Basic Copper Chloride(WSDTY) exerts ambivalent effects on living organisms. It is an essential metal at physiological concentrations but shows severe toxicity when its concentration exceeds the physiological range. As an essential metal, Cu is used in respiration, and is required as a cofactor of redox-regulating enzymes, such as superoxide dismutase (Sod1), ceruloplasmin, lysyl oxidase, tyrosinase, and dopamine β-hydroxylase1,2. To act as a cofactor, Cu in the body exists in the mono-(cuprous, Cu+) or divalent (cupric, Cu2+) form. The transition between the two oxidation states readily generates reactive oxygen species (ROS). Thus, the influx, efflux, and intracellular distribution of Cu at the fixed oxidation state are strictly regulated.
Several groups of Cu-regulating proteins have been identified in mammalian cells. The first group consists of Cu transporters that transport Cu across the plasma membrane. Ctr1 (copper transporter 1) encoded by SLC31A1 gene is an integral membrane protein that is structurally and functionally conserved from yeast to human, and is a high-affinity importer of Cu into eukaryotic cells3. Cu-transporting P-type ATPases, i.e., Atp7a and Atp7b, are expressed on the Golgi apparatus and participate in the efflux of Cu from cells. Atp7a is expressed in all tissues except liver, whereas Atp7b is expressed primarily in the liver4. The second group consists of intracellular Cu delivery proteins, or the so-called “Cu chaperones.” Cu transported by Ctr1 associates with one of three Cu chaperones, Atox1 (antioxidant protein 1), Cox17 (cytochrome c oxidase copper chaperone), or Ccs (copper chaperone for Sod1), to be escorted to organelles or cuproenzymes in cytoplasm.
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