Cadmium, lead and mercury are environmentally persistent toxicants that affect tissues and cellular components or exert an effect on generation of reactive oxygen species causing a decreased level of available antioxidant reserves. Sul furtransferases are enzymes that are widespread in nature. Rhodanese, 3-mercaptopyruvate sulfurtransferase and γ -cystathionase play an important role in the metabolism of L-cysteine. Heavy metal ions can bind to - SH groups of cysteine residues in their active sites and, therefore, decrease the activity of these enzymes and result in changes in the level of sulfane sulfur-containing compounds, products of L-cysteine desulfuration. Changes in the activity of sul furtransferases were investigated in the kidneys, heart, brain, liver and skeletal muscle of Marsh frogs ( Pelophylax ridibundus ) after 10 days of exposure to Pb(NO 3 ) 2 at the concentration of 28 mg/L and CdCl 2 at the concentration of 40 mg or 80 mg/L, and in Xenopus laevies tissues after 7 and 14 days of exposure to HgCl 2 at the concentration of 1.353 mg/L. The investigated heavy metal ions have a tendency to inhibit the activity of sulfurtransferases and decrease the level of glutathione, what can result in oxidative stress and oxidation of cysteine - SH groups to - SOH. This reversible oxidation and reduction of these redox sensitive groups can play a role in defenses against oxidative stress. Based on the presented results, one can surmise that also the expression of the three sulfurtransferases depends on heavy metal ions and/or some parameters of oxidative stress, what can explain the increase of the activity of MPST and CST in the kid ney.
KeywordsSulfurtransferasesHeavy Metal IonsOxidative Stress
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