Iron assimilation by the clam Laternula elliptica: Do stable isotopes (δ56Fe) help to decipher the sources?

Iron stable isotope signatures (δ(56)Fe) in hemolymph (bivalve blood) of the Antarctic bivalve Laternula elliptica were analyzed by Multiple Collector-Inductively Coupled Plasma-Mass Spectrometry (MC-ICP-MS) to test whether the isotopic fingerprint can be tracked back to the predominant sources of the assimilated Fe. An earlier investigation of Fe concentrations in L. elliptica hemolymph suggested that an assimilation of reactive and bioavailable Fe (oxyhydr)oxide particles (i.e. ferrihydrite), precipitated from pore water Fe around the benthic boundary, is responsible for the high Fe concentration in L. elliptica (Poigner et al., 2013 b). At two stations in Potter Cove (King George Island, Antarctica) bivalve hemolymph showed mean δ(56)Fe values of -1.19 ± 0.34‰ and -1.04 ± 0.39 ‰, respectively, which is between 0.5‰ and 0.85‰ lighter than the pool of easily reducible Fe (oxyhydr)oxides of the surface sediments (-0.3‰ to -0.6‰). This is in agreement with the enrichment of lighter Fe isotopes at higher trophic levels, resulting from the preferential assimilation of light isotopes from nutrition. Nevertheless, δ(56)Fe hemolymph values from both stations showed a high variability, ranging between -0.21‰ (value close to unaltered/primary Fe(oxyhydr)oxide minerals) and -1.91‰ (typical for pore water Fe or diagenetic Fe precipitates), which we interpret as a "mixed" δ(56)Fe signature caused by Fe assimilation from different sources with varying Fe contents and δ(56)Fe values. Furthermore, mass dependent Fe fractionation related to physiological processes within the bivalve cannot be ruled out. This is the first study addressing the potential of Fe isotopes for tracing back food sources of bivalves.

Goldfish brain and heart are well protected from Ni²âº-induced oxidative stress.

After 96 h goldfish exposure to 10, 25 or 50 mg/L of Ni(2+) no Ni accumulation was found in the brain, but lipid peroxide concentration was by 44% elevated in the brain, whereas carbonyl protein content was by 45-45% decreased in the heart. High molecular mass thiol concentration was enhanced by 30% in the heart, while in the brain low molecular mass thiol concentration increased by 28-88%. Superoxide dismutase activity was by 27% and 35% increased in the brain and heart, respectively. Glutathione peroxidase activity was lowered to 38% and 62% of control values in both tissues, whereas catalase activity was increased in the heart by 15-45%, accompanied by 18-29% decreased glutathione reductase activity. The disturbances of free radical processes in the brain and heart might result from Ni-induced injuries to other organs with more prominent changes in the heart, because of close contact of this organ with blood, whereas the blood-brain barrier seems to protect the brain.

Antioxidant system efficiently protects goldfish gills from Ni(2+)-induced oxidative stress.

Fish gills are target organs for waterborne metal ions and this work aimed to investigate the effects of waterborne Ni(2+) (10, 25 and 50 mg L(-1)) on goldfish gills. A special focus was on the relationship between Ni uptake and the homeostasis of reactive oxygen species (ROS) in the gills, the tissue, in direct contact with the metal pollutant. Ni-accumulation in the gills occurred as a function of exposure concentration (R(2)=0.98). The main indices of oxidative stress, namely carbonyl proteins (CP) and lipid peroxides (LOOH), decreased by 21-33% and 21-24%, as well as the activities of principal antioxidant enzymes superoxide dismutase and glutathione-dependent peroxidase, by 29-47% and 41-46%, respectively, in gills of Ni-exposed fish. One of the main players in the antioxidant defense of gills seems to be catalase, which increased by 23-53% in Ni-treated fish, and low molecular mass thiol-containing compounds (L-SH), exceeding untreated controls by 73-105% after fish exposure to 10-50 mg L(-1) of Ni(2+). The increased level of L-SH, mainly represented by reduced glutathione, was supported by enhanced activities of glutathione reductase (by 27-38%), glutathione-S-transferase (56-141%) and glucose-6-phosphate dehydrogenase (by 96-117%) and demonstrates the ability of the antioxidant system of gills to resist Ni-induced oxidative stress.

Tissue specificity in nickel uptake and induction of oxidative stress in kidney and spleen of goldfish Carassius auratus, exposed to waterborne nickel.

Toxic and carcinogenic effects of nickel compounds are suggested to result from nickel-mediated oxidative damage to macromolecules and/or inhibition of cellular antioxidant defenses. We investigated the effects of waterborne Ni(2+) (10, 25 and 50 mg/L) on the blood and blood-producing tissues (kidney and spleen) of goldfish to identify relationships between Ni accumulation and oxidative stress. Whereas the main hematological parameters (total hemoglobin and hematocrit) were unaffected, Ni(2+) exposure had substantial influence on goldfish immune system, causing lymphopenia. Ni accumulation increased renal iron content (by 49-78%) and resulted in elevated lipid peroxide (by 29%) and protein carbonyl content (by 274-278%), accompanied by suppression of the activities of superoxide dismutase (by 50-53%), glutathione peroxidase (15-45%), glutathione reductase (31-37%) and glucose-6-phosphate dehydrogenase (20-44%), indicating development of oxidative stress in kidney. In contrast to kidney, in spleen the activation of glutathione peroxidase (by 34-118%), glutathione-S-transferase (by 41-216%) and glutathione reductase (by 47%), as well as constant levels of low molecular mass thiols and metals together with enhanced activity of glucose-6-phosphate dehydrogenase (by 41-94%) speaks for a powerful antioxidant potential that counteracts Ni-induced ROS production. Further, as Ni accumulation in this organ was negligible, Ni-toxicity in spleen may be minimized by efficient exclusion of this otherwise toxic metal.