Abstract
Copper is an essential trace element required as a co-factor in many enzymatic reactions including: cytochrome oxidase, lysl oxidase, Cu/Zn superoxidase dismutase and ferroxidases. The human copper transporter, hCTR1, is comprised of 190 aa with 3 transmembrane domains and forms a homotrimeric complex with a central pore which transports monovalent Cu. Cu levels and fluxes are low in human cells and we were interested in determining the basis of this phenomenon. Using 64Cu isotopic uptake measurements, cell surface biotinylation and quantification of hCTR1 using purified recombinant hCTR1 protein as a standard we have determined the number of copper ions transported per minute by each hCTR1 trimer.
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