Copper/Zinc Superoxide Dismutase in Human Skin: Current Knowledge

Abstract

Superoxide dismutase is widespread in the human body, including skin and its appendages. Here, we focus on human skin copper/zinc superoxide dismutase, the enzyme that protects skin and its appendages against reactive oxygen species. Human skin copper/zinc superoxide dismutase resides in the cytoplasm of keratinocytes, where up to 90% of cellular reactive oxygen species is produced. Factors other than cell type, such as gender, age and diseased state influence its location in skin tissues. We review current knowledge of skin copper/zinc superoxide dismutase including recent studies in an attempt to contribute to solving the question of its remaining unexplained functions. The research described here may be applicable to pathologies associated with oxidative stress. However, recent studies on copper/zinc superoxide dismutase in yeast reveal that its predominant function may be in signaling pathways rather than in scavenging superoxide ions. If confirmed in the skin, novel approaches might be developed to unravel the enzyme's remaining mysteries.

Functionalized Silica Star-Shaped Nanoparticles and Human Mesenchymal Stem Cells: An In Vitro Model

“…We monitored the presence of oxidative stress by evaluating the SOD1 expression [ 66 , 67 ]. Compared to the related controls, no significant statistical differences were detected in the SOD1 expression in hBM-MSCs ( Figure 4 b,c) and hASCs ( Figure 4 e,f) on s-MSN, s-MSN-NH 2 , and s-MSN-Au at each time-point analyzed, as demonstrated by the densitometric analyses of Western blotting ( Figure 4 b,c,e,f).…”

“…We monitored the presence of oxidative stress by evaluating the SOD1 expression [66,67]. Compared to the related controls, no significant statistical differences were detected in the SOD1 expression in hBM-MSCs (Figure 4b (Figure 4b,c,e,f).…”

“…We monitored the presence of oxidative stress by evaluating the SOD1 expression [66,67]. Compared to the related controls, no significant statistical differences were detected in the SOD1 expression in hBM-MSCs (Figure 4b We evaluated the presence of storage material by using vital staining with Acridine Orange, a lysotropic dye that, in physiological conditions, in a pH-dependent manner, marks in green the cytoplasm and nucleic acid and in orange-red the acidic compartments (e.g., lysosomes, autophagolysosomes) [68,69].…”

Regulation of Mitochondrial Dynamics in Parkinson’s Disease—Is 2-Methoxyestradiol a Missing Piece?

“…They are responsible for the dismutation of O 2 into H 2 O 2 [94]. Depending on the metal atom present in the active sites, SODs can be divided into four separate groups: Copper-Zinc-SOD (Cu, Zn-SOD) [95], Iron SOD (Fe-SOD) [96], Manganese SOD (Mn-SOD) [97], and Nickel SOD [98]. CuZnSOD, also known as SOD1, is a homodimer predominantly localized in the cytoplasm, but only slight quantities have been detected in the intermembrane space of mitochondria [99].…”

“…CuZnSOD, also known as SOD1, is a homodimer predominantly localized in the cytoplasm, but only slight quantities have been detected in the intermembrane space of mitochondria [99]. Human skin Cu, Zn-SOD is an enzyme that protects skin against ROS and is present in the cytoplasm of keratinocytes, where even 90% of cellular ROS is formed [95]. Fe-SOD is an antioxidant of bacterial origin present for instance in E. coli [96].…”