Prion protein (PrP^C) is a glycoprotein anchored to the outer cell membrane by a glycosylphosphatidyl inositol residue and expressed predominantly by neurons and gliocytes. PrP^C undergoes endocytosis when Cu²⁺ ions interact with its N-terminal entailed octapeptide domains, so it has been proposed as a mediator of cell copper intake processes. To go deep in such hypothesis, steady-state kinetics of copper transport were studied in a neuron-like cell model (B104 neuroblastoma cells) by a fluorimetric method based on a copper-sensitive probe (Phen Green SK). Ion uptake followed a saturable kinetic displaying a Km_app value (0.14 ± 0.02 mM) lower than reported for the well-known high-affinity copper transporter Ctr1. In metal competition assays, Ag didn't evoke any inhibitory effect on the absolute copper intake, as expected if Ctr1 was the main interpreter of transport. Both Cd and Zn heavily inhibited the uptake process, the former being thought to affect PrP^C structure with loss of function, and the latter to compete with copper for the induction of PrP^C-mediated endocytosis. To quantify the contribute of prion-dependent endocytosis to copper intake, cells were subjected to hypertonic shock to disrupt the internalization machinery. In parallel, surface PrP^C was enzymatically removed by PI-phospholipase C treatment. In both cases, ion transport was similarly reduced, being this a proof of the exclusive involvement of PrP^C in the endocytotic cell copper uptake.