Differential sensitivity to cadmium of key mitochondrial enzymes in the eastern oyster, Crassostrea virginica Gmelin (Bivalvia: Ostreidae).
Combined effects of cadmium (Cd) and temperature on key mitochondrial enzymes [including Complexes I-IV of electron transport chain and Krebs cycle enzymes citrate synthase (CS), and NAD- and NADP-dependent isocitrate dehydrogenases (NAD-IDH and NADP-IDH)] were studied in a marine ectotherm, Crassostrea virginica in order to better understand the mechanisms of Cd-induced impairment of mitochondrial function. Matrix enzymes including CS and isocitrate dehydrogenases were the most sensitive to Cd making Krebs cycle a likely candidate to explain Cd-induced impairment of mitochondrial substrate oxidation. CS and NAD-IDH had IC(50) of 26 and 65 microM at the acclimation temperature (15 degrees C) and 65 (CS) and 1.5 (NAD-IDH) microM at elevated temperature (25 degrees C), respectively. Mitochondrial NADP-IDH was the most sensitive to Cd with IC(50) of 14 and 3.4 microM at 15 degrees and 25 degrees C, respectively. Electron transport chain (ETC) complexes were significantly less sensitive to the direct effects of Cd with IC(50) ranging from 260 to >>400 microM. Temperature increase led to a higher sensitivity of mitochondrial enzymes to the inhibitory effects of Cd as indicated by a decline in IC(50) with the exception of Complex III from gills and CS from gills and hepatopancreas. Cd exposure also resulted in a decrease in activation energy of mitochondrial enzymes suggesting that mitochondria from Cd-exposed oysters could exhibit reduced capacity to respond to temperature rise with an adequate increase in the substrate flux. These interactive effects of Cd and temperature on mitochondrial enzymes could negatively affect metabolic performance of oysters and possibly other ectotherms in polluted environments during temperature increase such as expected during the global climate change and/or tidal or seasonal warming in estuarine and coastal waters.
Ivanina
Anna V
AV
Biology Department, University of North Carolina , Charlotte, NC 28223, USA.
Habinck
Emily
E
Sokolova
Inna M
IM
D000818:Animals; D002104:Cadmium / Q000633:toxicity*; D002950:Citrate (si)-Synthase / Q000037:antagonists & inhibitors; D049896:Crassostrea / Q000187:drug effects* / Q000201:enzymology; D004305:Dose-Response Relationship, Drug; D042967:Electron Transport Complex I / Q000037:antagonists & inhibitors; D042963:Electron Transport Complex II / Q000037:antagonists & inhibitors; D014450:Electron Transport Complex III / Q000037:antagonists & inhibitors; D003576:Electron Transport Complex IV / Q000037:antagonists & inhibitors; D004734:Energy Metabolism / Q000187:drug effects; D004791:Enzyme Inhibitors / Q000633:toxicity*; D007521:Isocitrate Dehydrogenase / Q000037:antagonists & inhibitors; D008928:Mitochondria / Q000187:drug effects* / Q000201:enzymology; D024101:Mitochondrial Proteins / Q000037:antagonists & inhibitors* / Q000378:metabolism; D013696:Temperature; D014874:Water Pollutants, Chemical / Q000633:toxicity*
D004791:Enzyme Inhibitors; D024101:Mitochondrial Proteins; D014874:Water Pollutants, Chemical; D002104:Cadmium; D007521:Isocitrate Dehydrogenase; C039355:isocitrate dehydrogenase (NADP+); D042963:Electron Transport Complex II; D003576:Electron Transport Complex IV; D002950:Citrate (si)-Synthase; D042967:Electron Transport Complex I; D014450:Electron Transport Complex III