Change in metallothionein phosphorylation state in Mya arenaria clams: implication in metal metabolism and oxidative stress
Keywords:Phosphorylated metallothioneins, mitochondrial electron transport activity, cytochrome c oxidase, heavy metals, Mya arenaria
The contamination of the benthic environment poses a threat to long-lived sessile organisms such as clams. The purpose of this study was to investigate metal contamination in tissues and changes in metallothioneins (MT) in respect to its redox status in Mya arenaria clams collected at three polluted sites. The phosphorylation state of MT was also investigated to determine whether this state is changed in clams collected at heavy-metal contaminated site and its involvement in cytoprotective signaling during stress contamination. The results show that clams collected at least one of the three polluted sites presented significantly higher concentrations of silver (Ag), arsenic (As), cobalt (Co), copper (Cu), mercury (Hg), nickel (Ni), tin (Sn) and lead (Pb) in tissues. In the visceral tissue, total MT levels and the reduced, metal-binding form of the protein were significantly induced at the sites. The phosphorylation of MT and mitochondrial activity, as determined by electron transport and cytochrome c oxidase activities, were also significantly reduced at the contaminated sites. Reduced phosphate levels in MT were negatively correlated with total MT levels, suggesting that decreased
phosphorylation was involved in kinase-mediated signaling during cellular stress and could possibly alter the protein’s affinity to confer cytoprotection against heavy metal contamination. These preliminary investigations revealed that the phosphorylation state could change in polluted environment and provide some clues on the modulation of binding affinities during heavy-metal and oxidative stress in clams.