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The mechanisms of 3,5,3'-L-tri-iodothyronine (T₃) uptake into human erythrocytes were examined. Purified membranes of human erythrocytes were shown to have two classes of T₃-binding sites with one being a high-affinity site (dissociation constant, 59·2±17·8 nmol/l; maximum binding capacity, 344·3 ± 95·5 fmol/µg protein). Furthermore, it was shown that there were two pathways for T₃ uptake in human erythrocytes; one was saturable, stereospecific (T₃»thyroxine > 3,5,3'-_d-tri-iodothyronine), energydependent and dominant at 15 °C; the other was not displaced by unlabelled T₃ and was energyindependent but did not occur by passive diffusion. The former pathway which, it is suggested, is a receptor-mediated transport pathway, was inhibited by monodansylcadaverine, phloretin or oligomycin at 15 or 37 °C, but the latter pathway was not inhibited by these inhibitors. Our results strongly suggest that uptake of T₃ by the energy-independent pathway became predominant over the energy-dependent pathway at 37 °C and accounted for 83% of total T₃ uptake of human erythrocytes.

Journal of Endocrinology (1989) 121, 585–591