As in other transport epithelia, Ca⁺⁺ plays multiple roles in human placental syncytiotrophoblast, regulating diverse cellular processes and at the same time being transported from mother to fetus. Epithelial Ca⁺⁺ transport and membrane signalling functions rely, among others, on action of transporters and ion channels; functional expression of the latter has been scarcely studied in syncytiotrophoblast owing to difficulties in membrane access with electrophysiological techniques. Thus, our laboratory has worked on the characterization of Ca⁺⁺-permeable ion channels through reconstitution of purified membranes in giant liposomes suitable for patch-clamp. Having formerly detected a non-specific cation channel allowing Ca⁺⁺ permeation in the apical membrane of healthy, term human placentas, we have presently sought to characterize calcium currents present in the basal membrane. Highly purified membranes were obtained through a double protocol of apical and basal membrane isolation, which includes differential centrifugations, basal membrane precipitation with MgCl₂ and band separation through sucrose step gradients. Purified basal membranes were reconstituted through a dehydration-rehydration cycle in 10-50 μm liposomes, which were subjected to electrophysiological recordings. Western blots of apical and basal purified membrane fractions using polyclonal antibodies against three different calcium channels were performed to support our electrophysiological findings. In 5 of 13 experiments using symmetric conditions (140 mM KCl or K gluconate), we detected the presence of channels with high permeability to Ca⁺⁺ (PCa⁺⁺/PK⁺ up to 99.5). We proceeded to work in barium gradients (40 mM BaCl₂ pipette, 0.1 mM BaCl₂ bath), detecting barium-conducing channels in all of the experiments (n = 30). Barium total patch currents were consistently blocked by addition of NiCl₂, Nifedipine or Ruthenium Red to the bath, with approximate EC50 concentrations of 500 μM (n=8), 1 μM (n=5), and 0.5 μM (n=3), respectively. Western blots using polyclonal antibodies against the α subunit of voltage-gated calcium channels, and against TRPV5 and TRPV6 show the presence of these proteins in both basal and apical membrane fractions. These results are consistent with those of other laboratories, which have detected the expression of both TRPV calcium channels (blocked by Ruthenium Red) and L-type voltage-gated calcium channels (blocked by Nifedipine) in human placental tissue and cell lines. These basal membrane calcium channels would not be directly involved in mother-to-fetus directed calcium transport, but could participate in diverse other relevant trophoblast processes, such as exocytosis and calcium transport regulation.