Metallothioneins (MTs), a superfamily of cysteine-rich proteins, perform multiple functions, such as maintaining homeostasis of essential metals, detoxification of toxic metals and scavenging of oxyradicals.
Manganese enzymes are particularly essential in detoxification of superoxide free radicals in organisms that must deal with elemental oxygen.
By searching miRbase, we found that MnSOD, Gpx2 and TrxR2, three important mitochondrial antioxidant proteins that are essential for detoxification of O2.− and H2O2, are potential targets of miR-17*.
In conclusion, our study shows that the ARF-GAP Age3p is required for hyphal growth which is an important virulence factor of C. albicans and essential for detoxification of azole drugs which are routinely used for antifungal therapy.
Mitochondrial antioxidant enzymes, including manganese superoxide dismutase (MnSOD), glutathione-dependent peroxidase (GPX) and thioredoxin- dependent peroxidase (TrxR2), comprise a primary defense system in mitochondria and are essential for detoxification against ROS [10] [12].
The findings reported here represent the first demonstration of the function of coelomocytes of C. elegans: these cell types are essential for detoxification of heavy metals, but not of ROS, which are by products of multiple stresses as well as heavy metal toxicity.
GSH is essential for detoxification of APAP metabolites and NAPQI that cause hepatic necroinflammation.
In addition, the class II genes were up-regulated under excess Zn, indicating that they may be essential for detoxification of excessive metal ions other than Fe.
When Saccharomyces cerevisiae is exposed to Cd2+ most of the sulfur assimilated by the cells is converted into glutathione, a thiol-metabolite essential for detoxification.
In each of these species, single enzymes were identified as essential for detoxification or sequestration of glucosinolate breakdown products that appear to allow for minimal contact with isothiocyanates (Muller et al. 2010).
