness and its optical anisotropy. PS synthase exhibits a biphasic interaction with the bilayers. The first phase, occurring at low protein concentrations, involves both electrostatic and hydrophobic interactions, although it is dominated by the latter, and the enzyme causes a local decrease of the ordering of the lipid molecules. The second phase, occurring at high protein concentrations, is predominantly controlled by electrostatic interactions, and results in a cooperative binding of the enzyme to the membrane surface. Addition of the anionic lipids to a POPC bilayer causes a 5- to 15-fold decrease in the protein concentration at which the first binding phase occurs. The results reported herein lend experimental support to a previously suggested mechanism for the regulation of the polar head group composition in E. coli membranes